Embed Size (px)
Citation preview
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
Departm
ent o
f Chem
istry, B
iote
chnolo
gy a
nd F
ood S
cience
Team 4 – Lignocellulose to biofuels
Topic: enzyme technology for conversion of lignocellulosic biomass
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
Departm
ent o
f Chem
istry, B
iote
chnolo
gy a
nd F
ood S
cience
The biorefinery, 2nd generation biofuels and enzymes – NotesEnzymatic deconstruction is the method of choice.
Enzymes are a major cost.
Biofuel is only one of many possible products.
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
Departm
ent o
f Chem
istry, B
iote
chnolo
gy a
nd F
ood S
cience
UMN-UMB, Team 4 specific project: CBP21, a helper protein from the CBM33 family
Gustav Vaaje-Kolstad et al., Journal of Biological Chemistry 280: 11313 -11319 & 280:28492-28497 (2005) + Patent application
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
4
UMN-UMB, Team 4 specific project – starting point
Goals:Use of directed evolution (mutagenesis) to produce accessory proteins that act on cellulose.Generation of fundamental knowledge about how helper proteins such as CBP21 work.
People:Claudia Schmidt-Dannert group with post-doc Jake Vick.Eijsink group with post-doc Gustav Vaaje-Kolstad and (since 2010) Ph.D. student Zarah Forsberg.
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
5
UMN-UMB, Team 4 specific project – Developments since 2007
GH61 proteins act synergistically with cellulose and show structural similarity with CBM33 (CBP21)CBM33 proteins are enzymes that break down chitin chainsGH61 proteins are enzymes that break down cellulose chainsIdentification of natural CBM33 proteins that break down celluloseInteresting ideas and findings at UMN concerning mechanism
CBM33 GH61
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
Departm
ent o
f Chem
istry, B
iote
chnolo
gy a
nd F
ood S
cience
A new paradigm for degradation of crystalline polysaccharides
”Oxidohydrolase” (”CBM33” or ”GH61”), catalyzing chain cleavage in a fully crystalline context
+Endo
Exo-processive
Vaaje-Kolstad et al., 2010, Science 330:219-222
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
7
Very “hot” project. IP issues. Lots of mutagenesis work on CBP21 has been done and
mutant characterization is in progress. Several new, active CBM33s available. NMR structure of CBP21 (a CBM33) has been solved. Shift of focus from ”enzyme development” to enzyme
”understanding”. Several joint papers, including potential ”breakthrough”
papers on mechanism, are on their way. Funding is running out (?)
UMN-UMB, Team 4 – Status June 2011
NO
RW
EG
IAN
UN
IVER
SIT
Y O
F LIF
E S
CIE
NC
ES
www.umb.no
Departm
ent o
f Chem
istry, B
iote
chnolo
gy a
nd F
ood S
cience
Notes about the future
Funding ? (currently only one PhD student at UMB)
Many applications sent in Norway (but……)
MSc student exchange: Sophanit Mengesha
PhD student exchange: Zarah Forsberg (?)
Nb. Current potential is huge and progress is good, but
very high complexity (protein production, analytical
tools, theoretical biochemistry, many partners).
