Microchim Acta (2007)
DOI 10.1007/s00604-007-0834-8
Printed in The Netherlands
Review
Amperometric lactate biosensors and their applicationin (sports) medicine, for life quality and wellbeing
Nadia Nikolaus, Beate Strehlitz
UFZ, Helmholtz Centre for Environmental Research – UFZ, Environmental and Biotechnology Centre (UBZ), Leipzig, Germany
Received 16 May 2007; Accepted 28 June 2007; Published online 7 September 2007
# Springer-Verlag 2007
Abstract. The article reviews the use of electro-
chemical biosensors for detecting lactate, a key me-
tabolite of the anaerobic glycolytic pathway. This
compound plays an important role in (sports) medi-
cine, in the nutritional sector, in food quality control
and touches environmental concerns. Amperometric
biosensors offer a sensitive and selective means to
monitor organic analytes like lactate. A detailed study
on different aspects of amperometric lactate biosensor
preparation is described: the main configuration as-
pects are compiled regarding electrode materials,
biorecognition elements, immobilization methods,
mediators and cofactors as well as fields of application.
Comparative studies are conducted correlating differ-
ent configuration aspects and performance of the
resulting biosensors. This review contains 214 refer-
ences from the years 1974 to 2007.
Keywords: Biosensor; amperometry; lactic acid; enzyme sensor
Lactate is the key metabolite of the anaerobic glyco-
lytic pathway. Lactic acid exists as L-(þ) and D-(�)
enantiomers. While L-(þ)-lactate is the normal inter-
mediate in mammalian metabolism, the D-(�) enan-
tiomer is usually produced by microorganisms, algae,
and plants and is of limited utilization in humans [1].
A daily intake of less than 100 mg kg�1 D-lactate is
therefore recommended by the World Health Organi-
zation (WHO) [2].
Determination of L-lactate concentration in blood
is essential for the diagnosis of patient conditions in
intensive care and during surgery. An elevated lactate
level in blood is a major indicator of ischemic condi-
tions of the respective tissue. This ischemic situation
can be caused by all types of shock, suffocation and
respiratory insufficiency, carbon monoxide or cyanide
intoxication, heart failure, etc. [3, 4]. Another reason
for an altered lactate level is a disturbed lactate me-
tabolism which may be caused by diabetes or absorp-
tive abnormalities of short-chain fatty acids in the
colon [5].
In other fields of medicine, lactate plays an im-
portant role as well. In sports medicine (training of
athletes or racing animals) or space medicine, blood
lactate levels during exercise are an indicator for
training status and fitness [6–8]. In dental care, D-
lactate produced by carbohydrate-fermenting plaque
has proven to be important in the formation of dental
cavities [2].
However, the importance of lactate is not limited to
the medical sector. D- and L-lactic acid are found in
many foods and beverages. Produced naturally by lac-
tic acid bacteria, D- and L-lactic acid can be found in
many fermented milk products such as yoghurt, but-
Correspondence: Beate Strehlitz, UFZ, Helmholtz Centre for
Environmental Research – UFZ, Environmental and Biotechnology
Centre (UBZ), Permoserstrasse 15, D-04318 Leipzig, Germany
e-mail: [email protected]
termilk, and cheese, in fermented vegetables, like
sauerkraut or the Korean kimchi, in cured meats and
fish. L-lactic acid is added to foods and beverages
(E270) where a tart flavor is desired, and is widely
used as a non-volatile acidulant. However, there is
undesirable occurrence of lactate in foodstuff. In the
egg industry, an increased occurrence of L-lactate is
an indicator of spoilage by contamination or incu-
bation. Similarly, D-lactate acts as an indicator for
contamination of vacuum-packed chilled meat. The
quality of milk, beer, fruit and vegetable juices can
be assured by measurement of the D- and L-lactic acid
content. A contamination of fruit juices with lactic
acid producing bacteria often remains unnoticed for
a longer time, allowing the bacteria to spread and
infect huge volumes of juice. The alteration of the
organoleptic properties of the juice does not permit
a further consumption. In the wine industry, the course
of malolactic fermentation is monitored by following
the falling level of L-malic acid, and the increasing
level of L-lactic acid. This conversion leads to a de-
acidification and softening of the wine’s taste. The
production of D-lactic acid, however, can indicate
wine spoilage.
In the chemical industry, both D- and L-lactic acid
are raw materials in the production of compounds
such as polylactides and other biologically degradable
polymers; applications also exist for these acids in
cosmetics and pharmaceuticals [9]. Biotechnogical
production of lactic acid therefore is an economical
necessity. In the 1990s, 50% of the existing needs
were covered by lactic acid produced in fermenta-
tion [2].
Environmental concerns are touched when silage
effluent containing large amounts of lactate and other
organic substances is released into the water body.
Silage effluent has the potential to cause serious water
pollution, lowering the pH and creating an immense
Biochemical Oxygen Demand since it contains a high
concentration of organic compounds [10].
As can be seen from the examples mentioned
above, lactate is an important metabolite and it is of
increased interest to detect or monitor the existence or
production of L- and D-lactic acid in the most differ-
ent of media.
Among the various conventional analytical methods
available for the determination of this analyte, colori-
metric tests and chromatographic analysis are most
important. However, the majority of these methods
are complex, laborious and slow, complicated by in-
tensive sample pre-treatment and reagent preparation
[11, 12].
Therefore, the development of alternative methods
for lactic acid detection possessing the advantages of
being simple, direct, and real-time with no need of
sample preparation (except perhaps for dilution of
the sample), combining rapid response with high spe-
cificity and being inexpensive at the same time is still
very interesting [12–14].
One alternative to conventional methods for moni-
toring lactate is the use of (amperometric) biosensors,
which provide rapid, simple and direct measurements
[12]. As part of a research project with regards to
the determination of lactate in beverages by use of
amperometric biosensors, the relevant literature was
surveyed. The search was focused on the use of am-
perometric biosensors for lactate in the fields of
(sports) medicine, life quality, and wellbeing. There-
fore, the application of lactate biosensors in intensive
care will not be covered in this literature survey.
For the use of lactate biosensors in critical care, see
Ref. [15] (reviewing whole blood analyzers in cardiac
and critical care for a range of analytes, amongst
others lactate), [16] (biosensors for in vivo moni-
toring), or [17] (comparison of different biosensor
devices, influence of hematocrit, storage time, and
temperature of whole blood and plasma as well as
the use of anticoagulants on lactate determination).
In order to determine for this review whether the
amperometric lactate biosensor in question is used in
critical care applications or not, discriminating factors
were the need of blood sample preparation, like
microdialysis or centrifugation (blood plasma or se-
rum) or measurements in body fluids or tissues not
attainable to a non-medical (like spinal or cerebral
fluids, myocardium). If the amperometric biosensor
is used to detect lactate levels in readily available
body fluids (like sweat, saliva or whole blood), the
application in question is counted as medical, but
not critical care and therefore is included in this re-
view.
Amperometric biosensors: definition
As per definition of IUPAC, a biosensor is an integrat-
ed receptor-transducer device, which is capable of
providing selective quantitative or semi-quantitative
analytical information using a biological recognition
element. The receptor acts upon a biochemical mech-
anism, while the transducer is considered to be a
N. Nikolaus, B. Strehlitz
chemically modified electrode (CME) of electronic
conducting, semiconducting or ionic conducting ma-
terial and is in direct contact with the biochemical
receptor component [18].
Amperometric transduction is based on the mea-
surement of the current resulting from the electro-
chemical oxidation or reduction of an electroactive
species. The resulting current is directly correlated
to the bulk concentration of the electroactive species
or its production or consumption rate within the adja-
cent biocatalytic layer. Because of this mode of oper-
ation, amperometric sensors alter the concentration of
the analyte in their closest vicinity, that is within the
diffusion layer. So, knowledge of the rate-limiting
step, i.e. mass transport rate or analyte consumption
reaction rate, leads to a better understanding of their
operational characteristics [18]. For example, linear
dynamic ranges may be extended if the sensor re-
sponse is not controlled by the enzyme kinetics
but by other rate-limiting steps like the use of two
competing enzymes [19], or the substrate diffusion
through a covering membrane [18, 20–23].
In the IUPAC definition, the term biosensor is re-
stricted to a system, where the biological recognition
element is retained in direct spatial contact with the
transduction element [18]. Therefore, even if sensor
configurations that use enzyme solutions contained in
compartments near the transducer are regarded for
this review, such configurations with a lactate con-
suming enzyme reactor upstream of the sensor are
excluded.
As a means to increase the sensitivity and selectiv-
ity of a biosensor, it is possible to use a mediator
which reacts sufficiently rapidly with the biocatalyst
and is easily detected by the transducer. The IUPAC
definition declares that the mediator should be immo-
bilized to avoid additional processing steps such as
reagent addition. In order to form a steady-state diffu-
sion layer of some mm in thickness and thereby en-
abling fast electron transfer, the mediator should be
fixed at the electrode in such a way that immediate
dissolution from the electrode surface is possible
[24, 25]. On the other hand, in order to provide high
operational stability, the mediator should be suffi-
ciently fixed at the electrode. These rather contradic-
tory demands are not easy to fulfill leaving mediator
immobilization to be a technological challenge. A way
around this dilemma often described in literature
exists in adding the mediator to the bulk solution. In
such a configuration, the mediator is present in suffi-
cient amount and proximity to fulfill its task, but does
not meet the requirements according to IUPAC.
However, in order to possess a broad enough data
pool for this review, biosensors with immobilized
redox mediators as well as biosensors using redox
mediators in solution are included. With this under-
standing of the term ‘amperometric biosensor’, there
remain 186 articles which are considered for this re-
view. The deadline for articles to be included in this
consideration was January the 1st, 2007.
Construction of amperometric biosensors
Amperometric biosensors can be classified accord-
ing to their composition and fields of application.
Composition criteria include electrode material to be
chemically modified, biological recognition element
employed for the chemical modification, manner of
immobilization of these biological recognition ele-
ments, possible mediators used. The 186 relevant arti-
cles were scanned according to these criteria. The
obtained results are presented in pie charts. Numbers
bigger than 186 derive from multiple specifications
described in one article.
In the following, the composition criteria men-
tioned above and fields of application are described
in detail.
Electrode material
Amperometric measurements are usually performed
by maintaining a constant potential at a working elec-
trode or an array of working electrodes consisting
of metal or carbon based material. This potential is
maintained constant with respect to a reference elec-
trode (in the applications from the surveyed articles
mostly Ag=AgCl or saturated calomel electrodes).
If currents are low (10�9–10�6 A), the reference
electrode may also serve as auxiliary electrode.
Otherwise, a three-electrode set-up has to be used.
Working electrodes for amperometric biosensors can
consist of different materials. It seems that there are
some combinations of electrode material and immo-
bilized enzyme that are more favorable than others.
For example, Blaedel and Engstrom found 1980
that with dehydrogenases, platinum working elec-
trodes are less prone to fouling than glassy carbon
electrodes [26].
Response current densities obtained for an enzyme
modified carbon paste electrode, however, are lower
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
than for their solid counterparts. Additionally, nonco-
valently bound compounds that are soluble in aqueous
media may leach out from the paste into the surround-
ing solution and therefore corrupt the performance of
the sensor [27]. In order to prevent this effect and to
increase the operational stability of both carbon paste
as well as solid electrodes, membranes covering the
enzyme electrode surface can be beneficial [28].
The material of the working electrode is either met-
al or carbon based [18]. In the 196 entries found in
184 analyzed articles concerning amperometric lac-
tate biosensors, the numbers of metal and carbon
based electrodes are nearly equal (Fig. 1). 97 out of
196 (49.5%) entries are related to metal based work-
ing electrodes. Most of the described metal based
working electrodes are made of Pt (80.4%), as also
the Clark-type Oxygen electrode contains a Pt work-
ing electrode. 16.5% of the mentioned metal based
working electrodes are made of gold. Then there are
some special cases like metal oxide electrodes or elec-
trodes made of platinized polypyrrole. On the other
hand, carbon based working electrodes (total: 99 out
of 196, 50.5%) can be found in the form of carbon
paste electrodes (39.4% of all carbon based working
electrodes), glassy carbon electrodes (29.3%), screen
printed electrodes with graphite based printing ink
(18.2%), or graphite electrodes (13.1%).
After regarding possible electrode materials, anoth-
er important composition criterion, the biorecognition
element, is now considered.
Biorecognition element
As biological recognition element for amperometric
lactate biosensors several enzymes are used (see des-
cription below), as well as cell fractions and even whole
bacterial or yeast cells. The following lactate convert-
ing enzymes are used in lactate biosensor applications.
They catalyze the reactions described below [29].
Lactate oxidase (LOD, former EC 1.1.3.2, now EC
1.13.12.4):
L-lactate þ O2 þ H2O ! pyruvate þ H2O2 ð1ÞL-lactate dehydrogenase (cytochrome) (FCb,
EC 1.1.2.3):
L-lactate þ 2 ferricytochrome c
! pyruvate þ 2 ferrocytochrome c ð2Þ
L-lactate dehydrogenase (L-LDH, EC 1.1.1.27):
L-lactate þ NADþ ! pyruvate þ NADH þ Hþ ð3ÞD-lactate dehydrogenase (D-LDH, EC 1.1.1.28):
D-lactate þ NADþ ! pyruvate þ NADH þ Hþ;
ð4Þwith NADþ and NADH being the oxidized and re-
duced forms of nicotinamide dinucleotide.
For the composition of lactate biosensors, these en-
zymes are utilized in mono-enzyme or in multi-en-
zyme configuration with each other or in combination
with further enzymes. Regarding mono-enzyme con-
figurations, lactate oxidase (LOD) is the enzyme most-
ly used in amperometric biosensor applications (see
Fig. 2). The species produced in the reaction (1)
which is detected at the electrode is H2O2. LOD has
the advantage of being independent of immobilized or
added cofactors for the reaction to take place. Only
oxygen is necessary. One disadvantage is that a high
overpotential is needed for the detection of H2O2 at
noble metal electrodes. This causes interferences by
easily oxidizable species like ascorbate etc. [30].
When lactate dehydrogenase (LDH, EC 1.1.1.27
and 1.1.1.28) is used as the mono-enzyme for lactate
detection with amperometric biosensors, an additional
co-factor like NADþ is necessary. In the reaction with
LDH (cf. reactions (3) and (4)), NADH is the com-
pound to be detected at the electrode. The need for a
co-factor implies an additional immobilization step
(which is challenging), or the cofactor has to be added
to the solution. As in biosensors based on LOD, high
applied potentials are required for the direct oxidation
of the enzymatically produced NADH at solid electro-
Fig. 1. Material used for the transducer of amperometric lactate
biosensors. Percentages are given of the total of 196 entries in 184
articles. A Platinum; B Clark-type (Pt); C platinized polypyrrole;
D gold; E metal oxide; F carbon paste; G graphite; H screen
printing ink; I glassy carbon
N. Nikolaus, B. Strehlitz
des which again causes interferences from other oxi-
dizable species. Moreover, the reaction takes place
through radical intermediates giving rise to electrode
fouling and lack of stability [31, 32]. Additionally,
biosensors based on LDH were found to be less sen-
sitive for the determination of L-lactate in the micro-
molar range [33]. The reason is the rather unfavorable
enzyme reaction equilibrium of LDH catalyzed reac-
tions due to the low oxidizing power of NADþ (or
NADPþ, nicotinamide dinucleotide phosphate) result-
ing from the low formal potential of the NAD(P)þ=NAD(P)H redox couple, �560 mV vs. SCE at pH 7.0
[2]. As a consequence, only a relatively small amount
of product is available, leading to low currents for the
electrochemical detection and therefore giving lower
sensitivities and signal to noise ratios.
One advantage of using LDH in amperometric bio-
sensors, however, is that oxygen is not involved and
therefore the sensor is suited for measurements in
oxygen depleted surroundings. For the determination
of D-lactate in biosensors, D-LDH is the only existing
enzyme.
In contrast to the lactate dehydrogenase (EC
1.1.1.27 and EC 1.1.1.28) described above, L-lactate
dehydrogenase (cytochrome) (EC 1.1.2.3) is indepen-
dent of external co-factors. This offers an advantage
during immobilization. Another advantage concerning
this enzyme consists in its independency of oxygen.
Oxygen is not a competitive acceptor for L-lactate
dehydrogenase (cytochrome) and therefore does not
interfere when this receptor is used [34]. As a result,
oxygen-independent systems with mediated electron
transfer are possible with this enzyme [35].
Nevertheless, using L-lactate dehydrogenase (cyto-
chrome) suffers from some disadvantages as well.
D-lactate is a competitive inhibitor of the catalyzed
lactate oxidation, and pyruvate is known to be a
competitive inhibitor for the oxidized enzyme at low
concentrations [36]. Then, L-lactate dehydrogenase
(cytochrome) from yeast is pH sensitive, i.e. it is in-
active in acidic media. It therefore requires a good
buffering system for linear response. Also the enzyme
is readily saturated by lactate (Kmax¼ 1.2 mmol L�1
[37]). Since the normal blood lactate concentration
lies in the range of 1 mmol L�1 L-lactate, a dilution
step is necessary for determinations in the (sports) med-
ical sector, where more than ten times higher blood
lactate values can be reached.
Whole cell based sensors suffer not only from a
restricted reproducibility of the sensor preparation
but also from poor selectivity towards lactate because
of additional oxidoreductase activities that are direct-
ed to other substances than lactate possibly present in
complex probes [30].
The use of multi-enzyme configurations can hold
many advantages like recycling of the substrate of
the reaction leading to signal amplification. For exam-
ple, the enzymes LDH and LOD can be coupled [38],
or LDH and FCb [39]. This provides an amplification
factor of 2–250 and 8–40, respectively. Further ad-
vantages can be the avoidance of electrode fouling
or the elimination of interferences. One example for
interference elimination is the conversion of the inter-
ferant ascorbate into an electrochemically inert form
by additional use of ascorbate oxidase as reported in
[40]. In order to reduce electrode fouling for example
caused by NADH when reacting directly at Pt electro-
des, this cofactor can be recycled by an additional
enzyme, e.g. by diaphorase or NADH oxidase (EC
1.6.99), or by flavin reductase, each of them coupled
with LDH [31, 41, 42]. The problem of the unfavor-
able reaction equilibrium concerning reactions with
Fig. 2. Biological recognition element for amperometric lactate
biosensors. Percentages are given of the total of 194 entries in
184 articles. A Lactate oxidase (LOD) (former EC 1.1.3.2, now
1.13.12.4); B L- and D-lactate dehydrogenase (LDH) (EC 1.1.27
and EC 1.1.28); C L-lactate dehydrogenase (cytochrome), LDH
(cytochrome) (EC 1.1.2.3); D LDH=other enzymes: alanine trans-
aminase (EC 2.6.1.2), diaphorase (EC 1.8.1.4 or EC 1.6.99.-),
FMN (flavin mononucleotide) reductase (EC 1.5.1.29), NADH
dehydrogenase (EC 1.6.99.-), pyruvate oxidase (EC 1.2.3.3), salic-
ylate 1-monooxygenase (EC 1.14.13.1); E LDH=horseradish per-
oxidase, HRP (EC 1.11.1.7); F LDH=LOD; G LDH=LOD=HRP;
H whole cells and cell fractions from Acetobacter pasteurianus
cells, Alcaligenes eutrophus cells, Paracoccus denitrificans cells,
Hansenula anomala cells, cell fractions: membrane vesicles of
Paracoccus denitrificans, Escherichia coli respiratory chain
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
LDH can be solved by coupling a second enzyme
reaction to the first. This second enzyme reaction uses
one product of the first enzyme reaction (pyruvate,
converted from lactate by LDH) as substrate and so
the first reaction can be forced to its product side.
Examples are the transformation of pyruvate to glu-
tamate by glutamic-pyruvic transaminase [43] or of
pyruvate to L-alanine by alanine aminotransferase
(EC 2.6.1.2) [44].
The use of an oxidase=peroxidase multi-enzyme
system makes it possible to work at more negative
potentials in order to avoid electroactive interfer-
ences [27].
However, it has to be considered, whether the addi-
tional effort of immobilizing a second (or even third)
enzyme is worthwhile in terms of higher sensitivity
and selectivity (see Section ‘‘Set-up and performance’’).
Renneberg et al. [45] describe low stability and a lack
of reproducibility in a bienzyme system [45].
In Fig. 2, the distribution of the enzymes used in
amperometric lactate biosensors is shown in a pie
chart, with 194 entries found in 184 articles. As far
as mono-enzyme configurations are concerned, lactate
oxidase is the enzyme most widely used: More than
half of the correspondent entries (51.0%, i.e. 99
entries) describe applications with LOD as the immo-
bilized mono-enzyme, in contrast to 34 entries of
LDH used as sole enzyme (17.5%). Summing up all
entries for LOD and LDH, in mono- as well as multi-
enzyme configurations, the utilization of LOD is
slightly preferred (111 entries compared to 89 for
LDH). Regarding multi-enzyme configurations, the
combination of LDH with other enzymes like flavin
reductase, glutamic-pyruvic transaminase, NADH ox-
idase, pyruvate oxidase or salicylate hydroxylase is
mentioned. For the combination of LOD with other
enzymes, options are more limited. LOD=LDH as well
as the oxidase=peroxidase system are possible enzyme
combinations. One single article describes a three-
enzyme-configuration with the coupling of LOD,
LDH, and salicylate 1-monooxygenase. Whole bacte-
rial or yeast cells like Acetobacter pasteurianus,
Alcaligenes eutrophus, Paracoccus denitrificans or
Hansenula anomala cells or cell fractions are utilized
only to a minor degree (6 entries out of 194 in 184
articles, i.e. 3.1%).
After describing possible enzymes and other bio-
recognition elements for the composition of ampero-
metric lactate biosensors, the following section is
dedicated to different immobilization methods which
can be used to fix these biorecognition elements at the
electrode.
Immobilization of enzyme(s)
The key factor in developing a reliable biosensor is
the immobilization of the enzyme at the transducer.
The performance of an enzyme electrode in terms of
lifetime, linear range, sensitivity, selectivity, response
time, stability and susceptibility to interfering agents
depends strongly on the method used to immobilize
the enzyme [46].
In [47], the dependency of certain biosensor fea-
tures on the immobilization technique utilized is em-
phasized. Long-term stability of lactate biosensors
in vitro and operational stability in biological media
are compared. An apparent instability after short-time
usage in biological media led to the conclusion, that
immobilization procedures have to be designed par-
ticularly with regard to stability in exactly the com-
plex surrounding in which the biosensor is planned to
be utilized.
According to [18], there are several possible proce-
dures for the immobilization of enzymes at the trans-
ducer. Firstly, a solution of enzyme can be entrapped
behind an analyte permeable membrane. Then there is
the entrapment of biological receptors within a poly-
meric matrix or the entrapment within self-assembled
Fig. 3. Immobilization method used for the attachment of the
biorecognition element to the transducer. Percentages are given
of the total of 197 entries in 184 articles. A Containment; B en-
trapment; C covalent immobilization using glutaraldehyde; D co-
valent immobilization of the biological recognition element with
the aid of agents other than glutaraldehyde; E avidin–biotin inter-
action; F concanavalin A–mannose interaction; G biological rec-
ognition element incorporated in carbon paste, graphite, or screen
printing ink; H physisorption; I non-covalent attachment (non-spe-
cific adsorption) followed by a coverage with membrane layer(s)
N. Nikolaus, B. Strehlitz
monolayers or bilayer lipid membranes, respectively.
Another possibility is the covalent bonding of recep-
tors on membranes or surfaces activated by means of
bifuncional groups or spacers, such as glutaraldehyde,
carbodiimide, silanization, avidin–biotin interaction
etc. Finally, bulk modification of the entire electrode
material like enzyme-modified carbon paste or graph-
ite epoxy resin is mentioned.
In the literature studied for this review (cf. Fig. 3),
not all of these immobilization procedures were found
for the preparation of amperometric lactate biosen-
sors. There was no example for entrapping of enzyme
within self-assembled monolayers or bilayer lipid
membranes. Instead, other ways of immobilization
were described that are not mentioned in the IUPAC
recommendations.
Figure 3 displays the distribution of the immobili-
zation techniques used for the fabrication of ampero-
metric biosensors for lactate.
A slight majority of methods can be seen where the
biorecognition element is attached covalently to the
material of the working electrode.
56.3% of the total of 197 entries fall into this cate-
gory. The procedure mostly used here is the covalent
bonding by means of glutaraldehyde. However, there
also are other coupling reagents for covalent attach-
ment, like carbodiimide, succinimidyl ester, activated
aldehyde groups at membranes (UltraBindTM), tri-iso-
cyanate, microbial transglutaminase, etc. Additional-
ly, there is the method of entrapment of the biological
recognition element in a polymer matrix. For this pur-
pose, the enzyme(s) or whole cells are either mixed
with sol–gel precursors or with monomers which are
cross-linked either via electropolymerization, photo-
cross-linking, cross-linking using gamma irradiation,
isocyanate and other agents, or the enzymes are
entrapped using electrostatic interactions.
In two cases, Avidin–Biotin interaction and in one
case Concanavalin A mannose interaction is described
as the immobilization method which sum up to 1.5%
of all described methods.
In 42.1% of the total of 197 entries, non-covalent
attachment is used as the immobilization technique.
The respective methods used are, for example, physi-
sorption, i.e. a non-specific adsorption without cova-
lent attachment, physisorption followed by coverage
with a membrane, containment of enzyme solution
behind membranes, or bulk modification of the elec-
trode material (carbon paste, screenprinting ink, or
graphite) with the bioreceptor.
Mediators and cofactors
As mentioned in the section about the definition of
amperometric biosensors, sensitivity and selectivity
of a biosensor can be considerably enhanced by using
mediators. Fultz and Durst [48] report in their re-
view that the irreversible electrochemical behavior
of many biological species is due to a very slow het-
erogeneous electron transfer at electrodes. This leads
to a severe electrode fouling by adsorption of the bio-
component on the electrode or insulation of the elec-
troactive center in the molecule by the surrounding
protein matrix. One possible solution to this problem
would be the introduction of a mediator, i.e. an elec-
troactive species which acts as an electron shuttle
and therefore forms a redox coupling between the
electrode and the redox center in the biological
compound.
But not only electrode fouling can be prevented
using mediators. For instance, the very slow rates of
electron transfer to electrode surfaces as is the case for
many redox enzymes can be enhanced by the use of
mediators [49].
Another advantage of mediators is the reduction of
overpotential. Easily electro-oxidizable species can
interfere in the detection due to the overvoltage nec-
essary to directly oxidize the NADH or the H2O2 pro-
duced by the enzyme reaction [50].
In order to find the right mediator, it is important,
according to [48] to consider the formal potential of
the involved compounds: the formal potential of the
mediator should be close to that of the biocomponent
being studied.
For example, for the use of LOD in an amperomet-
ric biosensor, the oxidation potential of the chosen
mediator should be higher than the reduction potential
of flavin mononucleotide, which is a redox center of
LOD. Generally, the mediator which shows the high-
est redox potential would be expected to have the
highest electron-transfer rate from LOD to mediator.
However, it is important that the redox potential is not
too high. This again would lead to interference by
electron transfer from co-existent compounds such
as ascorbic acid to the mediator [51].
Another problem lies in the fact that the stability of
the biological recognition element i.e. the enzyme,
depends on the environment surrounding the biore-
ceptor. Stability is increased in more natural environ-
ments. However, frequently used mediators are highly
toxic compounds. For a more enzyme-friendly sur-
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
rounding, it is proposed to use polymeric FAD as
mediator in lactate detection which is, in addition,
free of danger to the environment [52].
Once the right mediator for a given set-up and ap-
plication is found (preferably as the result of an opti-
mization process), the next step is to immobilize the
mediator at the sensor surface or within the bulk sen-
sor material in order to obtain reagentless and at the
same time stable biosensors.
However, an immobilization of the mediator can
bear risks for the overall performance of the biosen-
sor. For example, experiments reported by Garjonyte
et al. [53] where whole yeast cells were incorporated
in carbon paste showed differences in the operational
and storage stabilities of a carbon paste lactate sensor
depending on whether the mediator (in this case phen-
azine methosulfate, PMS) was adsorbed at the sensor
surface or in solution. In the first case, lifetime was
reduced. When mediator was added to the measuring
solution, however, the exhausted sensor regained ac-
tivity. This shows that in this case the immobilized
mediator (and not the biological recognition element)
was the limiting factor for the lifetime of the biosen-
sor [53].
In order to give a survey of redox mediators and
cofactors used in amperometric biosensors for lactate,
in Fig. 4, their distribution is displayed in a pie chart.
Chemical structures and redox potentials of many
of the redox mediators mentioned below can be found
in the following reviews: Refs. [48] and [54].
Mediators used for amperometric biosensors for
lactate can be divided into three categories: (transi-
tion) metal compounds or complexes, conducting
polymers, and organic dyes.
(Transition) metal compounds include metallo-
organic compounds like ferrocene and its derivatives,
e.g. dimethylferrocene, ferrocene carboxylic acid,
hydroxymethylferrocene, 1,10-dimethylaminomethyl-
ferrocene, and poly(vinylferrocenium), transition met-
al complexes like Prussian blue (Fe7(CN)18(H2O)x
where 14 � x� 16), ferrocyanide ([FeCN6]4�), hexa-
cyanoferrate(III) ([FeCN6]3�), and entrapped ferri-
cyanide ions ([FeCN6]3�), Osmium complexes in
different redox polymers, Cobalt phthalocyanine, Tris
(1,10-phenanthroline) cobalt(III) perchlorate trihy-
drate, and cobalt-tetramethoxyphenyloporphyrin. In
the broader sense, Rhodium dispersed in carbon can
also be counted among this category, which sums up
to 31.9% of all mediators mentioned in the articles (58
of 182 entries).
The category of organic dyes is nearly as large as
that of the (transition) metal compounds and amounts
to 24.7% (45 of 182 entries). Among these organic
dyes are quinone derivatives, like juglone copolymers,
2-methyl-1,4-naphthoquinone, pyrroloquinoline qui-
none, benzoquinone, and tetracyanoquinodimethane
(TCNQ). Furthermore, there are tetrathiafulvalene
(TTF) and salts thereof, as well as indophenol deri-
vatives, like dichlorophenolindophenol. Also included
are phenazines like phenazine ethosulfate (PES),
phenazine methosulfate (PMS), salts and complexes
thereof, phenoxazines like Meldola blue and salts
thereof, and Nile blue derivatives, as well as pheno-
thiazines like methylene blue and poly(methylene
blue), methylene green, and toluidine blue-O.
The third category, that of conducting polymers is
of minor importance for the construction of ampero-
metric biosensors for lactate. Only 8.2% (15 entries
out of 182) of the reported mediators are conducting
polymers like poly(aniline), poly(aniline)–poly(acry-
late), poly(aniline)–poly(vinyl sulfonate), poly(ethyl-
eneimine), poly(pyrrole), poly(pyrrole)–poly(vinyl
sulfonate), and poly(vinylpyrrolidone).
The use of cofactors is described in 64 cases of the
184 studied articles. This corresponds to 68 entries for
the use of cofactor dependent LDH. In general, a co-
factor is an organic molecule or ion (usually a metal
Fig. 4. Mediators and cofactors used in amperometric biosensors
for lactate (in solution or attached to the sensor). Percentages are
given of the total of 182 entries in 184 articles. A Metallo-organic
compounds; B transition metal complexes; C rhodinized carbon;
D conducting polymers; E quinones; F tetrathiafulvalene (TTF)
and salts thereof; G indophenols; H phenazines; I phenoxazines;
J phenothiazines; K cofactors
N. Nikolaus, B. Strehlitz
ion) that is required by an enzyme for its activity [55].
It may be attached either loosely (coenzyme) or tight-
ly (prosthetic group). Examples for cofactors are
NADþ=NADH, FADþ, ferricytochrome c, and pyrro-
loquinoline quinone (PQQ).
Fields of application
In the late 1990s, it was stated that in spite of an
increased research activity concerning enzymatic bio-
sensor preparation, their commercial application and
their use in industry as a means for quality control is
limited. This was attributed to the fact that manu-
facturing reproducible electrodes on a large scale,
with long-time operational and storage stability and
the possibility of sterilization had not yet been
achieved to that date [56, 57].
While Kriz et al. [58] see a growing need for
the development of analytical instruments for quality
monitoring for the food industry, the situation men-
tioned above has not changed much: Of 69 articles
from the years 1998 to 2006 describing amperometric
biosensors for lactate (including reports of measure-
ments in critical care situations), more than half (37
articles, i.e. 54%) state measurements in buffer solu-
tion only, and not in complex media. This is possibly
due to the fact that the stability of the sensor depends
on its application (buffer or biological media), as it
was already stated in the chapter concerning the im-
mobilization of the biorecognition element [47].
In Fig. 5, fields of application of amperometric
lactate biosensors are compiled with regards to the
whole time range from the first appearance of those
biosensors in literature up to now. 50.5% of the total
number of entries (99 of 196 entries) describe the use
of amperometric lactate biosensors in model solutions
(buffer) only. The remaining 97 entries relate to the
life quality and wellbeing sectors (that is, quality con-
trol of food and beverages, pollution and bioprocess
control, and (sports) medicine, without critical care),
and describe applications in complex media. If we
focus on these applications, it can be stated that
54.6% (53 entries) of those deal with food and bev-
erages. The majority of those – 31 of 53 – are related
to lactate determinations in dairy products (milk, but-
termilk, cheese, cream, curd, kefir, sour cream, whey,
white cheese, and yoghurt) which is not surprising, as
lactate is one basic metabolite of lactic acid bacteria
(LABs) from dairy products. Nearly one third of the
applications in the nutritional sector (32.1%) deal with
non-milk based beverages, like beer, cider, wine, and
Japanese lactic fermenting beverages. Only five out of
53 applications (9.4%) concerning foodstuff are re-
lated to food quality control and to other than dairy
products (determination of lactate levels in baby food,
Korean kimchi, meat extracts, and tomato products).
The (sports) medicine sector amounts to 29.9% of
the 97 mentioned applications in complex media, con-
sisting mainly in lactate determinations in whole
blood but also in sweat, saliva, and interstitial fluid.
In the field of bioprocess monitoring, amperometric
biosensors for lactate are employed to observe the
production of lactic acid by LABs or its blocking by
inhibitory agents as well as the growth of animal and
microbial cell lines. Bioprocess monitoring contri-
butes to the applications in complex media with 11
entries out of 97. Applications of amperometric lac-
tate biosensors in the field of pollution detection in
water is only of minor importance (4 entries out of
97). One example is the discovery of lactate from
silage effluents as a contaminant of water. Another
one is the detection of heavy metal salts in drinking
water [59]. Here, the different sensitivities of some
lactate metabolizing enzymes to heavy metal salts is
employed (LOD from Pediococcus sp. and LDH
from lobster tail are insensitive to heavy metal salts
(HgCl2), whereas LDH from rabbit muscle is sensitive
to them [60]).
Fig. 5. Fields of application for amperometric lactate biosensors.
Percentages are given of the total of 196 entries in 184 articles. A
Dairy products; B non-milk based beverages; C lactate determina-
tion in foodstuff other than beverages; D medical applications
(without critical care); E bioprocess monitoring; F pollution detec-
tion; G biosensor tested in buffer solutions only, no application for
other matrixes
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Interferences and disturbances
The last sections were dedicated to the different com-
position factors and also fields of application of am-
perometric biosensors for the detection of lactate. The
following section will concentrate on aspects concern-
ing possible disturbances of the assay and their over-
coming as well as the dependency of the performance
of the biosensor on the respective composition.
Interferences in and disturbances of the assay natu-
rally vary with the specific sensor set-up and with the
field of application, i.e. the medium in which the lac-
tate determination takes place. Many authors not only
tested their system as to possible interferences or dis-
turbances, but also propose or utilize methods to over-
come them.
There are wanted forms of inhibition of enzymes,
as was already mentioned, for example in the assay
performed in [60]. Here, the inactivation of selected
enzymes by heavy metal salts is the actual indicator
that is detected.
However, unwanted inhibition of enzymes will con-
stitute a major disturbance of an assay.
Mascini et al. [61] affirm results from Lockridge
et al. [62] and Ghisla and Massey [63], that lactate
oxidase from Mycobacterium smegmatis is inhibited
by phosphate and other anions. This should be kept in
mind when those interfering substances are in the so-
lution analyzed by a lactate biosensor based on the
enzyme from this source. This circumstance certainly
will make it difficult to detect lactate in complex me-
dia like blood, for example. However, no inhibition by
phosphate was found for the enzyme lactate oxidase
from Pediococcus sp. [64], which is the lactate oxi-
dase most commonly used in the preparation of am-
perometric lactate biosensors (see Section ‘‘Set-up and
performance’’).
But also competitive inhibitors of enzyme reactions
can disturb the L-lactate assay, e.g., D-lactate is a
competitive inhibitor of LDH (cytochrome) lactate
oxidation [53]. This limits the field of application to
D-lactate free media.
pH and temperature influence the performance of
enzymatic reactions as well. pH optima for a activity
maximum of enzymes can differ depending on the
fact whether the enzyme is free in solution, immobi-
lized on a substrate or incorporated in membranes etc.
The reasons can be a deactivation due to denaturation
of the enzyme, or due to local pH effects. Optimum
pH values – determined in solution – for the reaction
of some lactate converting enzymes used in ampero-
metric biosensors are compiled in Table 1.
pH optima of unmodified enzymes can differ from
pH optima of immobilized enzymes. Therefore, pH
and temperature dependencies should be tested be-
forehand in order to find optimum working conditions
of the enzyme electrode.
It has to be reminded that according to the Arrhe-
nius law, a temperature increase results in an increase
of the reaction rate as long as the enzyme is not de-
natured at higher temperatures. Temperature depen-
dency of the enzyme activity therefore will normally
display a bell shaped curve [67].
However, not only the enzyme reaction can be
affected by inhibition: further on in the reaction
chain, the redox reaction at the electrode is also a
possible target for disturbances. Several publications
state that Ca2þ inhibits the oxidation of hydrogen
peroxide at platinum anodes (Th�eevenot in Ref. [68],
and also: [69, 70]). This affects amperometric bio-
sensors based on LOD and platinum working elec-
trodes. As a remedy, it is recommended to pass the
sample (mainly dairy products) through ion exchange
columns [69].
A very common disturbance of the detection with
amperometric biosensors is the interference caused by
electroactive species – amongst others, ascorbate,
urate, tyrosine, acetaminophen (Paracetamol). This in-
terference leads to false positive results in contrast to
the disturbances caused by inhibition of enzyme or
redox reaction. As already illustrated in the section
about mediators and cofactors, the use of an adequate
redox mediator can ameliorate the situation by lower-
ing the overpotential. Another possibility is the (addi-
tional) coverage of the working electrode with a
membrane (e.g., [70–73]).
This membrane serves as a selective barrier for eas-
ily oxidizable species that would otherwise produce
interferences [74]. The barrier can act as a size limi-
tation, e.g. by using membranes with defined pore size
Table 1. List of optimum pH values for lactate oxidation with the
respective enzyme in solution
Enzyme EC number Origin pH
optimum
Ref.
LOD EC 1.13.12.4 Pediococcus sp. 6.5 [65]
L-LDH EC 1.1.1.27 mammal
muscle
8.6 Schwert and
Winer in
Ref. [66]
D-LDH EC 1.1.1.28 Lactobacillus
leichmanii
8.0 Gasser et al.
in Ref. [66]
N. Nikolaus, B. Strehlitz
or as a repulsion layer of the often negatively charged
interferants by using equally charged membranes.
Set-up and performance
After discussing the key elements that constitute
an amperometric lactate biosensor, the integration of
these elements and the consequences of this integra-
tion for the overall performance are now to be regard-
ed. In Tables 2–6, data concerning the performance of
lactate biosensors is compiled together with set-up
information. Data in the five tables is grouped based
on the the kind of mediator used in the biosensor set-
up (cf. the section about mediators and cofactors).
Note that ‘‘n=a’’ signifies that the according data is
not explicitly given in the respective article. Neverthe-
less, it is possible that data may be accessible from
graphs. This concerns mainly operational stability and
linear range of the calibration curve. When concentra-
tion ranges of linear lactate detection are given, it
should nevertheless be kept in mind that the working
concentration range may extend the linear concentra-
tion range considerably [18].
In the case of the criterion ‘‘application’’, ‘‘n=a’’
means that either no application was given or that
measurements were performed in buffer only.
In order to compare sensitivities, normalization
to the surface area of the electrode is useful. For
this purpose, geometrical areas of electrodes – if
not explicitly given – were calculated from diameter
specifications.
Data in Tables 2–6 was analyzed according to dif-
ferent aspects. Firstly, it was examined, whether a
specific set-up of amperometric lactate biosensors is
preferred in a certain field of application. For this
purpose, the 97 entries from Fig. 5 – where actual
applications are described – were related to different
set-up features. Categorized into the application fields
of Fig. 5, the entries were sorted regarding the use of
mediator, of a two or three electrode set-up, electrode
material, biological recognition element, and immobi-
lization method. As a result, no coincidence of set-up
features and field of application for the lactate biosen-
sor could be found. This may indicate that all kind
of set-ups in principle are appropriate for the whole
range of applications possible for amperometric lac-
tate biosensors.
Nevertheless, there may be some components that
enhance the overall performance of the sensor more
than others. In order to examine this aspect, the sen-
sitivity normalized to the (geometric) area of the
sensor was taken as a measure for the performance
of the sensor. Sensitivity is one of the characteristic
features for the validation of amperometric biosen-
sors for lactate that is most often mentioned in the
texts. Therefore, sensitivity values published in the
investigated literature provide the broadest data pool
for the following investigation. There may be other
possible criteria to act as a measure for the perfor-
mance, like the linear concentration range, lower de-
tection limit or operational and long-term stabilities
for example, but we decided against comparing these
features as criteria for performance for the following
reasons:
The linear range of a biosensor can be extended
considerably by using covering membranes [6, 179],
without difference in the basic set-up, so it does not
seem to be a very specific criterion. The lower detec-
tion limit is connected with the sensitivity of a sensor,
and data for stabilities were given in the examined
articles in too many different ways to be comparable,
so sensitivity per area was chosen as a measure for the
performance of the sensors. The values of sensitivity
per area were calculated if they were not given in the
texts. Data was available for 78 entries out of the total
amount of 184 articles. Multiple entries could be de-
rived from one article.
Sensitivities ranged from 1�10�5 mA mmol�1 L
cm�2 [207] up to 1.4�106 mA mmol�1 L cm�2 [157].
This extremely large span of twelve orders of mag-
nitude was arbitrarily divided into three ranges in or-
der to examine the relation of sensitivity per area and
set-up in more detail. The first range with very good
sensitivities was set as >100mA mmol�1 L cm�2, the
second one between 100 and 10mA mmol�1 L cm�2,
and the third with suboptimal sensitivities as
<10mA mmol�1 L cm�2. These three ranges contain
different numbers of members (14, 28, and 36, res-
pectively). In the following examinations the different
group sizes were taken into account.
Three aspects were regarded in this analysis: the
material of the working electrode, the biological rec-
ognition element, and the method of immobilization
of the biorecognition element at the electrode.
In general, the material of the working electrode
seems to have less influence on the sensitivity per area
compared with the choice of biorecognition element
and method of immobilization. Carbon paste and Pt
electrodes show no negative effects on the perfor-
mance of the sensor, whereas screen printed and gold
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
2.
Co
mp
aris
on
of
set-
up
par
amet
ers
and
per
form
ance
dat
afo
ram
per
om
etri
cla
ctat
eb
iose
nso
rs;
(tra
nsi
tio
n)
met
alco
mp
ou
nd
su
sed
asm
edia
tor
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
l
of
wo
rkin
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elec
tro
de
El.
sys.
1P
ote
nti
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pH
;
tem
per
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re
Sen
siti
vit
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geo
met
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area
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wo
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elec
tro
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lin
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resp
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Op
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stab
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sto
rag
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stab
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Inte
rfer
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;
pro
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Ap
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cati
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Ref
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mat
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po
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win
e[1
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mat
rix
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vs.
SC
E6;
pH
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RT
n=
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21
1mm
olL
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ssy
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od
[79
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n=
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se:
9–
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ffer
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[80
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acy
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SC
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ab
loo
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2U
osm
ium
com
ple
xes
inre
do
xp
oly
mer
gla
ssy
carb
on
30
Vv
s.S
CE
;
pH
7.3
;3
7� C
n=a;
7.1
mm
2n=
a;n=
a;n=
a9
0%
of
init
ial
resp
on
se:
16
0h
of
con
tin
uo
us
op
erat
ion
;n=
a
acet
amin
op
hen
,
asco
rbat
e,
ura
te;
low
po
ten
tial
n=
a[6
5]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
12
6.8
U
1,1
0 -d
imet
hy
lfer
roce
ne=
N,N
-dim
eth
yla
min
o
met
hy
lfer
roce
ne=
ferr
oce
ne
carb
on
pas
te
20
.2–
0.4
Vv
s.
SC
E;
pH
9.3
;
25� C
31mA
mm
ol�
1L
cm�
2;
0.7
8m
m2
n=
a;
0–
1m
mo
lL�
1=
2–
2.5
mm
olL
�1
(Nafi
on
coat
ed);
24=
50
sec
(Nafi
on
coat
ed)
n=
a;n=
aas
corb
ate;
Mel
do
la
blu
e
n=
a[2
0]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
0.0
00
4U
cob
alt
ph
thal
ocy
anin
e
gla
ssy
carb
on
30
.6V
vs.
Ag=
Ag
Cl;
pH
7;
25� C
1.0
2m
Am
ol�
1=
16
1m
Am
ol�
1;
0.0
71
cm2
0.5mm
olL
�1;
0–
0.0
6m
mo
lL�
1=
0.1
43
mm
olL
�1
(dep
end
ing
on
com
po
siti
on
);4
5se
c
n=
a;<
50
%o
f
init
ial
resp
on
se:
18
day
s(s
tora
ge
inbu
ffer
at4� C
)
asco
rbat
e;
ult
rafi
ltra
tio
n
mem
bra
ne
n=
a[7
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
0.0
07
U
cob
alt
ph
thal
ocy
anin
e
gla
ssy
carb
on
30
.5V
vs.
Ag=
Ag
Cl;
pH
6.5
;2
5� C
3.9
8mA
mm
ol�
1L
cm�
2;
7.1
mm
2
8mm
olL
�1;
0.0
2–
4m
mo
lL�
1;
5–
35
sec
n=
a;7
2%
of
init
ial
resp
on
se:
1m
on
th(s
tora
ge
inbu
ffer
at4� C
)
asco
rbat
e;
Mn
O2
nan
op
arti
cles
inch
ito
san
lay
er
mil
k[8
2]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
>1
2U
mg�
1p
aste
ferr
oce
ne
carb
on
pas
te
20
.7V
vs.
Pt;
pH
8.9
;R
T
11
7mA
mm
ol�
1
Lcm
�2=
13
3mA
mm
ol�
1L
cm�
2;
0.0
7cm
2
n=
a;0
.5–
5.5
mm
olL
�1;
20
sec
n=
a;>
5m
on
ths
n=
a;n=
an=
a[5
6]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
17
U
osm
ium
com
ple
xes
inre
do
xp
oly
mer
gla
ssy
carb
on
3n=
a;n=
a;
n=
a
n=a;
19
.6m
m2
n=
a;0
–1
mm
olL
�1;
n=
a
n=
a;n=
an=
a;n=
an=
a[8
3]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=
a
osm
ium
com
ple
xes
inre
do
xp
oly
mer
gla
ssy
carb
on
30
.15
Vv
s.
SC
E;
pH
7.3
;
21
.3� C
69mA
mm
ol�
1
Lcm
�2;
7.1
mm
2
n=
a;0
–0
.5m
mo
lL�
1;
n=
a
50
%o
fin
itia
l
acti
vit
y:
16
h;
n=
a;
ox
yg
en;
deo
xy
gen
ated
solu
tio
ns
n=
a[8
4]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=
a
osm
ium
com
ple
xes
inre
do
xp
oly
mer
gla
ssy
carb
on
30
.45
Vv
s.
SC
E;
pH
7.1
5;
21
.8� C
0.3
Am
ol�
1
Lcm
�2;
7.1
mm
2
n=
a;0
–0
.2m
mo
lL�
1;
1se
c
loss
of
enzy
me
acti
vit
yw
ith
in
12
–2
4h
;n
o
curr
ent
afte
r
1m
on
th(s
tora
ge
atR
T)
n=
a;n=
an=
a[8
5]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
26
U
Rh
dis
per
sed
inca
rbo
n
carb
on
pas
te
20
.4V
vs.
Ag=
Ag
Cl;
pH
7;
n=
a
n=a;
n=a
n=
a;
0.1
–1
.5m
mo
lL�
1;
n=
a
30
%o
fin
itia
l
acti
vit
y:
45
ho
f
con
tin
uo
us
op
erat
ion
;4
4%
of
init
ial
acti
vit
y:
25
day
s(s
tora
ge
at4� C
)
n=
a;n=
ace
ll
cult
ure
bro
th
[86
]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
2(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
l
of
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
-
cati
on
Ref
.2
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
1U
mg�
1p
aste
Rh
dis
per
sed
inca
rbo
n
carb
on
pas
te
30=�
0.2
Vv
s.
Ag=
Ag
Cl;
pH
7.4
;R
T
n=
a;0
.8m
m2
0.0
15
mm
ol�
1L
(S=N¼
3);
0–
0.5
mm
olL
�1=
–;
8se
c=2
min
n=
a;n=
a–
;lo
wp
ote
nti
aln=
a[8
7]
LO
D(E
C1
.1.3
.x);
Pediococcus
sp.;
1.6
U
ferr
icyan
ide
carb
on
film
20
.5V
vs.
refe
ren
ce
elec
tro
de;
n=
a;n=
a
n=
a;n=
a0
.1m
mo
lL�
1;
0.1
–2
0m
mo
lL�
1;
60
sec
sin
gle
-use
test
stri
ps;
n=a
asco
rbat
e;n=
ab
loo
d[8
8]
LO
D(E
C
1.1
3.1
1.1
4)
(sic
!);
Pediococcus
sp.;
52
U
Rh
dis
per
sed
inca
rbo
n
carb
on
pas
te
n=
a�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
7.4
;
25� C
n=
a;7
mm
2n=
a;n=a;
n=a
n=
a;5
0%
of
init
ial
acti
vit
y:
0.5
day
s(s
tora
ge
at6
0� C
)
tem
per
atu
re;
n=
a
n=
a[8
9]
LO
D(E
C
23
2-8
41
-6)
(sic
!);
Pediococcus
sp.;
2.1
U
hy
dro
xy
met
hy
l-
ferr
oce
ne
Au
30
.3V
vs.
SS
CE
7;
pH
7;
20� C
0.7
7�
0.0
8mA
mm
ol�
1L
;
0.2
cm2
0.0
1m
mo
lL�
1;
0–
0.3
mm
olL
�1;
70
sec
n=
a;>
1m
on
th
(sto
rag
ein
ph
osp
hat
ein
bu
ffer
at4� C
)bu
t:d
rop
of
50
%o
fre
spo
nse
afte
rfi
rst
assa
y,
then
stab
le!
asco
rbat
e;n=
ab
eer,
win
e
[8]
LO
D(n
oE
Cg
iven
);
Enterococcus
sp.=
Pediococcus
sp.;
2–
6U
Pru
ssia
nb
lue
gla
ssy
carb
on
3�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
5.5
;n=
a
n=
a;7
.1m
m2
0.7mm
olL
�1;
0–
0.8
mm
olL
�1;
n=
a
99
–1
00
%o
fin
itia
l
sen
siti
vit
y:
40
–8
0
det
erm
inat
ion
s;
25
%o
fin
itia
l
sen
siti
vit
y:
2w
eek
s(s
tora
ge
inbu
ffer
at4� C
)
acet
amin
op
hen
,
asco
rbat
e,
ura
te;
Nafi
on
lay
er
n=
a[7
2]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=
a
dim
ethyl-
ferr
oce
ne
gra
ph
ite
n=
an=
a;n=
a;
n=
a
50
nA
mm
ol�
1L
;
n=
a
1mm
olL
�1;
0.0
01
–1
.2m
mo
lL�
1;
n=
a
n=
a;n=
an=
a;n=
aan
imal
cell
cult
ivat
ion
[90
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=
a
ferr
oce
ne
Au
3n=
a;
pH
7.4
;n=
a
n=
a;2=
20
mm
20
.1m
mo
lL�
1;
0–
16
mm
olL
�1;
n=
a
n=
a;n=
an=
a;n=
an=
a[9
1]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
20
4U
ferr
oce
ne
Pt
2n=
a;
pH
6.2
5;
n=
a
n=
a;n=
an=
a;n=a
n=a
n=
a;n=
an=
a;n=
am
ilk
[47
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
0.0
7–
0.1
05
U
osm
ium
com
ple
x
carb
on
30
.4V
vs.
SC
E;
pH
7.1
3;
22� C
20
mA
mo
l�1
Lcm
�2;
0.0
09�
0.0
02
cm2
(det
erm
ined
area
)
n=
a;0
–1
mm
olL
�1;
12
sec
75
%o
fin
itia
l
curr
ent:
6h
of
con
tin
uo
us
op
erat
ion
;
4m
on
ths
(sto
rag
e
dry
at4� C
)
asco
rbat
e;
inte
rfer
ant-
elim
inat
ing
lay
ero
fG
OD
8
and
HR
P9
n=
a[9
2]
N. Nikolaus, B. Strehlitz
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
2.0
4U
osm
ium
com
ple
x
gla
ssy
carb
on
30
.4V
vs.
Ag=
Ag
Cl;
pH
6.8
;n=
a
1.0
2mA
mm
ol�
1L
;
n=a
0.0
5m
mo
lL�
1;
0.1
–9
mm
olL
�1;
10
sec
n=
a;<�
5%
RS
D1
0:
1w
eek
asco
rbat
e,O
2;
deo
xy
gen
ated
solu
tio
ns
n=
a[9
3]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=a
Pru
ssia
nb
lue
carb
on
3�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
7;
n=
a
10
.4mA
mm
ol�
1L
;
0.2
cm2
1mm
olL
�1;
0.0
1–
0.5
mm
olL
�1;
1–
2m
in
n=
a;8
0%
acti
vit
y:
1m
on
th(s
tora
ge
inbu
ffer
at4� C
)
Ca2
þ;
n=a
win
e,
yo
gh
urt
[94
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
0.0
8U
Pru
ssia
nb
lue
Pt
20
Vv
s.
Ag=
Ag
Cl;
pH
7.5
;n=
a
87mA
mo
l�1
L;
1cm
20
.05
mm
olL
�1;
0.0
1–
1m
mo
lL�
1;
15
sec
90
%o
fin
itia
l
acti
vit
y:
60
ho
f
con
tin
uo
us
op
erat
ion
;n=
a
asco
rbat
e;
con
du
ctiv
e
po
lym
er
nan
otu
bu
les
n=
a[9
5]
LO
D(E
C1
.1.3
.2,
now
EC
1.1
3.1
2.4
);
n=a;
n=a
Rh
dis
per
sed
inca
rbo
n
carb
on
pas
te
20
.35
Vv
s.
Ag=
Ag
Cl;
pH
7;
n=
a
n=a;
n=a;
50
nm
olL
�1;
0.1
–1
.5m
mo
lL�
1;
20
–3
0se
c
sin
gle
use
;n=a
fou
lin
gb
y
par
ticu
late
s;
cen
trif
ug
atio
n,
dil
uti
on
sila
ge
effl
uen
ts
[10
]
LO
D(n
oE
Cg
iven
);
n=a;
n=a
cob
alt-
tetr
amet
ho
xy
-
ph
eny
lpo
rph
yri
n
carb
on
pas
te
20
.4V
vs.
Ag=
Ag
Cl;
pH
7;
RT
n=a;
n=a;
n=
a;0
–1
.5m
mo
lL�
1;
<1
min
sin
gle
use
;n=a
n=a;
n=
an=
a[9
6]
LO
D(n
oE
Cg
iven
);
n=a;
n=a
cob
alt-
tetr
amet
ho
xy
-
ph
eny
lpo
rph
yri
n
carb
on
pas
te
20
.4V
vs.
Ag=
Ag
Cl;
n=a;
n=a
n=a;
2.5
mm
2n=
a;n=
a;n=
an=
a;n=
an=a;
n=
an=
a[9
7]
LO
D(n
oE
Cg
iven
);
n=a;
5U
ferr
icyan
ide
carb
on
scre
en
pri
nti
ng
ink
30
.4V
vs.
Ag=
Ag
Cl;
pH
7.8
;2
5� C
n=a;
n=a
1m
mo
lL�
1;
1–
50
mm
olL
�1;
50
sec
n=
a;<
10
mo
nth
s
(sto
rag
ed
ryat
�3
0� C
)
cro
ss-t
alk
;
n=a
lact
ic
ferm
enti
ng
bev
erag
e
[98
]
LO
D(n
oE
Cg
iven
);
n=a;
n=a
ferr
oce
ne
Pt
30
.2=0
.5V
vs.
Ag=
Ag
Cl;
pH
7;
n=
a
n=a;
n=a
0.5
mm
olL
�1;
n=
a;
5–
10
sec
n=
a;(s
tora
ge
in
bu
ffer
at4� C
)
asco
rbat
e,
fru
cto
se,
glu
cose
,O
2,
ure
a;re
do
x
med
iato
r
n=
a[9
9]
LO
D(n
oE
Cg
iven
);
n=a;
n=a
ferr
oce
ne
Pt
30
.7V
vs.
SC
E;
pH
7;
37� C
n=a;
0.3
6m
m2
n=
a;
0.0
5–
0.6
mm
olL
�1;
1m
in
few
day
s;n=
an=a;
n=
an=
a[1
00
]
D-L
DH
(no
EC
giv
en);
n=a;
0.1
mg
mL�
1
dia
ph
ora
se(n
oE
C
giv
en);
n=a;
1m
gm
L�
1
ferr
ocy
anid
e,
NA
Dþ
in
solu
tio
n
Pt
20
.1V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de;
pH
9;
RT
20mA
mm
ol�
1L
cm�
2;
0.2
mm
20
.01
mm
olL
�1
(S=N¼
2);
0.0
1–
2mm
olL
�1;
3m
in
n=
a;>
2m
on
ths
n=a;
n=
an=
a[1
01
]
D-L
DH
(EC
1.1
.1.2
8);
Lactobacillus
leichmanii
;3
54
Um
L�
1
dia
ph
ora
se(E
C1
.8.1
.4);
Clostridium
kluyveri;
6.4
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
Au
20
.2V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de
(Au
);
pH
9;
RT
2mA
mm
ol�
1L
cm�
2;
n=a
5mm
olL
�1;
0.0
05
–1
.5m
mo
lL�
1;
2m
in
n=
a;n=
an=a;
low
po
ten
tial
n=
a[1
02
]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
2(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
l
of
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
-
cati
on
Ref
.2
D-L
DH
(EC
1.1
.1.2
8);
Lactobacillusleichmanii
;
35
4U
mL�
1d
iap
ho
rase
(EC
1.8
.1.4
);
Clostridium
kluyveri;
6.4
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
Au
20
.2V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de
(Au
);
pH
9;
RT
2–
8mA
mm
ol�
1L
cm�
2;
0.2
5m
m2
0.0
1m
mo
lL�
1;
0.0
05
–1
.5m
mo
lL�
1;
2–
5m
in
3w
eek
s(1
0
det
erm
inat
ion
sp
er
day
,st
ora
ge
in
bu
ffer
at4� C
);n=
a
n=
a;n=
a;n=
a[1
03
]
D-L
DH
(EC
1.1
.1.2
8);
Lactobacillusleichmanii
;
35
4U
mL�
1d
iap
ho
rase
(EC
1.8
.1.4
);
Clostridium
kluyveri;
6.4
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
Au
20
.2V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de
(Au
);
pH
9;
RT
8mA
mm
ol�
1L
cm�
2;
0.2
5m
m2
0.0
1m
mo
lL�
1;
0.0
2–
1.1
mm
olL
�1;
5m
in
3w
eek
s(1
0
det
erm
inat
ion
sp
er
day
,st
ora
ge
in
bu
ffer
at4� C
);n=
a
n=
a;n=
a;n=
a[1
04
]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
;4
Um
L�
1
dia
ph
ora
se(E
C1
.8.1
.4);
Clostridium
kluyveri;
40
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
DH
11
inso
luti
on
Pt
20
.1V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de
(Pt)
;
pH
9;
30� C
3.8mA
mm
ol�
1L
;n=a
n=a
0.0
2–
3m
mo
lL�
1
<2
min
10
day
s(s
ever
al
det
erm
inat
ion
s,
sto
rag
ein
bu
ffer
at
4� C
);7
0–
80
%o
f
init
ial
acti
vit
ity
:
1m
on
th(s
tora
ge
at
4� C
inbu
ffer
)
n=
a;n=
aal
coh
oli
c
bev
erag
es,
mil
k
[42
]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
;6
Ucm
�3;
dia
ph
ora
se(E
C1
.8.1
.4);
Clostridium
kluyveri;
15
0U
cm�
3
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
n=
an=
a0
.8V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de;
n=
a;
25� C
0.2
–0
.9mA
mm
ol�
1L
;
n=
a
n=a;
0.0
05
–0
.15=
0.0
2–
6m
mo
lL�
1;
1–
3m
in
n=
a;2
–4
0d
ays
(sto
rag
ein
bu
ffer
at4� C
)
n=
a;n=
an=
a[7
6]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
;4
Um
L�
1
NA
DH
ox
idas
e
(EC
1.6
.99
);
Thermusthermophilus;
50
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
DH
inso
luti
on
Pt
20
.55
Vv
s.
pse
ud
o
refe
ren
ce
elec
tro
de
(Pt)
;
pH
9;
30� C
2.5mA
mm
ol�
1L
;n=a
n=a
0.0
4–
1.5
mm
olL
�1
<2
min
10
day
s(s
ever
al
det
erm
inat
ion
s,
sto
rag
ein
bu
ffer
at
4� C
);7
0–
80
%o
f
init
ial
acti
vit
ity
:
1m
on
th(s
tora
ge
at
4� C
inbu
ffer
)
n=
a;n=
aal
coh
oli
c
bev
erag
es,
mil
k
[42
]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
;7
Um
L�
1
NA
DH
ox
idas
e
(EC
1.6
.99
);Thermus
thermophilus;
28
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
DH
inso
luti
on
Pt
20
.8V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de
(Pt)
;
pH
9;
30� C
50
0–
57
0n
Am
mo
l�1
L;
n=
a
n=a
0.0
1–
1m
mo
lL�
1
2–
3m
in
50
%o
fin
itia
l
acti
vit
y:
6h
of
con
tin
uo
us
op
erat
ion
(en
zym
ein
solu
tio
n)=
4m
on
ths,
50
–1
00
assa
ys
per
day
(im
mo
bil
ized
enzy
me,
sto
rag
ein
bu
ffer
at4� C
);n=
a
n=
a;n=
ach
eese
,
mil
k,
yo
gh
urt
[10
5]
N. Nikolaus, B. Strehlitz
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;1
94
Um
L�
1
dia
ph
ora
se(E
C1
.8.1
.4);
Clostridium
kluyveri;
6.4
Um
L�
1
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
Au
20
.2V
vs.
pse
ud
o
refe
ren
ce
elec
tro
de
(Au
);
pH
9;
RT
1.8mA
mm
ol�
1L
cm�
2;
n=
a
10mm
olL
�1;
0.0
02
–1
.7m
mo
lL�
1;
3m
in
n=
an=
an=
a;lo
w
po
ten
tial
n=a
[10
2]
L-L
DH
(no
EC
giv
en);
mu
scle
;2
5m
gm
L�
1
dia
ph
po
rase
(no
EC
giv
en);
n=
a;2
5m
gm
L�
1
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
Pt
20
.3V
vs.
SC
E;
pH
9.2
;
n=a
0.5mA
mm
ol�
1L
;n=
an=
a;
0.2
–8
mm
olL
�1;
40
sec
n=
a;n=
an=
a;n=a;
n=a
[10
6]
L-L
DH
(EC
1.1
.1.2
7);
rabbit
musc
le;
100
Ucm
�3;
dia
phora
se(E
C1.8
.1.4
);
Clostridiumkluyveri;
350
Ucm
�3
hex
acy
ano
-
ferr
ate,
NA
Dþ
inso
luti
on
n=
an=a
0.8
Vv
s.
pse
ud
o
refe
ren
ce
elec
tro
de;
n=a;
25� C
0.2
5mA
mm
ol�
1L
;
n=
a
n=
a;
0.0
05
–0
.15
mm
olL
�1;
1m
in
n=
a;2
day
s
(sto
rag
ein
buff
erat
4� C
)
n=
a;n=a
n=a
[76
]
L-L
DH
(no
EC
giv
en);
bov
ine
hea
rt;
55
UL
-LD
H
(cy
toch
rom
e)(n
o
EC
giv
en);
bak
er’s
yea
st;
10
U
hex
acy
ano
-
ferr
ate,
NA
DH
inso
luti
on
Pt
20
.25
Vv
s.
Ag=
Ag
Cl;
pH
6;
25� C
n=
a;n=
a0
.3mm
olL
�1;
0.3
–2
0=1
00mm
olL
�1;
n=
a
n=
a;n=
an=
a;n=a
n=a
[39
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
31
.2U
;
per
ox
idas
e(E
C1
.11
.1.7
,
typ
eV
I);
ho
rser
adis
h;
57
6U
osm
ium
com
ple
x
gla
ssy
carb
on
30
Vv
s.S
CE
;
pH
7.4
;R
T
n=
a;n=
an=
a;
0.2
–1
.8m
mo
lL�
1;
n=
a
50
%o
fin
itia
l
acti
vit
y:
6h=>
30
h
of
con
tin
uo
us
op
erat
ion
;n=
a
n=
a;n=a
n=a
[10
7]
LO
D(n
oE
Cg
iven
);n=
a;
n=
a;p
ero
xid
ase
(no
EC
giv
en);
ho
rser
adis
h;
n=a
ferr
oce
ne
carb
on
pas
te
2�
0.1
Vv
s.
Ag=
Ag
Cl;
n=a;
n=
a
14
.31
nAmm
ol�
1L
;
n=
a
n=
a;
4–
40mm
olL
�1;
n=
a
n=
a;2
0%
of
init
ial
sen
siti
vit
y:
2m
on
ths
(sto
rag
e
at4� C
)
n=
a;n=a
ferm
en-
tati
on
bro
ths
[33
]
LO
D(E
C1
.1.3
.2);
n=
a;
10
2U
;p
ero
xid
ase
(EC
1.1
1.1
.7,
typ
eII
);
ho
rser
adis
h;
27
00
U
ferr
oce
ne
gra
ph
ite-
Tefl
on
30
Vv
s.
Ag=
Ag
Cl;
pH
7.4
;2
5� C
0.4
24mA
mm
ol�
1L
(FIA
12),
2.9
8mA
mm
ol�
1L
(bat
ch);
7.1
mm
2
0.9mm
olL
�1
(FIA
),
1.4mm
olL
�1
(bat
ch);
0.0
05
–1
0m
mo
lL�
1
(FIA
),
0.0
02
5–
1m
mo
lL�
1
(bat
ch);<
2m
in
60
day
s(3
det
erm
inat
ion
s
per
day
,re
pet
itiv
e
po
lish
ing
);
6m
on
ths
(sto
rag
e
at4� C
)
asco
rbat
e,
mal
ate,
tart
rate
,
succ
inat
e;
n=
a
win
e,
yo
gh
urt
[10
8]
LO
D(n
oE
Cg
iven
);n=
a;
n=
a;p
ero
xid
ase
(no
EC
giv
en);
ho
rser
adis
h;
n=a
ferr
oce
ne
gra
ph
ite-
Tefl
on
n=a
0V
vs.
refe
ren
ce
elec
tro
de;
pH
7.4
;n=
a
n=
a;7
.1m
m2
n=
a;
0.0
05
–1
mm
olL
�1;
n=
a
20
day
s(3
0
det
erm
inat
ion
s
per
day
);n=
a
n=
a;n=a
yo
gh
urt
[12
]
LO
D(E
C1
.1.3
.x);
Pediococcus
sp.;
33
–5
0mg
;p
ero
xid
ase
(EC
1.1
1.1
.7,
typ
eII
);
ho
rser
adis
h;
3mg
osm
ium
com
ple
xes
inre
do
x
po
lym
er
gla
ssy
carb
on
n=a
0V
vs.
SC
E;
pH
7;
n=
a
9.1
6mA
mm
ol�
1L
;
19
.6m
m2
n=
a;
0.0
25
–0
.5m
mo
lL�
1;
n=
a
3h
;n=
a–
;lo
w
po
ten
tial
,
mu
ltil
ayer
com
po
siti
on
mil
k[7
1]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
2(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
l
of
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
-
cati
on
Ref
.2
Hansenula
anomala
wh
ole
cell
s;0
.42
Um
g�
1
pas
te
var
iou
s
med
iato
rs,
sin
gle
and
mix
ed
carb
on
pas
te
20
.05
–0
.3V
vs.
SC
E;
pH
7.6
–7
.7;
25� C
14
–1
16mA
mm
ol�
1L
cm�
2;
0.2
8m
m2
n=a;
0–
6=8
mm
olL
�1
(fer
ricy
anid
e);
1–
2.1
min
(fer
ricy
anid
e)
70
%o
fin
itia
l
resp
on
se:
30
min
(in
bu
ffer
at
25� C
);9
0%
of
init
ial
acit
vit
y:
>2
mo
nth
s
(sto
rag
ed
ry
at4� C
)
asco
rbat
e;
n=a
n=
a[1
09
]
Paracoccusdenitrificans
mem
bra
ne
ves
icle
s=Paracoccusdenitrificans
wh
ole
cell
s
ferr
oce
ne
carb
on
pas
te
30
.3V
vs.
Ag=
Ag
Cl;
pH
7.3
;3
0� C
0.4
79mA
mm
ol�
1L
(D-l
acta
te=m
emb
ran
e
ves
icle
s),
0.5
03mA
mm
ol�
1L
(L-l
acta
te=
mem
bra
ne
ves
icle
s),
0.1
19mA
mm
ol�
1L
(L-l
acta
te=w
ho
lece
lls)
;
3.1
4m
m2
n=a;
0–
0.2
mm
olL
�1
(D-l
acta
te=m
emb
ran
e
ves
icle
s),
0–
0.1
mm
olL
�1
(L-l
acta
te=
mem
bra
ne
ves
icle
s),
0–
3m
mo
lL�
1
(L-l
acta
te=w
ho
lece
lls)
;
2–
10
min
n=
a;n=a
n=a;
n=a
n=
a[1
10
]
1El.Sys.
Tw
o(2
)o
rth
ree
(3)
elec
tro
de
syst
em.
2Ref.
Ref
eren
ce.
3NAD
þN
ico
tin
amid
ead
enin
ed
inu
cleo
tid
e.4RT
Ro
om
tem
per
atu
re.
5S=N
Sig
nal
ton
ois
era
tio
.6SCE
Sat
ura
ted
calo
mel
elec
tro
de.
7SSCE
So
diu
msa
tura
ted
calo
mel
elec
tro
de.
8GOD
Glu
cose
ox
idas
e.9HRP
Ho
rse
rad
ish
per
ox
idas
e.1
0RSD
Rel
ativ
est
and
ard
dev
iati
on
.1
1NADH
Nic
oti
nam
ide
aden
ine
din
ucl
eoti
de
(red
uce
dfo
rm).
12FIA
Flo
win
ject
ion
anal
ysi
s.
N. Nikolaus, B. Strehlitz
Table
3.
Co
mp
aris
on
of
set-
up
par
amet
ers
and
per
form
ance
dat
afo
ram
per
om
etri
cla
ctat
eb
iose
nso
rs;
org
anic
dy
esu
sed
asm
edia
tor
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
lo
f
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
ca-
tio
n
Ref
.2
D-L
DH
(EC
1.1
.1.2
8);
Lactobacillus
leichmanii
;0
.5U
Mel
do
lab
lue-
rein
eck
esa
lt,
NA
Dþ
3
gra
ph
ite
scre
en
pri
nti
ng
ink
2�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
8.5
;2
5� C
20
7n
Am
mo
l�1
L;
17
mm
25
0mm
olL
�1
(S=N
4¼
5=
2);
0.1
–1
mm
olL
�1;
15
0se
c
dis
po
sab
lese
nso
r;
75
%o
fin
itia
l
acti
vit
y:
2w
eek
s
(sto
rag
eat
4� C
)
ph
eno
lic
com
po
un
ds;
Nafi
on
and
po
lyet
hy
len
e-
imin
ela
yer
win
e[1
11
]
D-L
DH
(EC
1.1
.1.2
8);
Lactobacillus
leichmanii
;0
.5U
(reu
sab
le)
Mel
do
lab
lue-
rein
eck
esa
lt,
NA
Dþ
imm
ob
iliz
ed
and
inso
luti
on
gra
ph
ite
scre
en
pri
nti
ng
ink
2�
0.1
5V
vs.
Ag=
Ag
Cl;
pH
8.5
;n=
a
28
0=5
89
nA
mm
ol�
1L
;
n=
a
30=
50mm
olL
�1;
12
0=
15
0se
c
n=
a;7
4%
of
init
ial
acti
vit
y:
2w
eek
s
ph
eno
lic
com
po
un
ds;
low
po
ten
tial
win
e[1
1]
D-L
DH
(EC
1.1
.1.2
8);
Lactobacillus
leichmanii
;0
.5U
(reu
sab
lean
d
dis
po
sab
le)
Mel
do
lab
lue
or
Mel
do
la
blu
e-re
inec
ke
salt
,N
AD
þ
gra
ph
ite
scre
en
pri
nti
ng
ink
2�
0.0
5V
vs.
Ag=
Ag
Cl;
n=
a;2
5� C
n=
a;n=
a3
0=
50mm
olL
�1;
0.0
5–
1=
0.0
75
–1
mm
olL
�1
30
sec
>3
0as
say
s=d
isp
osa
ble
sen
sor;
n=
a
n=
a;n=
aw
ine
[11
2]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
ssp
.
crem
oris;
23
–1
87
Um
g�
1
gra
ph
ite
pow
der
tolu
idin
eb
lue
Oan
dp
oly
-
eth
yle
nei
min
e,
NA
Dþ
carb
on
pas
te
3�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
7;
n=
a
n=
a;0
.05
3cm
23
0mm
olL
�1
(S=N¼
2);
0.0
5–
5m
mo
lL�
1;
n=
a
>7
0%
of
init
ial
acti
vit
y:
23
0
assa
ys;
40
%o
f
init
ial
val
ue:
31
day
s(s
tora
ge
dry
at4� C
py
ruvat
e,D
L-�
-
hy
dro
xy
bu
tyri
c
acid
;n=a
ferm
en-
tati
on
bro
th
[2]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
ssp
.
crem
oris;
n=
a
tolu
idin
eb
lue
Oan
dp
oly
-
eth
yle
nei
min
e,
NA
Dþ
carb
on
pas
te
3�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
7;
n=
a
n=
a;n=
a0
.7m
mo
lL�
1;
0–
10
mm
olL
�1;
n=
a
20
ho
fco
nti
nu
ou
s
op
erat
ion
(dec
reas
ing
resp
on
se;
cali
bra
tio
n
nec
essa
ry)
n=
a
n=
a;n=
afe
rmen
-
tati
on
bro
th
[11
3]
L-L
DH
(EC
1.1
.1.2
7);
pig
mu
scle
;4
4U
ph
enaz
ine
met
ho
sulf
ate
(PM
Sþ
),
NA
Dþ
Pt
20
(wit
hP
MSþ
)=0
.75
V(w
ith
ou
t
PM
Sþ
)v
s.
Ag=
Ag
Cl;
pH
8;
30� C
n=
a;4
.9m
m2
n=
a;0
–1
.5m
mo
lL�
1;
3m
in(w
ith
PM
Sþ
),
5–
6m
in(w
ith
ou
t
PM
Sþ
)
n=
a;5
0%
of
init
ial
acti
vit
y:
60
h(s
tora
ge
at4� C
)
n=
a;n=
an=
a[1
14
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
6U
Mel
do
lab
lue
or
Mel
do
la
blu
e-re
inec
ke
salt
,N
AD
þ
gra
ph
ite
scre
en
pri
nti
ng
ink
20
Vv
s.
Ag=
Ag
Cl;
n=
a;2
5� C
1.0
2=
3.0mA
mm
ol�
1L
;
n=
a
10mm
olL
�1;
20
–2
00mm
olL
�1
30
sec
dis
po
sab
le
sen
sor;
n=
a
n=
a;n=
aw
ine
[11
2]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
3(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
lo
f
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
ca-
tio
n
Ref
.2
L-L
DH
(EC
1.1
.1.2
7)
rab
bit
mu
scle
;2
.5m
g
1-m
eth
ox
y-
ph
enaz
ine
met
ho
sulf
ate-
Rei
nec
ke
salt
,
NA
Dþ
in
solu
tio
n
carb
on
pas
te
30
Vv
s.S
CE
5;
pH
8.5
;R
T6
(50� C
bet
wee
n
mea
sure
men
ts)
n=a;
3.1
4m
m2
n=
a;0
–1
mm
olL
�1;
n=
a
>8
0h
;n=
an=a;
n=a
n=
a[1
15
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
21
0U
met
hy
len
e
blu
e,N
AD
þ
inso
luti
on
gla
ssy
carb
on
2�
0.1
Vv
s.
SC
E;
pH
8.8
;
25� C
2.2
5m
Am
ol�
1L
;
19
.6m
m2
1mm
olL
�1;
n=
a;
20
–3
0se
c
n=
a;n=
an=a;
n=a
n=
a[1
16
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
16
0U
mL�
1
ph
enaz
ine
met
ho
sulf
ate
(PM
Sþ
),
NA
Dþ
inso
luti
on
Au
3�
0.1
Vv
s.
SC
E;
pH
8.1
;2
5� C
1.6
mA
mm
ol�
1L
(co
nfi
g.
17),
1.3
mA
mm
ol�
1L
(co
nfi
g.
28);
0.0
71
cm2
1mm
olL
�1
(co
nfi
g.
1),
5mm
olL
�1
(co
nfi
g.
2);
0.0
05
–1
0m
mo
lL�
1
(co
nfi
g.
1),
0.1
–1
0m
mo
lL�
1
(co
nfi
g.
2);
n=
a;1
mo
nth
(sto
rag
eat
4� C
)
asco
rbat
e;
elec
tro
po
lym
eriz
ed
pro
tect
ion
lay
er
n=
a[1
17
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
7–
12
%
(w=w
)in
gra
ph
ite
pas
te
tetr
acy
ano
qu
ino
-
dim
eth
ane,
NA
Dþ
in
solu
tio
n
carb
on
pas
te
30
.22
Vv
s.
SC
E;
pH
7.5
;2
5� C
n=a;
7.1
mm
20
.2m
mo
lL�
1;
n=
a;
15
–3
0se
c
n=
a;5
5%
of
init
ial
resp
on
se:
30
day
s(s
tora
ge
inbu
ffer
atR
T)
tem
per
atu
re,
pH
;n=a
n=
a[1
18
]
L-L
DH
(EC
1.4
.1.3
(sic
!));
rab
bit
mu
scle
or
chic
ken
hea
rt;
20
0U
mL�
1
Mel
do
lab
lue,
NA
Dþ
gra
ph
ite-
epo
xy=
gra
ph
ite
scre
en
pri
nti
ng
ink
(so
l–g
el)
3�
0.1
–0
.3V
vs.
SC
E;
pH
8=7
;R
T
80
mA
mo
l�1
L
(gra
ph
ite-
epo
xy
)=2
60mA
mo
l�1
L
(scr
een
pri
nte
d);
28
.3m
m2
(gra
ph
ite-
epo
xy
)=2
4o
r3
8m
m2
(scr
een
pri
nte
d)
0.8
7mm
olL
�1
(gra
ph
ite-
epo
xy
)=0
.01
–0
.11
mm
olL
�1
(scr
een
pri
nte
d)
(S=N¼
3);
1–
1.2mm
olL
�1
(gra
ph
ite-
epo
xy
)=0
.12
5–
2.4
8m
mo
lL�
1
(scr
een
pri
nte
d);
<3
0se
c
ca.
80
–6
0%
of
init
ial
sen
siti
vit
y:
1w
eek
(sto
rag
e
inbu
ffer
at4� C
)
n=a;
low
po
ten
tial
n=
a[1
19
]
L-L
DH
(no
EC
giv
en);
po
rcin
eh
eart
;n=
a
po
ly(m
eth
yle
ne
blu
e),
NA
Dþ
gla
ssy
carb
on
30
–0
.1V
vs.
SC
E;
pH
8.5
;
RT
n=a;
7.1
mm
2n=
a;n=
a;2
0–
30
sec
>1
0as
say
s;n=
an=a;
n=a
n=
a[1
20
]
L-L
DH
(no
EC
giv
en);
rab
bit
mu
scle
;
5=
10=
20
U
Mel
do
la
blu
e,N
AD
þca
rbo
n
scre
en
pri
nti
ng
ink
3�
0.0
5V
vs.
SC
E;
pH
8;
23� C
24
.38
nA
mm
ol�
1L
;
n=a
0.5
–8
mm
olL
�1;
1–
20
mm
olL
�1;
n=
a
n=
a(s
tora
ge
at
RT
and
usa
ge
wit
hin
3d
ays)
;
asco
rbat
e,
py
ruvat
e;n=
a
n=
a[1
21
]
L-L
DH
;n=
a;
4U
mg�
1p
aste
tolu
idin
eb
lue
O,
NA
DH
9
inso
luti
on
carb
on
pas
te
30
Vv
s.
Ag=
Ag
Cl;
pH
7.2
;n=
a
73mA
cm�
2m
ol�
1;
0.0
7cm
20
.5m
mo
lL�
1;
1.5
–8
mm
olL
�1;
n=
a
>9
8%
of
init
ial
sig
nal
:4
5as
say
s;
n=
a
n=a;
n=a
n=
a[1
22
]
N. Nikolaus, B. Strehlitz
L-L
DH
(cy
toch
rom
e)
(EC
1.1
.2.3
);
Hansenula
anomala
;
0.1
mg
N-m
eth
yl-
ph
enaz
iniu
m
com
ple
xed
wit
h
tetr
acy
ano
qu
ino
-
dim
eth
ane
Pt
3�
0.3
–0
.4V
vs.
Ag=
Ag
Cl;
pH
6.6
;2
0� C
n=
a;n=
an=a;
n=a;
3–
10
min
n=
a;n=a
n=
a;n=
an=a
[12
3]
L-L
DH
(cy
toch
rom
e)
(EC
1.1
.2.3
);
Hansenula
polymorpha
;
0.0
38
–0
.07
6U
met
hy
len
eb
lue=
ph
enaz
ine
eth
osu
lfat
e
gra
ph
ite
30
.3V
vs.
Ag=A
gC
l;
pH
7.2=
7.6
;
RT
n=
a;7
.3m
m2
n=a;
n=a;
6se
cn=
a;5
0%
init
ial
resp
on
se:
9–
24
h
(sto
rag
ein
buff
er
at4� C
)
n=
a;n=
an=a
[80
]
L-L
DH
(cy
toch
rom
e)
(no
EC
giv
en)
Saccharomyces
cerevisiae;
1.6
mg
mL�
1
tetr
ath
iafu
lval
ene
Pt
30
.2V
vs.
SC
E;
pH
7;
RT
n=
a;4
91mm
2n=a;
n=a;
n=
an=
a;n=a
acet
amin
op
hen
,
asco
rbat
e,u
rate
;
elec
tro
po
lym
eriz
ed
po
ly(p
hen
ol)
film
n=a
[12
4]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
12
6.8
U
Mel
do
lab
lue
carb
on
pas
te
20
.05
–0
.25
V
vs.
SC
E;
pH
7.9
;2
5� C
16
4mA
mm
ol�
1L
cm�
2;
0.7
8m
m2
n=a;
0–
2m
mo
lL�
1;
12
sec
n=
a;n=a
asco
rbat
e;
Mel
do
lab
lue
n=a
[20
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
8.5
U
tetr
ath
iafu
lval
ene=
tetr
acy
ano
qu
ino
-
dim
eth
ane
carb
on
pas
te
30
.15
Vv
s.
Ag=A
gC
l;
pH
7;
30� C
64
2n
Am
mo
l�1
L;
7m
m2
56mm
olL
�1
(S=N¼
3);
0–
0.6
mm
olL
�1;
90
sec
n=
a;9
0%
of
init
ial
acti
vit
y:
36
day
s(s
tora
ge
inbu
ffer
at4� C
)
n=
a;n=
am
ilk
,
yo
gh
urt
[12
5]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=a
tetr
ath
iafu
lval
ene
gra
ph
ite
n=
an=
a;n=
a;
n=
a
50
nA
mm
ol�
1L
;
n=
a
1mm
olL
�1;
0.0
01
–1
.2m
mo
lL�
1;
n=a
n=
a;n=a
n=
a;n=
aan
imal
cell
cult
ivat
ion
[90
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
60
–1
20
U
ind
op
hen
ol
der
ivat
ives
gra
ph
ite
on
Pt
n=
a0
.1–
0.4
Vv
s.
Ag=A
gC
l;
pH
5.7
;n=a
4–
20
8n
Am
mo
l�1
L;
2m
m2
n=a;
0–
16
mm
olL
�1;
n=a
30
–7
0%
of
init
ial
acti
vit
y:
30
det
erm
inat
ion
s;
80
%o
fin
itia
l
acti
vit
y:
2–
12
day
s
acet
amin
op
hen
,
asco
rbat
e,
crea
tin
ine,
glu
cose
,O
2,
ure
a,
ure
ate;
med
iato
r
n=a
[12
6]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
60
–1
20
U
ind
op
hen
ol
der
ivat
ives
gra
ph
ite
on
Pt
n=
a0
.2–
0.4
Vv
s.
Ag=A
gC
l;
pH
5.7
;n=a
1–
20
8n
Am
mo
l�1
L;
2m
m2
n=a;
0–
16
mm
olL
�1;
n=a
30
–6
9%
of
init
ial
acti
vit
y:
30
det
erm
inat
ion
s;
80
%o
fin
itia
l
acti
vit
y:
2–
12
day
s
acet
amin
op
hen
,
asco
rbat
e,
crea
tin
ine,
glu
cose
,
O2,
ure
a,u
reat
e;
med
iato
r
blo
od
[51
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=a
qu
ino
ne
gla
ssy
carb
on
3�
0.1
Vv
s.
Ag=A
gC
l;
pH
6;
25� C
70mA
mo
l�1
Lcm
�2;
0.0
7cm
25
0mm
olL
�1;
0.0
5–
1.5
mm
olL
�1;
n=a
>9
wee
ks
(sev
eral
det
erm
inat
ion
s,
sto
rag
ein
bu
ffer
at4� C
);n=
a
acet
amin
op
hen
,
asco
rbat
e,g
lyci
n,
O2;
low
po
ten
tial
yo
gh
urt
[67
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=a
qu
ino
ne
gla
ssy
carb
on=P
t
30
.5=�
0.1
V
vs.
Ag=
Ag
Cl;
pH
6;
25� C
0.3
5=5
0mA
mm
ol�
1L
cm�
2;
0.0
7=0
.03
14
cm2
50mm
olL
�1
(S=N¼
3);
0.0
5–
0.5=
0.0
2–
0.6
mm
olL
�1;
n=a
50
%o
fin
itia
l
acti
vit
y:>
4w
eek
s
(2d
eter
min
atio
ns
per
wee
k);
n=
a
acet
amin
op
hen
,
asco
rbat
e,g
lyci
n,
O2;
low
po
ten
tial
blo
od
[12
7]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
3(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
lo
f
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
ca-
tio
n
Ref
.2
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
16
U
tetr
ath
iafu
lval
ene
gla
ssy
carb
on
30
.17
Vv
s.
SC
E;
pH
7;
30� C
n=a;
9.6
mm
2n=
a;n=
a;4
0se
c6
0d
eter
min
atio
ns;
80
%o
fin
itia
l
acti
vit
y:
2m
on
ths
(sto
rag
ein
bu
ffer
at4� C
)
asco
rbat
e,O
2;
deo
xy
gen
ated
solu
tio
ns
n=
a[1
28
]
LO
D(n
oE
Cg
iven
);
Streptococcus
sp.;
0.1
74
–5
.22
U
met
hy
len
e-g
reen
carb
on
pas
te
n=
a0
.15
Vv
s.
Ag=A
gC
l;
pH
7;
25� C
50
.4mA
mm
ol�
1
Lcm
�2;
0.2
8m
m2
n=
a;0
–4=
0–
8m
mo
lL�
1;
30
sec
few
min
ute
s;
>2
month
s(s
tora
ge
dry
at4� C
)
asco
rbat
e;n=a
blo
od
[12
9]
LO
D(E
C1
.1.3
.2);
n=a;
n=a
tetr
ath
iafu
lval
ene
and
tetr
acy
ano
-
qu
ino
dim
eth
ane
salt
Pt
3n=
a;n=
a;n=a
0.2
24mA
mm
ol�
1L
;
n=a
0.1
mm
olL
�1;
0–
56
mm
olL
�1;
1.2
min
n=
a;n=
aac
etam
ino
ph
en,
asco
rbat
e,
ura
te;
n=
a
n=
a[1
30
]
LO
D(n
oE
Cg
iven
);
n=a;
25
mg
mL�
1te
trat
hia
fulv
alen
eca
rbo
n
film
2=
30
.16
Vv
s.
SC
E=
0.2
V
vs.
Ag=
Ag
Cl;
pH
7.3
5;
30� C
n=a;
12
.6=
28
.3m
m2
n=
a;n=
a;<
5se
c=se
ver
alm
inu
tes
sin
gle
use
;
n=
a
n=
a;n=
an=
a[1
31
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;1
0U
LO
D
(no
EC
giv
en);
Pediococcus
sp.;
2U
ph
enaz
ine
met
ho
sulf
ate,
NA
DH
in
solu
tio
n
Pt
2�
0.7
Vv
s.
Ag=A
gC
l;
pH
7;
30� C
n=a;
n=a
n=
a;n=
a;n=
an=
a;n=
ah
eav
ym
etal
s
alts
(hig
h
con
cen
trat
ion
s);
hea
vy
met
al
det
ecti
on
[59
]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostocmenteroides
(sic
!);
19
5U
;A
LT
(L-a
lan
ine
amin
o-
tran
sfer
ase,
EC
2.6
.1.2
);
po
rcin
eh
eart
;1
20
U
(en
zym
ere
acto
r)
tolu
idin
eb
lue
O,
NA
Dþ
carb
on
pas
te
2�
0.0
5V
vs.
Ag=A
gC
l;
pH
7;
25� C
n=a;
0.0
71
cm2
n=
a;0
.25
–4
mm
olL
�1;
n=
a
n=
a;n=
aP
yru
vat
e;
Co
imm
ob
iliz
atio
n
of
AL
T
n=
a[4
4]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;1
00mg
dia
ph
ora
se(E
C
1.6
.99
.-);Bacillus
stearothermophilus;
10mg
2-m
eth
yl-
1,4
-
nap
hth
oq
uin
on
e,
NA
Dþ
carb
on
pas
te
2�
0.1
5V
vs.
Ag=A
gC
l;
pH
8.5
;2
5� C
n=a;
0.0
9cm
2n=
a;n=
a;n=
an=
a;(s
tora
ge
inbu
ffer
at5� C
)
O2;
deo
xy
gen
ated
solu
tio
ns
n=
a[4
1]
L-L
DH
(EC
1.1
.1.2
7);
pig
mu
scle
;1
0U
glu
tam
ic-p
yru
vic
tran
sam
inas
e(E
C
2.6
.1.2
);p
orc
ine
hea
rt;
2U
bis
(ben
zo-
ph
eno
xaz
iny
l)
der
ivat
ive
of
tere
ph
talo
ic
acid
,N
AD
þin
solu
tio
n
gra
ph
ite
30
Vv
s.
Ag=A
gC
l;
pH
7.4
;n=a
n=a;
3.1
4m
m2
n=
a;n=
a;1
5se
cn=
a;n=
ael
ectr
oac
tive
sub
stan
ces,
hem
ato
crit
;
low
po
ten
tial
,
mem
bra
nes
wit
h
low
per
mea
bil
ity
blo
od
[43
]
N. Nikolaus, B. Strehlitz
electrodes were more frequently found in the sensitiv-
ity range below 10mA mmol�1 L cm�2.
Considering the biological recognition element,
neither the use of LOD seems to have any influence
on the sensitivities of the resulting sensors nor the
use of multi enzyme configurations with one excep-
tion of a multi enzyme set-up aiming for signal am-
plification [157]. The use of L-LDH results in a
tendency to higher sensitivities, and also, to a lesser
extent, whole cells and cell fractions. Using D-LDH
seems to produce sensors with lower sensitivities than
with L-LDH, possibly due to the slightly smaller
specific activity of the utilized D-LDH forms (from
Lactobacillus leichmanii or Staphylococcus epider-
midis, 150–500 U mg�1 protein) compared to L-LDH
(from various origins, 400–1200 U mg�1 protein) [211].
Whole cells or cell fractions as biological recogni-
tion elements lead to lactate biosensors with a sensi-
tivity distribution comparable to that of D-LDH.
The influence of the method of immobilization can
be seen in the comparison of entrapment and cova-
lent attachment. Using entrapment as immobilization
method seems to result in biosensors with higher sen-
sitivities per area compared to covalent attachment.
This is in accordance with many quotations in litera-
ture, e.g. [57, 108, 212, 213], stating a lower activity
of covalently bound enzymes due to conformational
changes or steric hindrances of the enzyme in the
course of immobilization. All other methods of im-
mobilization show minor effects on the sensitivity of
the sensor.
From these considerations it seems only possible to
give suggestions but no general advice for the con-
struction of amperometric biosensors for lactate. The
interaction of the different configurations concerning
working electrode material, biological recognition
element, and immobilization method needs thorough
optimization procedures in order to receive sensitive,
but also stable and selective biosensors.
Industrial products
Commercially available biosensor systems for the de-
tection of lactate can be purchased for medical pur-
poses, biotechnology, and food control. For overviews
concerning commercially available lactate biosensors
see Refs. [52, 214]. The following list (being not ex-
haustive) gives some examples of commercially avail-
able lactate biosensor devices. Amperometric lactate
biosensor systems for applications in (sports) medicineL-L
DH
(no
EC
giv
en);
ho
gm
usc
le;
4–
8U
NA
DH
ox
idas
e(n
o
EC
giv
en);Streptococcus
faecalis;
4–
8U
ph
enaz
ine
met
ho
sulf
ate,
NA
Dþ
in
solu
tio
n
gra
ph
ite
3n=a;
pH
8;
25� C
n=
a;n=
an=a;
n=a;
4m
in5
0%
of
init
ial
sen
siti
vit
y:
5h
;n=a
n=
a;n=
an=
a[2
1]
Hansenula
anomala
wh
ole
cell
s;0
.42
Um
g�
1
pas
te
var
iou
s
med
iato
rs,
sin
gle
and
mix
ed
carb
on
pas
te
20
.05
–0
.3V
vs.
SC
E;
pH
7.6
–7
.7;
25� C
14
–1
16mA
mm
ol�
1L
cm�
2;
0.2
8m
m2
n=a;
0–
6=8
mm
olL
�1
(fer
ricy
anid
e);
1–
2.1
min
(fer
ricy
anid
e)
70
%o
fin
itia
l
resp
on
se:
30
min
(in
bu
ffer
at2
5� C
);
90
%o
fin
itia
l
acit
vit
y:>
2m
on
ths
(sto
rag
ed
ryat
4� C
)
asco
rbat
e;n=
an=
a[1
09
]
Saccharomyces
cerevisiae
wh
ole
cell
s
ph
enaz
ine
met
ho
sulf
ate
carb
on
pas
te
30
Vv
s.
Ag=
Ag
Cl;
pH
7.2
;R
T
n=
a;6
.6m
m2
16
–2
1m
mo
lL�
1
(S=N¼
3);
0–
1m
mo
lL�
1
D-=
L-l
acta
te;
1m
in
1d
ay(6
0–
70
det
erm
inat
ion
s);
10
0–
85
%o
fin
itia
l
acit
vit
y:
1m
on
th
(sto
rag
eat
RT
)
asco
rbat
e;n=
ak
efir,
yo
gh
urt
[53
]
1El.Sys.T
wo
(2)
or
thre
e(3
)el
ectr
od
esy
stem
.2Ref.R
efer
ence
.3NAD
þN
ico
tin
amid
ead
enin
ed
inu
cleo
tid
e.4S=N
Sig
nal
ton
ois
era
tio
.5SCE
Sat
ura
ted
calo
mel
elec
tro
de.
6RT
Ro
om
tem
per
atu
re.
7Config.1
Co
nfi
gu
rati
on
of
elec
tro
de:
PM
S=
po
ly(p
yrr
ole
-2-c
arb
ox
yli
cac
id)=
enzy
me.
8Config.2
Co
nfi
gu
rati
on
of
elec
tro
de:
PM
S=p
oly
(4,4
0 -d
ihy
dro
xy
ben
zop
hen
on
e)=en
zym
e.9NADH
Nu
cleo
tin
eam
ide
aden
ine
din
ucl
eoti
de
(red
uce
dfo
rm).
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
4.
Co
mp
aris
on
of
set-
up
par
amet
ers
and
per
form
ance
dat
afo
ram
per
om
etri
cla
ctat
eb
iose
nso
rs;
con
du
ctin
gp
oly
mer
su
sed
asm
edia
tor
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
l
of
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
cati
on
Ref
.2
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
ssp
.
crem
oris;
23
–1
87
Um
g�
1
gra
ph
ite
pow
der
tolu
idin
eb
lue
Oan
dp
oly
-
eth
yle
nei
min
e,
NA
Dþ
3
carb
on
pas
te
3�
0.0
5V
vs.
Ag=A
gC
l;
pH
7;
n=a
n=
a;0
.05
3cm
23
0mm
olL
�1
(S=N
4¼
2);
0.0
5–
5m
mo
lL�
1;
n=
a
>7
0%
of
init
ial
acti
vit
y:
23
0
assa
ys;
40
%
of
init
ial
val
ue:
31
day
s(s
tora
ge
dry
at4� C
py
ruvat
e,D
L-�
-
hy
dro
xy
bu
tyri
c
acid
;n=
a
ferm
enta
tio
n
bro
th
[2]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
ssp
.
crem
oris;
n=
a
tolu
idin
eb
lue
Oan
dp
oly
-
eth
yle
nei
min
e,
NA
Dþ
carb
on
pas
te
3�
0.0
5V
vs.
Ag=A
gC
l;
pH
7;
n=a
n=
a;n=
a0
.7m
mo
lL�
1;
0–
10
mm
olL
�1;
n=
a;
20
ho
fco
nti
nu
ou
s
op
erat
ion
(dec
reas
ing
resp
on
se;
cali
bra
tio
n
nec
essa
ry)
n=
a
n=a;
n=
afe
rmen
tati
on
bro
th
[11
3]
D-L
DH
(EC
1.1
.1.2
8);
Leuconostoc
mesenteroides
;1
50
U
po
lyet
hy
len
e-
imin
e,N
AD
þca
rbo
n
pas
te
3�
0.0
5V
vs.
Ag=A
gC
l;
pH
7;
n=a
n=
a;n=
an=
a;
0.0
2–
0.3
mm
olL
�1;
n=
a
>2
00
assa
ys;
n=
aac
etam
ino
ph
en,
asco
rbat
e;
elec
tro
po
lym
eriz
ed
o-p
hen
yle
ne-
dia
min
ela
yer
ferm
enta
tio
n
bro
th
[13
2]
L-L
DH
(EC
1.1
.1.2
7);
Bacillus
stearothermophilus;
n=a
po
lyan
ilin
e,
NA
Dþ
in
solu
tio
n
gla
ssy
carb
on
20
.05
Vv
s.
SC
E5;
pH
7;
35� C
n=
a;0
.38
cm2
n=
a;
0.4
–0
.55
mo
lL�
1;
n=
a
24
ho
fco
nti
nu
ou
s
op
erat
ion
at4� C
;
n=
a
n=a;
n=
an=
a[1
33
]
L-L
DH
(EC
1.1
.1.2
7);
Bacillus
stearothermophilus;
n=a
po
lyan
ilin
e,
NA
Dþ
in
solu
tio
n
gla
ssy
carb
on
30
.05=
0.1
V
vs.
SC
E;
pH
7.1
;3
5� C
n=
a;0
.38
cm2
n=
a;n=
an=
an=
a;n=a
n=a;
n=
an=
a[1
34
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
1m
gm
L�
1p
oly
anil
ine=
po
ly(a
cry
lic
acid
),N
AD
þ
Au
30
.6V
vs.
Ag=A
gC
l;
pH
7;
30� C
n=
a;1
.5cm
2n=
a;n=
a;n=
a9
0%
of
init
ial
acti
vit
y:
12
h
con
tin
uo
us
op
erat
ion
atR
T6
(30� C
);9
0%
of
init
ial
acti
vit
y:
1m
on
th(s
tora
ge
at4� C
)
n=a;
n=
an=
a[1
35
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
17
00
U
po
ly(o
-
ph
eny
lene-
dia
min
e),
NA
Dþ
carb
on
pas
te
30
.15
Vv
s.
Ag=A
gC
l;
pH
9.5
;n=a
0.1
6mA
mm
ol�
1L
;
50
.3m
m2
0.7
5mm
olL
�1;
1–
40mm
olL
�1;
35
sec
n=
a;n=a
n=a;
n=
an=
a[1
36
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
0.1
mg
po
lyp
yrr
ole
-
po
lyv
iny
l-
sulp
ho
nat
e,
NA
Dþ
in
solu
tio
n
n=
an=a
0.2
Vv
s.
pse
ud
o
refe
ren
ce
elec
tro
de;
pH
7.2
;R
T
n=
a;n=
an=
a;
0.5
–6
mm
olL
�1;
40
sec
n=
a;2
wee
ks
(sto
rag
eat
4to
10� C
)
asco
rbat
e,
citr
ate,
glu
cose
,
glu
tam
ate;
n=a
n=
a[1
37
]
N. Nikolaus, B. Strehlitz
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=a
po
lyan
ion
do
ped
po
ly(p
yrr
ole
)
film
pla
tin
ized
po
lym
er
30
.4V
vs.
Ag=A
gC
l;
pH
7;
37� C
5mA
mm
ol�
1
Lcm
�2;
3.1
4m
m2
5mm
olL
�1;
0–
2=
0–
16=
0–
30
mm
olL
�1;
20
–3
0se
c
50
%o
fin
itia
l
acti
vit
y:
50
day
s
of
con
tin
uo
us
op
erat
ion
;2
yea
rs
(sto
rag
ed
ryat
�1
8� C
),1
yea
r
(sto
rag
eat
RT
)
n=a;
n=
an=
a[5
7]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=a
po
lyim
ine
ion
-
exch
ang
e
po
lym
er-g
el
Pt
3n=
a;p
H7
;
n=
a
n=
a;n=
an=
a;
0–
5=
0–
20
mm
olL
�1
(FIA
7);
45
–6
0se
c
>4
0d
ays
of
con
tin
uo
us
op
erat
ion
;
mo
nth
s–
sever
al
yea
rs(s
tora
ge
dry
at4
–2
5� C
)
n=a;
n=
an=
a[1
38
]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
10
0U
po
lyp
yrr
ole
Pt
30
.8V
vs.
SC
E;
n=
a
n=
a
0.6
nA
mm
ol�
1L
;
n=
a
n=
a;n=
a;n=
an=
a;n=a
n=a;
n=
an=
a[1
39
]
LO
D(n
oE
Cg
iven
);
n=a;
n=a
po
lyp
yrr
ole
Pt
30
.2=
0.5
Vv
s.
Ag=A
gC
l;
pH
7;
n=a
n=
a;n=
a0
.5m
mo
lL�
1;
n=
a;
5–
10
sec
n=
a;(s
tora
ge
in
bu
ffer
at4� C
)
asco
rbat
e,
fru
cto
se,
glu
cose
,O
2,
ure
a;re
do
x
med
iato
r
n=
a[9
9]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;1
–4
.5U
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
0.1
–0
.8U
po
lyan
ilin
e,
NA
Dþ
in
solu
tio
n
Ind
ium
tin
ox
ide
30
.2–
0.2
5V
vs.
Ag=
Ag
Cl;
pH
7;
RT
5.5
–3
8.5mA
mm
ol�
1L
;
n=
a
0.0
5to
1m
mo
lL�
1;
0.1
–1
to
1–
4m
mo
lL�
1;
n=
a
n=
a;5
0%
of
init
ial
acti
vit
y:
2–
3w
eek
s(s
tora
ge
at4
–1
0� C
)
n=a;
n=
an=
a[1
40
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;4
.5U
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
0.1
U
po
lyan
ilin
e,
NA
Dþ
in
solu
tio
n
Ind
ium
tin
ox
ide
30
.2–
0.2
5V
vs.
Ag=
Ag
Cl;
pH
7;
RT
n=
a;1
cm2
0.0
5to
1m
mo
lL�
1;
0.1
–1
to
1–
4m
mo
lL�
1;
n=
a
n=
a;2
1d
ays
(sto
rag
eat
4–
10� C
)
pH
,te
mp
erat
ure
;
n=a
n=
a[1
41
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;
16
–8
0U
mg�
1ca
rbo
n
pas
teG
luta
mic
py
ruv
ic
tran
sam
inas
e(G
TP
)
(EC
2.6
.1.2
);p
igh
eart
;
0–
5U
mg�
1ca
rbo
np
aste
po
ly(o
-
ph
eny
lene-
dia
min
e),
NA
Dþ
carb
on
pas
te
30
–0
.15
Vv
s.
Ag=A
gC
l;
pH
9.5
;n=a
0.5
6–
1.1mA
mm
ol�
1L
;
7.1
mm
2
0.0
3–
0.6mm
olL
�1;
0.5
–7
7mm
olL
�1=
0.5
–8
.5mm
olL
�1;
40
sec=
80
sec
1d
ay(1
0
det
erm
inat
ion
s);
40
–6
0%
of
init
ial
acti
vit
y:
over
nig
ht
(sto
rag
e
inbu
ffer
)
asco
rbat
e,u
rate
,
L-c
yst
ein
e,
glu
tath
ion
e,
par
acet
amo
l;
cover
age
by
po
ly(o
-
amin
op
hen
ol)
film
,
zero
po
ten
tial
cid
er[3
2]
1El.Sys.
Tw
o(2
)o
rth
ree
(3)
elec
tro
de
syst
em.
2Ref.
Ref
eren
ce.
3NAD
þN
ico
tin
amid
ead
enin
ed
inu
cleo
tid
e.4S=N
Sig
nal
ton
ois
era
tio
.5SCE
Sat
ura
ted
calo
mel
elec
tro
de.
6RT
Ro
om
tem
per
atu
re.
7FIA
Flo
win
ject
ion
anal
ysi
s.
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
5.
Co
mp
aris
on
of
set-
up
par
amet
ers
and
per
form
ance
dat
afo
ram
per
om
etri
cla
ctat
eb
iose
nso
rs;
cofa
cto
rsu
sed
alo
ne,
wit
ho
ut
add
itio
nal
med
iato
rs
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
lo
f
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
ca-
tio
n
Ref
.2
L-L
DH
(EC
1.1
.1.2
7);
bov
ine
hea
rt;
37
5U
NA
Dþ
3P
t2
0.8
75
Vv
s.
SC
E;
pH
8.8
;
n=a
1.2
nAmm
ol�
1L
;
0.2
mm
23mm
olL
�1;
0–
20
0mm
olL
�1;
3–
7m
in
n=
a;n=
an=
a;n=
an=
a[2
6]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
n=
a
NA
Dþ
in
solu
tio
n
Au
20
.6V
vs.
Au
;
pH
7;
21� C
8.6mA
mo
l�1;
n=
a
28mm
olL
�1;
0.1
–2
mm
olL
�1;
n=
a
80
day
sin
sem
i-
con
tin
uo
us
op
erat
ion
20
hp
erd
ay,
5d
ays
per
wee
k;
2m
on
ths
(sto
rag
e
at4� C
)
n=
a;n=
am
ilk
,
crea
m,
curd
,
butt
erm
ilk,
sour
crea
m
[14
2]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
6%
(w=
w)
NA
Dþ
carb
on
pas
te
30
.8V
vs.
Ag=
Ag
Cl;
pH
7.4
;R
T4
n=
a;7
.1m
m2
0.1
mm
olL
�1
(S=N¼
3);
–5;
n=
a
n=
a;n=
an=
a;n=
an=
a[1
43
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;1
%
(w=
w)
insc
reen
pri
nti
ng
ink
NA
Dþ
carb
on
scre
en
pri
nti
ng
ink
30
.35
Vv
s.
Ag=
Ag
Cl;
pH
8.2
;R
T
13
.8–
65
.0n
A
mm
ol�
1L
;
n=
a
0.1
1m
mo
lL�
1;
0–
9.1
mm
olL
�1;
15
sec
n=
a;>
40
day
s
(sto
rag
ein
dry
nit
rog
enat
mo
sph
ere
at4� C
)
n=
a;lo
wp
ote
nti
aln=
a[5
0]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
n=
a
NA
Dþ
gla
ssy
carb
on
30
.8V
vs.
SC
E;
pH
9;
25� C
n=
a;6
.9m
m2
n=
a;n=
a;n=
an=
a;5
0%
of
init
ial
acti
vit
y:
3w
eek
s
(sto
rag
ein
bu
ffer
at4� C
)
py
ruvat
e(i
nh
ibit
or
of
reac
tio
n);
n=
a
n=
a[1
44
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
6%
(w=
w)
NA
Dþ
gra
ph
ite-
epo
xy
30
.7V
vs.
Ag=
Ag
Cl;
pH
7.4
;R
T
n=
a;7
.1m
m2
80mm
olL
�1
(S=N¼
3,
bat
ch),
0.5
mm
olL
�1
(FIA
6);
0.0
8–
2m
mo
lL�
1
(bat
ch);
10
sec
40
%o
fin
itia
l
acti
vit
y:
12
h,
but
ren
ewab
leb
y
po
lish
ing
:>
90
%
of
init
ial
acti
vit
y:
>1
6d
ays;
n=
a
acet
amin
op
hen
,
asco
rbat
e,u
rate
;
pre
ven
tio
no
f
fou
lin
gef
fect
s:
ren
ewab
lech
arac
ter
of
the
elec
tro
de
n=
a[1
45
]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
n=
a
py
rro
lo-
qu
ino
lin
e-
qu
ino
ne,
NA
Dþ
in
solu
tio
n
Au=P
t=g
lass
y
carb
on=
py
roly
tic
gra
ph
ite
20
.2V
vs.
SC
E;
pH
8.1
;2
5� C
n=
a;0
.07
1cm
20
.05
mm
olL
�1;
n=
a;7
–1
0se
c
n=
a;5
0%
of
init
ial
acti
vit
y:
2m
on
ths
(sto
rag
ein
bu
ffer
at4� C
)
acet
amin
op
hen
,
asco
rbat
e,u
ric
acid
;
elec
tro
po
lym
eriz
ed
1,2
-,1
,3-,
1,4
-dia
min
ob
enze
ne=
4-a
min
o-b
iph
eny
l
n=
a[1
46
]
L-L
DH
(no
EC
giv
en);
bov
ine
hea
rt;
n=
a
NA
Dþ
gla
ssy
carb
on
20
.75=0
.45
Vv
s.
Ag=
Ag
Cl;
pH
8;
25� C
n=
a;7
.1m
m2
4mm
olL
�1=
80mm
olL
�1
(rea
gen
tles
s)
(S=N¼
1);
–;
�1
2–
15
min
85
–8
0%
of
init
ial
resp
on
se:
sev
eral
ho
urs
of
con
tin
uo
us
op
erat
ion
;n=
a
n=
a;n=
an=
a[1
47
]
L-L
DH
(no
EC
giv
en);
rab
bit
mu
scle
;n=
a
NA
Dþ
gla
ssy
carb
on
30
.7V
vs.
SC
E;
pH
9;
n=
a
n=
a;2
.9cm
2n=
a;n=
a;n=
an=
a;5
0%
of
init
ial
acti
vit
y:
3w
eek
s
(sto
rag
ein
bu
ffer
at4� C
)
n=
a;n=
an=
a[1
48
]
N. Nikolaus, B. Strehlitz
LD
H;
n=
a;n=a
py
rro
lo-
qu
ino
lin
e
qu
ino
ne-
NA
Dþ
Au
20
.1V
vs.
SC
E;
pH
8;
n=
a
n=
a;ca
.0
.2cm
2n=a;
n=a;
n=a
<5
%d
egra
dat
ion
per
ho
ur
in
con
tin
uo
us
op
erat
ion
;n=
a
n=
a;n=
an=a
[14
9]
L-L
DH
(cyto
chro
me)
(EC
1.1
.2.3
);
Hansenula
anomala
;
3.6
U
ferr
icy
to-
chro
me
c
Au=
gla
ssy
carb
on=
Pt
30
.5V
vs.
SC
E;
pH
7.2
;n=
a
n=
a;7
mm
2n=a;
0–
6m
mo
lL�
1=
0–
7m
mo
lL�
1=
0.0
5–
6m
mo
lL�
1;
1m
in
>1
mo
nth
(20
0
assa
ys,
sto
rag
e
inbu
ffer
at
4� C
);n=a
n=
a;n=
an=a
[15
0]
L-L
DH
(cyto
chro
me)
(no
EC
giv
en)
bak
er’s
yea
st;
n=
a
aso
lect
in,
cyto
chro
me
c
carb
on
pas
te
30
.15
Vv
s.
SC
E;
pH
7.4
;2
3� C
n=
a;7
.07
mm
21mm
olL
�1
(3�
val
ue)
;
8–
80
0mm
olL
�1;
75
sec
n=a;
70
%o
f
init
ial
acti
vit
y:
5w
eek
s(s
tora
ge
inbu
ffer
at4� C
)
asco
rbat
e,u
rate
;
low
po
ten
tial
n=a
[15
1]
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=
a
FA
D7
Pt
2n=
a;n=a;
n=a
n=
a;n=
an=a;
n=a;
n=a
n=a;
n=
aac
etam
ino
ph
en,
amin
og
uan
idin
e,
asco
rbat
e,en
zym
es
(cat
alas
e,p
ero
xid
ase)
,
glu
cose
,g
luta
thio
ne;
nu
cleo
po
rean
d
cell
ulo
seac
etat
e
mem
bra
nes
blo
od
[15
2]
D-L
DH
(no
EC
giv
en);
Staphylococcus
epidermidis
;5
UL
OD
(no
EC
giv
en);
Pediococcus
sp.;
5U
;
per
ox
idas
e(n
oE
C
giv
en);
ho
rser
adis
h;
75
U
NA
Dþ
in
solu
tio
n
Pt
2�
0.6
5V
vs.
Ag=
Ag
Cl;
pH
8.6
;3
7� C
12
.21
7n
A
mm
ol�
1L
(D-=
L-l
acta
te);
0.5
mm
2
0.0
25
mm
olL
�1;
0.0
5–
3m
mo
lL�
1;
2m
in
5m
on
ths
(18
0–
20
0
det
erm
inat
ion
s,
sto
rag
ein
bu
ffer
);
2–
5m
on
ths
(sto
rag
e
dry
at�
15� C
)
elec
tro
acti
ve
sub
stan
ces;
Tefl
on
mem
bra
ne
tom
ato
pro
du
cts
[1]
L-L
DH
(EC
1.1
.1.2
7);
bov
ine
hea
rt;
n=
a
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
n=
a
NA
DH
8
inso
luti
on
Pt
n=
an=
a;p
H7
.4;
30� C
n=
a;n=
a0
.08mm
olL
�1
(S=N¼
5);
0.0
8–
8mm
olL
�1;
n=a
10
%d
evia
tio
no
f
aver
age
val
ue:
10
day
s(2
0
det
erm
inat
ion
s
per
day
);n=
a
n=
a;n=
am
ilk
[15
3]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;0
.4U
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
1.8
U
NA
DH
inso
luti
on
Pt
2�
0.7
Vv
s.
Ag=
Ag
Cl;
pH
7;
30� C
n=
a;0
.03
1m
m2
3n
mo
lL�
1;
0.0
25
–1=
3–
20
0m
mo
lL�
1;
n=a
80
%o
fin
itia
l
acti
vit
y:
2w
eek
s
(20
det
erm
inat
ion
s
per
day
);n=
a
n=
a;n=
afe
rmen
-
tati
on
bro
th
[15
4]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;2
0U
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
8U
NA
DH
inso
luti
on
Pt
2�
0.7
Vv
s.
Ag=
Ag
Cl;
pH
7;
30� C
n=
a;0
.03
1m
m2
20
nm
olL
�1;
20
–3
00
nm
olL
�1;
n=a
40
0d
eter
min
atio
ns;
80
%o
fin
itia
l
acti
vit
y:
6w
eek
s
(sto
rag
ein
bu
ffer
at4� C
)
n=
a;n=
afe
rmen
-
tati
on
bro
th
[15
5]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;5
U
LO
D(E
C1
.13
.12
.4);
Pediococcus
sp.;
5U
NA
DH
inso
luti
on
Pt
2�
0.7
Vv
s.
SC
E;
pH
7=
9;
30� C
n=
a;0
.03
mm
2n=a;
n=a;
n=a
>8
h;>
15
day
s
(sto
rag
ein
bu
ffer
or
dry
at4� C
)
n=
a;n=
ah
eav
y
met
al
det
ecti
on
[60
]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
5(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)
of
enzy
me
use
din
sen
sor
pre
par
atio
n
Med
iato
r,
cofa
cto
r
Mat
eria
lo
f
wo
rkin
g
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;
tem
per
atu
re
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
g
elec
tro
de
Low
erd
etec
tio
n
lim
it;
lin
ear
ran
ge;
resp
on
seti
me
Op
erat
ion
al
stab
ilit
y;
sto
rag
e
stab
ilit
y
Inte
rfer
ence
;
pro
tect
ion
agai
nst
inte
rfer
ence
Ap
pli
cati
on
Ref
.2
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;0
.1–
1U
LO
D(n
oE
Cg
iven
);
Pediococcus
sp.;
0.1
–1
U
NA
Dþ
,
NA
DH
Pt
2�
0.7
Vv
s.
Ag=
Ag
Cl;
pH
7;
30� C
n=
a;n=
a1
0n
mo
lL�
1(w
ith
recy
clin
g)=
10mm
olL
�1
(wit
ho
ut
recy
clin
g);
n=
a;1
0se
c
n=
a;n=
ap
yru
vat
e;n=
ab
loo
d,
hea
vy
met
al
det
ecti
on
[15
6]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;n=
aL
OD
(no
EC
giv
en);
Pediococcus
sp.;
n=
a
NA
DH
inso
luti
on
Pt
n=
an=a;
pH
7.4
;
30� C
n=
a;0
.06
cm2
5n
mo
lL�
1(S=N¼
2);
0.0
05
–0
.5mm
olL
�1;
30
sec
>2
wee
ks
(10
det
erm
inat
ion
s
per
day
,st
ora
ge
inbu
ffer
at
4� C
);n=a
n=a;
n=
a;n=
a[3
8]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;2
U
dia
ph
ora
se(n
oE
C
giv
en);Bacillus
stearothermophilus;
0.4
U
NA
DH
inso
luti
on
Pt
20
.25
Vv
s.
Ag=
Ag
Cl;
pH
7;
22� C
n=
a;n=
a0
.5mm
olL
�1
(3�
val
ue)
;0
.00
1–
1m
mo
lL�
1;
40
sec
n=
a;n=
an=a;
n=
a;n=
a[4
9]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;7
0U
flav
inre
du
ctas
e(n
oE
C
giv
en);Escherichia
coli
;
21
U
rib
ofl
avin
and
NA
Dþ
inso
luti
on
gla
ssy
carb
on
3�
0.1
Vv
s.
SC
E;
pH
8.8
;
20� C
11
.75
mA
mo
l�1
Lcm
�2;
19
.6m
m2
1mm
olL
�1;
0–
23mm
olL
�1;
n=
a
n=
a;fe
wd
ays
(sto
rag
ein
bu
ffer
at4� C
)
acet
amin
op
hen
,
asco
rbat
e,u
rate
;
low
po
ten
tial
n=
a[3
1]
L-L
DH
(EC
1.1
.1.2
7);
rab
bit
mu
scle
;
3.3
4UmL
�1;
py
ruvat
eo
xid
ase
(EC
1.2
.3.3
);Aerococcus
viridans;
1.4
0UmL
�1;
sali
cyla
teh
yd
rox
yla
se
(EC
1.1
4.1
3.1
);
Pseudomonassp
;
0.5
6UmL
�1;
NA
Dþ
in
solu
tio
n
Pt
2n=a;
pH
7.5
;
23� C
3.0
5–
27
6.3
5mA
mm
ol�
1L
;
0.2
mm
2
4.3mm
olL
�1
(S=N¼
3);
n=
a;2
sec
n=
a;5
0%
of
init
ial
resp
on
se:
11
day
s(s
tora
ge
inbu
ffer
at4� C
)
elec
tro
acti
ve
sub
stan
ces;
Tefl
on
mem
bra
ne
hea
lth
y
sup
ple
men
ts,
sod
a,sp
ort
dri
nk
s,
yo
gh
urt
mil
k
[15
7]
1El.Sys.
Tw
o(2
)o
rth
ree
(3)
elec
tro
de
syst
em.
2Ref.
Ref
eren
ce.
3NAD
þN
ico
tin
amid
ead
enin
ed
inu
cleo
tid
e.4RT
Ro
om
tem
per
atu
re.
5–
No
nex
iste
nt.
6FIA
Flo
win
ject
ion
anal
ysi
s.7FAD
Fla
vin
aden
ine
din
ucl
eoti
de.
8NADH
Nic
oti
nam
ide
aden
ine
din
ucl
eoti
de
(red
uce
dfo
rm).
N. Nikolaus, B. Strehlitz
Table
6.
Co
mp
aris
on
of
set-
up
par
amet
ers
and
per
form
ance
dat
afo
ram
per
om
etri
cla
ctat
eb
iose
nso
rs;
no
med
iato
ru
sed
or
no
dat
ag
iven
(n=
a)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)o
fen
zym
eu
sed
inse
nso
rp
rep
arat
ion
Med
iato
r,co
fact
or
Mat
eria
lo
fw
ork
ing
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;te
mp
erat
ure
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
gel
ectr
od
e
Low
erd
etec
tio
nli
mit
;li
nea
rra
ng
e;re
spo
nse
tim
e
Op
erat
ion
alst
abil
ity
;st
ora
ge
stab
ilit
y
Inte
rfer
ence
;p
rote
ctio
nag
ain
stin
terf
eren
ce
Ap
pli
cati
on
Ref
.2
L-L
DH
(cy
toch
rom
e)(E
C1
.1.2
.3);
Hansenula
anomala
;n=
a
–g
lass
yca
rbo
n3
�0
.1–
0.2
Vv
s.S
CE
3;
pH
7;
n=a
n=
a;5
mm
2n=a;
0–
0.3=0
.5m
mo
lL�
1;
1–
1.5
min
90
%re
pro
du
cib
ilit
y:
2–
3d
ays
(50
assa
ys
per
day
);n=a
asco
rbat
e;lo
wp
ote
nti
alce
llcu
ltu
refl
uid
s[1
58
]
L-L
DH
(cy
toch
rom
e)(E
C1
.1.2
.3);
Hansenula
anomala
;n=
a
–g
rap
hit
e3
0.0
4–
0.0
6V
vs.
Ag=
Ag
Cl;
pH
7;
25� C
n=
a;1
5.9
mm
2n=a;
n=
a;n=
a8
8%
of
init
ial
sen
siti
vit
y:
4d
ays,
32
%o
fin
itia
lse
nsi
tiv
ity
:7
day
s(4
ho
fo
per
atio
np
erd
ay,
sto
rag
ein
bu
ffer
at4� C
);n=
a
ox
yg
en;
deo
xy
gen
ated
solu
tio
ns
n=a
[15
9]
LO
D(E
C1
.1.3
.2);
Aerococcusviridans;
0.2
34
U
–P
t3
0.6
5V
vs.
Ag=A
gC
l;p
H7
;R
T4
30
0�
10
nA
mm
ol�
1L
;0
.43�
0.0
3m
m2
(det
erm
ined
acti
ve
area
)
2mm
olL
�1;
0.0
02
–1
mm
olL
�1;
21
sec
n=a;
n=a
acet
amin
op
hen
,as
corb
ate,
ura
te;
elec
tro
syn
thes
ized
bil
ayer
mem
bra
nes
mil
kan
dy
og
hu
rt[1
60
]
LO
D(E
C1
.1.3
.2);
Aerococcusviridans;
n=
a
–P
t3
n=
a;p
H7
;R
T3
0n
Am
mo
l�1
Lm
m�
2;
0.2
5m
m2
n=a;
0.0
5–
15
mm
olL
�1;
<1
5se
c
4w
eeks
of
conti
nuous
oper
atio
nin
bovin
ese
rum
;>
2yea
rs(s
tora
ge
at4� C
)
acet
amin
op
hen
;n
ocr
oss
talk
bec
ause
of
cata
lase
top
lay
er
blo
od
[16
1]
LO
D(n
oE
Cg
iven
);Aerococcusviridans;
20
0–
14
.00
0U
mL�
1
–A
un=a
0.7
Vv
s.A
g=A
gC
l;p
H7
;n=a
n=
a;7
mm
2n=a;
n=
a;n=
an=a;
n=a
n=
a;n=
an=a
[16
2]
LO
D(n
oE
Cg
iven
);Aerococcusviridans;
22
Um
L�
1
–P
t3
0.6
5V
vs.
Ag=A
gC
l;p
H7
.4;
25� C
n=
a;n=
a0
.05
mm
olL
�1;
0–
0.1
mm
olL
�1;
70
sec
n=a;
n=a
–;
dif
fere
nti
alm
easu
rem
ents
tom
ato
pas
te,
bab
yfo
od
[58
]
LO
D(n
oE
Cg
iven
);Aerococcusviridans,
ran
do
mm
uta
gen
esis
;0
.2UmL
�1
–P
t3
0.7
Vv
s.A
g=A
gC
l;p
H7
;2
4� C
n=
a;5
mm
2n=a;
n=
a;2
0se
cn=a;
n=a
n=
a;n=
an=a
[16
3]
LO
D(E
C1
.13
.12
.4);
Mycobacterium
smegmatis;
n=a
–P
t2
n=
a;p
H7
;2
0� C
n=
a;1
76
mm
2n=a;
0–
10
mm
olL
�1;
1m
inn=a;
n=a
n=
a;n=
an=a
[16
4]
LO
D(E
C1
.13
.12
.4);
Mycobacterium
smegmatis;
15
U
–P
t3
n=
a;p
H7
.2;
19� C
n=
a;n=
a8mm
olL
�1;
8–
80
0mm
olL
�1;
3–
4m
in
97
%o
fin
itia
lac
tiv
ity
:1
2h
of
con
tin
uo
us
op
erat
ion
inp
lasm
a;8
8%
of
init
ial
acti
vit
y:
15
day
s(s
tora
ge
inb
uff
erat
4� C
)
albu
min
,as
corb
ate,
Ca2
þ,
Mg
2þ
,o
xal
ate;
n=
a
blo
od
[70
]
LO
D(E
C1
.13
.12
.4);
Mycobacterium
smegmatis;
1.5
–2
.51
Um
L�
1
solu
tio
n
–P
tn=a
n=
a;p
H5
.6–
6;
8–
34
.5� C
n=
a;n=
an=a;
1.5
–1
8.7
5m
mo
lL�
1
(lo
g–
log
scal
e)n=
a
n=a;
sev
eral
wee
ks
(sto
rag
eo
fen
zym
eso
luti
on
at0� C
)
n=
a;n=
an=a
[16
5]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
6(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)o
fen
zym
eu
sed
inse
nso
rp
rep
arat
ion
Med
iato
r,co
fact
or
Mat
eria
lo
fw
ork
ing
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;te
mp
erat
ure
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
gel
ectr
od
e
Low
erd
etec
tio
nli
mit
;li
nea
rra
ng
e;re
spo
nse
tim
e
Op
erat
ion
alst
abil
ity
;st
ora
ge
stab
ilit
y
Inte
rfer
ence
;p
rote
ctio
nag
ain
stin
terf
eren
ce
Ap
pli
cati
on
Ref
.2
LO
D(E
C1
.13
.12
.4);
Mycobacterium
smegmatis;
30
U
n=
an=a
n=a
n=
a;p
H6
;2
5� C
n=a;
n=a
n=a;
n=a;
n=
an=
a;>
2m
on
ths,
>5
00
det
erm
inat
ion
s,5
0%
of
init
ial
acti
vit
y:
10
day
s
ph
osp
hat
ean
do
ther
anio
ns
n=
a[6
1]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
1.0
15
Um
g�
1p
aste
–ca
rbo
nce
ram
ic3
0.5
Vv
s.S
CE
;p
H7
;R
T
n=a;
n=a
n=a;
n=a;
n=
an=
a;3
wee
ks
n=
a;n=
an=
a[1
66
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
20
0U
–ca
rbo
np
aste
30
.6V
vs.
Ag=
Ag
Cl;
pH
7;
24� C
21mA
mm
ol�
1L
cm�
2;
3.5
mm
21
0mm
olL
�1
(S=N
5¼
3);
0.0
75
–1
mm
olL
�1;
20
–6
0se
c
56
%o
fin
itia
lac
tiv
ity
:2
40
ho
fco
nti
nu
ou
so
per
atio
n;
80
%o
fin
itia
lac
tiv
ity
:>
5m
on
ths
(sto
rag
efr
eeze
dri
edat
4� C
)
n=
a;n=
an=
a[1
67
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
20
0U
mL�
1
–ca
rbo
np
aste
30
.8V
vs.
Ag=
Ag
Cl;
pH
7;
24� C
15
.59�
0.7
2mA
mm
ol�
1L
;3
.5m
m2
10mm
olL
�1
0.0
75
–1
mm
olL
�1;
20
–6
0se
c
56
%o
fin
itia
lac
tiv
ity
:2
40
ho
fco
nti
nu
ou
so
per
atio
n;>
5m
on
ths
(sto
rag
efr
eeze
dri
edat
amb
ien
th
um
idit
yan
dR
T)
n=
a;n=
an=
a[1
68
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
4U
–P
d=
Au
-m
od
ified
carb
on
pas
te=
Pt
20
.6V
vs.
Ag=
Ag
Cl;
pH
7;
25
–3
7� C
15
nA
mm
ol�
1L
;0
.2m
m2
0.1
mm
olL
�1
0.0
1–
2m
mo
lL�
1=
0.6
–4
0m
mo
lL�
1=
0.1
–2
0m
mo
lL�
1;
15
sec
85
%o
fin
itia
lse
nsi
tiv
ity
:1
5d
ays,
>2
00
0d
eter
min
atio
ns;
>1
yea
r(s
tora
ge
of
mem
bra
nes
dry
at�
20� C
),4
0d
ays
atR
T,
20
day
sat
40� C
–;
dif
fusi
on
lim
itat
ing
mem
bra
nes
blo
od
[16
9]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
5.5
U
–p
lati
niz
edg
rap
hit
e2
0.3
Vv
s.A
g=
Ag
Cl;
pH
7;
n=
a
1.7
1mA
mm
ol�
1L
;0
.17
cm2
10mm
olL
�1;
0.0
2–
4m
mo
lL�
1;
10
–4
5se
c
n=
a;3
mo
nth
s(s
tora
ge
inbu
ffer
at5� C
=d
ryin
ph
osp
hat
esa
ltat
RT=
dry
inp
ho
sph
ate-
sod
ium
azid
esa
ltm
ixtu
reat
RT
)
acet
amin
op
hen
,as
corb
ate,
ura
te;
nafi
on
lay
er,
low
po
ten
tial
mil
k,
sou
rcr
eam
,y
og
hu
rt
[17
0]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
5.5
U
–p
lati
niz
edg
rap
hit
e2
0.3
Vv
s.A
g=
Ag
Cl;
pH
7;
n=
a
2.9
4mA
mm
ol�
1L
;0
.17
cm2
13mm
olL
�1;
0.0
26
–1
.7m
mo
lL�
1;
10
–5
0se
c
n=
a;>
80
day
s(s
tora
ge
inp
ho
sph
ate-
azid
eat
4� C
)
acet
amin
op
hen
,as
corb
ate,
ura
te;
nafi
on
lay
er,
low
po
ten
tial
mil
k,
sou
rcr
eam
,w
ine,
yo
gh
urt
[73
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
66
U–
pla
tin
ized
gra
ph
ite
scre
enp
rin
tin
gin
k
30
.35
Vv
s.A
g=
Ag
Cl;
pH
7;
30� C
n=a;
27
.5m
m2
n=a;
n=a;
n=
an=
a;2
00
day
s(s
tora
ge
at2
5� C
)n=
a;n=
an=
a[1
71
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
0.1
5U
–P
t2
n=
a;p
H7
;2
8� C
7.2�
0.1
nA
mm
ol�
1L
;7
.1m
m2
n=a;
n=a;
n=
a8
6%
of
init
ial
sen
siti
vit
y:
2d
ays
of
con
tin
uo
us
op
erat
ion
;6
0%
of
init
ial
sen
siti
vit
y:
13
0d
ays
(sto
rag
ein
bu
ffer
at4� C
)
acet
amin
op
hen
,as
corb
ate,
ura
te;
bil
ayer
mem
bra
ne
tom
ato
juic
e[1
72
]
N. Nikolaus, B. Strehlitz
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
2.1
6U
–P
t2
�0
.65
Vv
s.A
g=
Ag
Cl;
pH
7.4
;2
1� C
n=a;
3.1
mm
25
0mm
olL
�1;
0.2
–1
8m
mo
lL�
1;
1–
3m
in
92
%o
fin
itia
lre
spo
nse
:5
day
so
fco
nti
nu
ou
so
per
atio
nin
stan
dar
dso
luti
on=
30
det
erm
inat
ion
sin
wh
ole
blo
od
;n=a
asco
rbat
e,cy
stei
ne,
glu
tath
ion
e,u
rate
;ce
llu
lose
acet
ate
mem
bra
ne
blo
od
[17
3]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
4U
–P
t2
0.6
Vv
s.A
g=
Ag
Cl;
n=
a;R
T
n=a;
0.2
mm
2n=a;
0.2
–2
0m
mo
lL�
1;
90
sec
>1
0d
ays
(20
00
mea
sure
men
ts),
85
%o
fre
lati
ve
sen
siti
vit
y:
15
day
s,6
0%
of
rela
tive
sen
siti
vit
y:
1m
on
th;
9m
on
ths
–;
dif
fusi
on
lim
itat
ing
mem
bra
nes
blo
od
[6]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
10
U
–P
t2
0.6
5V
vs.
Ag=
Ag
Cl;
n=
a;R
T
n=a;
n=a
n=a;
0–
0.1
6m
mo
lL�
1;
2m
in
n=
a;n=
a–
;p
oly
(tet
ra-
flu
oro
eth
yle
ne)
mem
bra
ne
swea
t[1
74
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
50
U
–P
t2
n=
a;p
H7
.45
;n=
an=a;
n=a
n=a;
n=a;
2m
in8
0%
of
init
ial
resp
on
se:
1w
eek
(15
det
erm
inat
ion
sp
erd
ay);
n=
a
hy
dro
gen
per
ox
ide;
mem
bra
ne,
du
alel
ectr
od
e
sali
va
[14
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
12
3.2
U
–P
t2
0.2
5V
vs.
Ag=
Ag
Cl;
pH
7;
25� C
n=a;
6.5
mm
2n=a;
0–
0.7
2m
mo
lL�
1;
6–
10
min
n=
a;>
40
day
s(s
tora
ge
dry
atR
T)
asco
rbat
e,m
etal
ion
s,o
rgan
icac
ids,
pH
,te
mp
erat
ure
;ce
llu
lose
acet
ate
lay
er
kim
chi,
yo
gh
urt
[17
5]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t2
�0
.7V
vs
Ag=
Ag
Cl;
pH
7;
25� C
n=a;
n=a
n=a;
0.0
6–
1.8
5m
mo
lL�
1;
14
sec
n=
a;>
3m
on
ths
(sto
rag
eat
<1
0� C
inth
ed
ark
)
n=
a;n=
asw
eat
[17
6]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t2
0.6
5V
vs.
SC
E;
pH
7;
n=
a
n=a;
0.2
5cm
2n=a;
n=a;
n=
an=
a;7
7%
of
init
ial
acti
vit
y:
6m
on
ths
(sto
rag
eat
4� C
)
n=
a;n=
an=
a;[1
77
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t2
n=
a;p
H7
;2
5� C
n=a;
n=a
n=
a;0
–0.5
mm
olL
�1;
2.5
min
n=
a;n=
a–
;d
ilu
tio
no
fsa
mp
lew
ine
[17
8]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t2
n=
a;p
H7
;n=
an=a;
n=a
n=a;
0–
10
mm
olL
�1;
13
0se
cn=
a;n=
a–
;b
ilay
erm
emb
ran
efe
rmen
ted
mil
k,
mil
k[1
79
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t2
n=
a;p
H7
;n=
an=a;
n=a
n=a;
n=a;
n=
an=
a;n=
aas
corb
ate;
cell
ulo
seac
etat
ela
yer
ferm
ente
dm
ilk
[18
0]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
80
–1
00
Um
L�
1
–P
t3
0.7
Vv
sA
g=
Ag
Cl;
pH
7;
n=
a
n=a;
n=a
n=a;
0–
0.2
mm
olL
�1;
4se
cn=
a;n=
aac
etam
ino
ph
en,
asco
rbat
e,cy
stei
ne,
ura
te;
po
lyp
yrr
ole
film
n=
a[7
4]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
10
0U
mL�
1
–P
t3
0.7
Vv
sA
g=
Ag
Cl;
pH
7;
RT
n=a;
n=a
70=
20
0n
mo
lL�
1
(S=N¼
3);
70
–5
00
nm
olL
�1;
10
sec
8d
ays
of
con
tin
uo
us
op
erat
ion
;3
wee
ks
(sto
rag
ein
bu
ffer
at4� C
)
acet
ate,
acet
amin
op
hen
,cy
stei
ne,
ura
te;
po
ly(p
yrr
ole
)la
yer
n=
a[1
81
]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t3
0.6
Vv
s.A
g=
Ag
Cl;
pH
6.8
;n=a
14
.8mA
mm
ol�
1L=
13mA
mm
ol�
1L
;7
.07
mm
2
0.0
1–
3m
mo
lL�
1;
n=a;
10
sec
n=
a;<
2w
eek
s(s
tora
ge
inbu
ffer
at4� C
)
asco
rbat
e;co
imm
ob
iliz
atio
no
fas
corb
ate
ox
idas
e
n=
a[4
0]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
6(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)o
fen
zym
eu
sed
inse
nso
rp
rep
arat
ion
Med
iato
r,co
fact
or
Mat
eria
lo
fw
ork
ing
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;te
mp
erat
ure
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
gel
ectr
od
e
Low
erd
etec
tio
nli
mit
;li
nea
rra
ng
e;re
spo
nse
tim
e
Op
erat
ion
alst
abil
ity
;st
ora
ge
stab
ilit
y
Inte
rfer
ence
;p
rote
ctio
nag
ain
stin
terf
eren
ce
Ap
pli
cati
on
Ref
.2
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
n=a
–P
t3
0.6
Vv
s.A
g=A
gC
l;p
H7
;2
5� C
n=
a;0
.3cm
2n=
a;n=
a;n=
an=a;
n=
an=
a;n=
an=a
[18
2]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
4.9
U
–P
tn=a
n=
a;p
H7
.5;
22� C
n=
a;n=
a8
.6mm
olL
�1
(S=N¼
3);
0–
0.4
8m
mo
lL�
1;
n=
a
>8
ho
fco
nti
nu
ou
so
per
atio
n;
80
%o
fin
itia
lac
tiv
ity
:>
1y
ear
(sto
rag
eat
4� C
)
asco
rbat
e,cy
stei
ne,
hy
dro
chlo
rid
e;n=
am
ilk
,y
og
hu
rt[1
83
]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–A
u3
0.3=
1.1
Vv
sA
g=A
gC
l(s
tep
ped
po
ten
tial
pu
lse
pai
r);
pH
7;
25� C
n=
a;1
5m
m2
n=
a;0
.25
–1
.5m
mo
lL�
1;
n=
a
n=a;
n=
aas
corb
ate;
pu
lse
pai
r,d
iffe
ren
tial
det
erm
inat
ion
n=a
[18
4]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–A
u=
Pt
3n=
a;p
H7
;n=
an=
a;0
.25
cm2
(Au
)=0
.05mm
2(P
t)n=
a;n=
a;n=
an=a;
n=
an=
a;n=
an=a
[18
5]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
0.4
U
–g
lass
yca
rbo
n3
1V
vs.
Ag=A
gC
l;p
H7
.7;
25� C
n=
a;n=
a0
.1mm
olL
�1
(S=N¼
5);
0–
0.3
mm
olL
�1;
5se
c
50%
of
init
ial
acti
vit
y:>
60
day
s(1
0det
erm
inat
ions
per
day
,st
ora
ge
inbuff
erat
4� C
);n=
a
acet
amin
op
hen
,as
corb
ate,
ure
ate;
po
lyio
nco
mp
lex
mat
rix
(per
m-s
elec
tiv
ity
)
sou
rm
ilk
[18
6]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
0.3
2U
–g
lass
yca
rbo
n3
1V
vs.
Ag=A
gC
l;p
H7
.7;
30� C
n=
a;0
.14
cm2
20mm
olL
�1
(S=N¼
5);
0–
6m
mo
lL�
1;
30
sec
50
%o
fin
itia
lac
tiv
ity
:>
56
day
s(3
0d
eter
min
atio
ns
per
day
,st
ora
ge
atR
T);
n=a
acet
amin
op
hen
,as
corb
ate,
ure
ate;
po
lyio
nco
mp
lex
mat
rix
(per
m-s
elec
tiv
ity
)
sou
rm
ilk
[18
7]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
0.3
8U
–g
rap
hit
e=p
lati
niz
edg
rap
hit
e
30
.7V
vs.
Ag=A
gC
l;p
H6
.5;
RT
0.0
86=0
.08
3n
Amm
ol�
1L
mm
�2;
3.1
4m
m2
3mm
olL
�1;
0–
1m
mo
lL�
1;
28
–4
6se
c
50
%o
fin
itia
lac
tiv
ity
:5
3=
13
3h
of
con
tin
uo
us
op
erat
ion
;>
20
wee
ks
(sto
rag
ein
hu
mid
env
iro
nm
ent
at4� C
)
n=
a;n=
an=a
[18
8]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–p
lati
niz
edca
rbo
n2
0.3
5V
vs.
Ag=A
gC
l;p
H7
;3
0� C
n=
a;n=
an=
a;n=
a;1
0se
csi
ng
le-u
se;
n=
aC
a2þ
(cat
ion
s),
elec
tro
acti
ve
com
po
un
ds;
ion
exch
ang
eco
lum
ns,
dif
fere
nti
ald
eter
min
atio
n
bu
tter
mil
k,
yo
gh
urt
[69
]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
1.8
U–
Pt
2�
0.7
Vv
s.A
g=A
gC
l;p
H7
;3
0� C
n=
a;0
.03
1m
m2
5mm
olL
�1;
5–
30
0m
mo
lL�
1;
n=
a
80
%o
fin
itia
lac
tiv
ity
:2
wee
ks
(20
det
erm
inat
ion
sp
erd
ay);
n=
a
n=
a;n=
afe
rmen
-ta
tio
nb
roth
[15
4]
N. Nikolaus, B. Strehlitz
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
12
8U
–P
t2
0.6
Vv
s.A
g=A
gC
l;p
H7
;2
0� C
1.7
–1
2.5
nA
mm
ol�
1L
;n=
a
n=
a0
–1
0m
mo
lL�
1;
42
–9
4se
cn=a;
n=
an=
a;n=
an=a
[18
9]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t2
0.6
Vv
s.A
g=P
d;
pH
8.5
;n=a
n=
a;5
3cm
20
.02mm
olL
�1
(S=N¼
3);
0.0
2–
10
00mm
olL
�1,
0.5
5–
50
mm
olL
�1
(FIA
6);
1m
in
91
%o
fin
itia
lac
tiv
ity
:1
2h
inco
mp
lex
med
ia,
42
00
det
erm
inat
ion
s;n=
a
pH
,te
mp
erat
ure
;n=
afe
rmen
-ta
tio
nb
roth
[19
0]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t2
0.6
5V
vs.
Ag=A
gC
l;p
H7
.1;
25� C
1m
Am
ol�
1L
;5
0.3
mm
21
2.5mm
olL
�1
(3�
val
ue)
;0
.02
5–
25
mm
olL
�1;
30
sec
30
day
s;n=a
–;
‘‘G
luco
-p
roce
sseu
r’’
crea
mch
eese
,w
hey
fro
my
og
hu
rt
[19
1]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t2
n=
a;p
H7
;n=
an=
a;n=
an=
a;n=
a;n=
an=a;
n=
an=
a;n=
am
ilk
[19
2]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t2
n=
a;p
H7
.4;
25� C
n=
a;n=
an=
a;n=
a;n=
a8
0%
of
init
ial
acti
vit
y:
15
day
so
fco
nti
nu
ou
so
per
atio
n;
75
%o
fin
itia
lac
tiv
ity
:2
yea
rs(s
tora
ge
at4� C
)
–;
n=
ab
loo
d[1
93
]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t3
0.4
Vv
s.A
g=A
gC
l;p
H7
.4;
37� C
15
1n
Am
mo
l�1
Lcm
�2;
n=
a
n=
a0
–1
2m
mo
lL�
1;
30
sec
n=a;
n=
an=
a;n=
an=a
[46
]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t3
0.6
5V
vs.
Ag=A
gC
l;p
H7
.4;
n=a
91
5.9
4�
29
.02
nA
mm
ol�
1L
;n=a
0.0
1m
mo
lL�
1;
0.0
1–
0.3
mm
olL
�1;
25
sec
n=a;
n=
aac
etam
ino
ph
en,
asco
rbat
e;n
on
-co
nd
uct
ing
film
n=a
[19
4]
LO
D(n
oE
Cg
iven
);Pediococcus
sp.;
n=a
–P
t3
0.7
Vv
s.A
g=A
gC
l;p
H7
;2
6�
1� C
n=
a;1
0m
m2
n=
a;n=
a;1
0se
cn=a;
n=
a–
;b
lock
ing
mem
bra
ne
inte
rsti
tial
flu
id[1
95
]
LO
D(E
C1
.1.3
.2);
n=
a;n=
a–
Pt
n=a
0.6
75
Vv
s.re
fere
nce
;n=
a;R
T
n=
a;n=
a;n=
a;n=
a;5
7se
cn=a;
n=
am
ann
ito
l;p
oly
mer
icla
yer
s
blo
od
[23
]
LO
D(n
oE
Cg
iven
);n=
a;n=
a–
carb
on
scre
enp
rin
tin
gin
k2
0.3
5V
vs
Ag=A
gC
l;p
H7
;3
0� C
5.2
–7
.8mA
mm
ol�
1L
;n=
an=
a;n=
a;n=
a2
h(1
35
det
erm
inat
ion
s);
n=a
Ca2
þ(c
atio
ns)
,el
ectr
oac
tive
com
po
un
ds;
pas
sin
gth
rou
gh
ion
exch
ang
eco
lum
ns,
dif
fere
nti
ald
eter
min
atio
n
bu
tter
mil
k,
yo
gh
urt
[19
6]
LO
D(n
oE
Cg
iven
);n=
a;2
6–
40
mg
mL�
1
sol–
gel
–g
rap
hit
e=p
lati
niz
edca
rbo
n
30
.35
Vv
s.A
g=A
gC
l;p
H7
;2
3� C
87
0–
28
00mA
mo
l�1
L;
n=
an=
a;0
–0
.3m
mo
lL�
1;
n=
asi
ng
leu
se;
>2
wee
ks
(sto
rag
eat
4� C
)
mat
rix
effe
cts;
n=
aw
ine
[19
7]
LO
D(n
oE
Cg
iven
);n=
a;n=
a–
gra
ph
ite
scre
enp
rin
tin
gin
k2
n=
a;n=
a;n=
an=
a;n=
an=
a;0
–1
0m
mo
lL�
1;
n=a
n=a;
>2
00
day
s(s
tora
ge
ov
ersi
lica
gel
at2
5� C
)
–;
dif
fere
nti
ald
eter
min
atio
nm
eat
[19
8]
LO
D(n
oE
Cg
iven
);n=
a;2
1.9
–1
7.5
U–
gra
ph
ite
scre
enp
rin
tin
gin
k3
0.3
5V
vs.
Ag=A
gC
l=S
CE
;p
H7
;3
0� C
25
.4mA
mm
ol�
1L
;1
4m
m2
n=
a;0
–2
mm
olL
�1;
n=
an=a;
>2
00
day
s(s
tora
ge
dry
)as
corb
ate,
H2O
2;
nafi
on
lay
er
n=a
[19
9]
(continued)
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
Table
6(continued
)
En
zym
e;o
rig
in;
amo
un
t(a
ctiv
ity
)o
fen
zym
eu
sed
inse
nso
rp
rep
arat
ion
Med
iato
r,co
fact
or
Mat
eria
lo
fw
ork
ing
elec
tro
de
El.
sys.
1P
ote
nti
al;
pH
;te
mp
erat
ure
Sen
siti
vit
y;
geo
met
ric
area
of
wo
rkin
gel
ectr
od
e
Low
erd
etec
tio
nli
mit
;li
nea
rra
ng
e;re
spo
nse
tim
e
Op
erat
ion
alst
abil
ity
;st
ora
ge
stab
ilit
y
Inte
rfer
ence
;p
rote
ctio
nag
ain
stin
terf
eren
ce
Ap
pli
cati
on
Ref
.2
LO
D(n
oE
Cg
iven
);n=
a;5
U–
Pt
20
.6V
vs.
Ag=
Ag
Cl;
pH
6.6
;2
5� C
0.6
82
–0
.32
1n
Amm
ol�
1L
;3
.1m
m2
0.5mm
olL
�1;
0–
0.5=
0–
1m
mo
lL�
1;
50
sec
70=
84
%o
fin
itia
lre
spo
nse
:1
6h
of
con
tin
uo
us
op
erat
ion
;9
2%
of
init
ial
sig
nal
:6
wee
ks
(sto
rag
ed
ryat
4� C
)
–;
nafi
on
lay
erb
loo
d,
bu
tter
mil
k,
yo
gh
urt
[20
0]
LO
D(n
oE
Cg
iven
);n=
a;n=
a–
Pt
20
.6V
vs.
Ag=
Ag
Cl;
n=
a;n=
a
0.2
–5
.5mA
mm
ol�
1L
;7
.07
mm
2n=
a;n=
a;1
0se
cn=a;
<2
wee
ks
n=
a;n=
a;n=a
[20
1]
LO
D(n
oE
Cg
iven
);n=
a;n=
a–
Pt
20
.65
Vv
s.A
g=
Ag
Cl;
n=
a;n=
a
24
nA
mm
ol�
1L
;1
9.6
mm
2n=
a;n=
a;n=
an=a;
n=
a;–
;d
iffe
ren
tial
det
erm
inat
ion
sali
va,
swea
t[2
02
]
LO
D(n
oE
Cg
iven
);n=
a;n=
a–
Pt
20
.65
Vv
s.A
g=
Ag
Cl;
pH
7;
n=
a
n=a;
n=
a;2mm
olL
�1;
0.0
05
–1
mm
olL
�1;
3m
in
80
%o
fin
itia
lac
tiv
ity
:<
15
0d
eter
min
atio
ns;
(sto
rag
ein
bu
ffer
)
n=
a;n=
a;w
ine
[20
3]
LO
D(n
oE
Cg
iven
);n=
a;1
.6U
–P
t3
0.7
5V
vs.
Ag=
Ag
Cl;
pH
7.4
;R
T
4.5
nAmm
ol�
1L
;0
.32
cm2
0.1
mm
olL
�1;
0.1
–1
.5m
mo
lL�
1;
15
sec=
2m
in
n=a;
50
%o
fin
itia
lre
spo
nse
:5
day
s(s
tora
ge
inbu
ffer
at4� C
)
asco
rbat
e,N
AD
H,
ura
te;
cell
ulo
sem
emb
ran
e
n=a
[20
4]
LO
D(n
oE
Cg
iven
);n=
a;n=
a–
n=
a3
n=
a;n=
a;2
8� C
2.8
9�
1.3
nA
mm
ol�
1L
;0
.25
mm
2n=
a;0
.2–
25
mm
olL
�1;
n=
a
n=a;
n=
an=
a;n=
asu
b-
cuta
neo
us
[20
5]
LO
D(n
oE
Cg
iven
);n=
a;n=
an=
an=
an=
a0
.7V
vs.
Ag=
Ag
Cl;
;n=
a;n=
a
n=a;
n=
an=
a;0
–1
1.5
mm
olL
�1;
n=
a
6–
7d
ays;
n=a
–;
n=
ab
loo
d[1
7]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
36
Up
ero
xid
ase
(EC
1.1
1.1
.7,
typ
eV
I);
ho
rser
adis
h;
28
0U
–ca
rbo
np
aste
3�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
7;
n=
a
n=a;
n=
an=
a;n=
a;n=
a>
24
h(F
IA);
n=a
acet
amin
op
hen
,as
corb
ate;
elec
tro
-p
oly
mer
ized
o-p
hen
yle
ne-
dia
min
ela
yer
ferm
enta
tio
nb
roth
[14
0a]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
26
Um
g�
1g
rap
hit
ep
ow
der
;p
ero
xid
ase
(EC
1.1
1.1
.7,
typ
eV
I);
ho
rser
adis
h;
28
0U
mg�
1
gra
ph
ite
pow
der
–ca
rbo
np
aste
2�
0.0
5–
0.0
5V
vs.
Ag=A
gC
l;p
H7
;2
5� C
n=a;
7.1
mm
2n=
a;n=
a;n=
an=a;
n=
an=
a;n=
an=a
[20
6]
LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
26
Um
g�
1g
rap
hit
ep
ow
der
;p
ero
xid
ase
(EC
1.1
1.1
.7,
typ
eV
I);
ho
rser
adis
h;
28
0U
mg�
1
gra
ph
ite
pow
der
–ca
rbo
np
aste
3�
0.0
5V
vs.
Ag=
Ag
Cl;
pH
6.5
;n=
a
n=a;
0.0
18
cm2
n=
a;1
0–
50
mg
L�
1;
n=
a8
0%
of
init
ial
sig
nal
:2
0h
of
con
tin
uo
us
op
erat
ion
(30
det
erm
inat
ion
sp
erh
ou
r);
n=
a
–;
low
po
ten
tial
n=a
[27
]
N. Nikolaus, B. Strehlitz
and/or clinical purposes can be purchased for ex-
ample at ABT GmbH (Radeberg, Germany), Arkray
Inc. (Kyoto, Japan), Diasys Diagnostic Systems
GmbH (Holzheim, Germany), EKF-diagnostic GmbH
(Barleben/Magdeburg, Germany), Med-Tronik GmbH
(Friesenheim, Germany), or SensLab GmbH (Leipzig,
Germany). Sensolytics GmbH (Bochum, Germany),
TRACE analytics GmbH (Braunschweig, Germany)
and YSI Inc. (Yellow Springs, USA) produce lactate
biosensor devices for biotechnological purposes. The
devices of Chemel AB (Lund, Sweden) and Tectronik
S. r. l. (Limena, Italia) can be used in food and food
production control.
After more than thirty years of development of am-
perometric lactate biosensors, it is very likely that,
especially for the food, wellbeing, sports, and medical
(point-of-care testing) sectors, more and more com-
mercial products will arise.
Acknowledgement. Financial support for this work was provided by
the European Commission in a 3-year collective research project
(QUALI-JUICE) within the sixth framework programme (Contract
No.: COLL-CT-2005-012461).
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Acta 555: 308LO
D(E
C1
.1.3
.2);
Pediococcus
sp.;
40
Um
g�
1g
rap
hit
ep
ow
der
;p
ero
xid
ase
(EC
1.1
1.1
.7,
typ
eV
I);
ho
rser
adis
h;
28
0U
mg�
1
gra
ph
ite
pow
der
–ca
rbo
np
aste
3�
0.0
5–
0.0
5V
vs.
Ag=
Ag
Cl;
pH
7;
25� C
25
0–
40
8n
Am
mo
l�1
L;
n=
a3mm
olL
�1
(S=N¼
3);
0.0
03
–1
mm
olL
�1;
<4
0se
c
57
–8
4%
of
init
ial
sen
siti
vit
y:
18
ho
fco
nti
nu
ou
so
per
atio
n;
>2
0d
ays
acet
amin
op
hen
,as
corb
ate,
ura
te;
low
po
ten
tial
n=
a[3
0]
LO
D(E
C1
.1.3
.4)
(sic
!);
n=a;
2.4
–3
.5U
mg�
1;
per
ox
idas
e(E
C1
.11
.1.7
);h
ors
erad
ish
;5
.4U
mg�
1
–ca
rbo
nsc
reen
pri
nti
ng
ink
30
Vv
s.A
g=A
gC
l;p
H7
.2;
n=a
0.2
7–
1.3
0n
Am
ol�
1L
;3
.14
mm
21
0mm
olL
�1;
5–
40mm
olL
�1
to2
0–
25
0mm
olL
�1;
n=
a
90
%o
fin
itia
lsi
gn
al:>
50
det
erm
inat
ion
s;>
2w
eek
s(s
tora
ge
atR
T)
–;
dil
uti
on
of
sam
ple
mil
k,
wh
ite
chee
se,
yo
gh
urt
[20
7]
Acetobacter
pasteurianus
wh
ole
cell
s–
Pt
n=a
n=
a;p
H6
;2
6� C
n=
a;n=
a1
00mm
olL
�1;
0.1
–1
.5mm
olL
�1;
1–
4m
in
60
%o
fin
itia
lac
tiv
ity
:3
20
h;
n=
a
acet
ald
ehy
de,
acet
ate,
eth
ano
l,p
yru
vat
e;n=a
mil
k,
yo
gh
urt
[20
8]
Alcaligenes
eutrophus
KT
02
wh
ole
cell
s–
Pt
2�
0.8
Vv
s.A
g=A
gC
l;p
H7
.2;
31� C
n=
a;n=
an=
a;n=a;
n=a
n=
a;n=
an=a;
n=a
n=
a[2
09
]
Escherichia
coli
resp
irat
ory
chai
n=
Escherichia
coli
wh
ole
cell
s
–P
t2
n=
a;p
H7
.6;
37� C
n=
a;n=
an=
a;n=a;
90
sec
40
0d
eter
min
atio
ns;
>6
mo
nth
s(s
tora
ge
inbu
ffer
wit
haz
ide,
wit
ho
ut
O2
at4� C
)
inh
ibit
ors
or
acti
vat
ors
inb
iolo
gic
alm
edia
;n=a
blo
od
,w
ine,
yo
gh
urt
[21
0]
1El.Sys
.T
wo
(2)
or
thre
e(3
)el
ectr
od
esy
stem
.2Ref
.R
efer
ence
.3SCE
Sat
ura
ted
calo
mel
elec
tro
de.
4RT
Ro
om
tem
per
atu
re.
5S=N
Sig
nal
ton
ois
era
tio
.6FIA
Flo
win
ject
ion
anal
ysi
s.
Amperometric lactate biosensors and their application in (sports) medicine, for life quality and wellbeing
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