Table 1
Some examples of alkaline-active maltooligosaccharide-forming
α-amylases from alkaliphiles
Organism
Molecular wt
(kDa)
pH optimum pH stability
Temperature
optimum (
C)
Temperature
stability (
C)
Major hydrolysis product
Reference
Bacillus
sp. A-40-2 B
10–10.5
9.0–11.5
N.D.
N.D.
G1, G2, G3
[17]
Bacillus
sp. ANT-6 94.5
10.5
7.0–11.0
80
50–100
ND
[29]
Bacillus
strain
GM8901
97
11.0–12.00
6.0–13.0
60
Up to 50
G4 via G6 and G5
intermediates
[44]
Bacillus
sp. IMD
370
159
10.0
8.5–10.5
40
Up to 45
G4 and less
[121]
Bacillus
sp. strain
XAL601
224
9.0
–
70
–
G2–G4
[108]
Bacillus
sp. H-167
102
10.5
7.0–12.0
60
50–55
G6>G4>G2>G5>G3.G1
[45]
Bacillus
isolate
KSM-K38
55
8.0–9.5
6.0–11.0
55–60
Up to 30
G3, G6, with G7 and G2 as
intermediates
[25]
Bacillus
strain
KSM-1378
53
8.0–8.5
6.0–10.0
55
Up to 45
G3, G5, G6, G2
[31]
Bacillus
sp. TS-23
65
9.0
7.0–10.0
60
30–90
G4
[62]
Bacillus
sp. TS 23
65
9.0
–
60
–
G5
[30]
Bacillus clausii
BT-21
101
9.5
N.D
55
Up to 55
G6, G4 and G2
[122]
Bacillus coagulans
R
3
N.D.
10.5
7.0–11.0
85
Up to 75
G1–G4 and higher
[123]
Bacillus halodurans
LBK 34
119
10.5–11.5
9.0
60
Up to 55
G6 and G4.G2.G5>G3
and G1
[43]
Starch-Modifying Enzymes
229