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1 2 3 4M
36
kDa
28
55
95130
5
Supplementary Fig. 1
Supplementary Fig. 1. Expression and purification of Bacillus sp. BRC1 Bdh in/from E. coli. Lane 1, total
cell lysates of E. coli BL21 harboring pET28a (control); lane 2, total cell lysates of E. coli BL21 harboring
pET-bhd; lane 3, soluble fraction; lane 4, insoluble fraction; lane 5, purified Bdh (arrow).
pH
2 4 6 8 10 12
Re
lati
ve A
cti
vity
(%
)
0
20
40
60
80
100
Temperature (oC)
20 30 40 50 60 70 80 90 100
Re
lati
ve A
cti
vity
(%
)
0
20
40
60
80
100
A
B
Supplementary Fig. 2
Supplementary Fig. 2. Effects of pH (A) and temperature (B) on Bdh activity toward the substrates D-2,3-BD
(closed circles) and acetoin (open circles).
D-2,3-BD (mM)
0 200 400 600 800 1000
Sp
eci
fic
Ac
tiv
ity
(U m
g-1)
0
10
20
30
40
50
Meso-2,3-BD (mM)
0 500 1000 1500 2000
Sp
eci
fic
Ac
tiv
ity
(U m
g-1)
0
10
20
30
40
50
Acetoin (mM)
0 10 20 30 40 50
Sp
eci
fic
Ac
tivit
y (U
mg-1
)
0
3
6
9
12
15
Diacetyl (mM)
0 10 20 30 40 50
Sp
eci
fic
Ac
tivit
y (U
mg-1
)
0
2
4
6
8
10
A
C
B
D
Supplementary Fig. 3
Supplementary Fig. 3. Enzyme kinetics of Bacillus sp. BRC1 Bdh. A, D-2,3-BD; B, Meso-2,3-BD; C,
Acetoin; D, Diacetyl
Rel
ativ
e ac
tivi
ty (
%)
0
20
40
60
80
100
120 BRC1/pWH BRC1/pWH-bdh
Xylose 5%
Xylose 5%
Xylose 20%
Xylose 20%
EFB hydro
lysate
EFB hydro
lysate
Supplementary Fig. 4
Supplementary Fig. 4. Enzyme activity of Bdh from recombinant Bacillus sp. BRC1 strains. Closed bars, D-
2,3-BD; open bars, acetoin.