Abstract
Several decades ago, the first reports on differences in action pattern between amylases from different sources indicated that the starch polymers are not degraded in a completely random manner. We here give an overview of different action patterns of amylases on amylose and amylopectin, focusing on the so-called multiple attack action of the enzymes. Nowadays, the multiple attack action is generally an accepted concept to explain the differences in amylase action pattern. However, the pancreatic α-amylase remains one of the few enzymes known with a considerable level of multiple attack action. Despite some recent studies, the molecular mechanism of the multiple attack action is still largely unclear. Probably, the degree to which the active site architecture and binding properties allow both the reorganization (sliding) of the substrate in the active site and the stabilisation of the productive enzyme/substrate complex mainly determine the multiple attack action of amylases.
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Abbreviations
- BAA:
-
Bacillus amyloliquefaciens α-amylase
- BLA:
-
Bacillus licheniformis α-amylase
- BSuA:
-
Bacillus subtilis α-amylase
- BStA:
-
Bacillus stearothermophilus maltogenic α-amylase
- DMA:
-
degree of multiple attack
- DP:
-
degree of polymerisation
- GH:
-
glycoside hydrolase
- MW:
-
molecular weight
- PPA:
-
porcine pancreatic α-amylase
- RVTS :
-
total level of reducing sugars
- RVPS :
-
level of reducing polysaccharides
- SBD:
-
starch binding domain
- TAKA:
-
Aspergillus oryzae α-amylase
- λ max :
-
wavelength of maximal extinction
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Bijttebier, A., Goesaert, H. & Delcour, J.A. Amylase action pattern on starch polymers. Biologia 63, 989–999 (2008). https://doi.org/10.2478/s11756-008-0169-x
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DOI: https://doi.org/10.2478/s11756-008-0169-x