Skip to Content
Merck
  • A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch.

A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch.

FEBS letters (2014-03-13)
Hui Peng, Yunyun Zheng, Maojiao Chen, Ying Wang, Yazhong Xiao, Yi Gao
ABSTRACT

A novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family (CBM69) was identified in the α-amylase (AmyP) of the recently established alpha-amylase subfamily GH13_37. The SBD and its homologues come mostly from marine bacteria, and phylogenetic analysis indicates that they are closely related to the CBM20 and CBM48 families. The SBD exhibited a binding preference toward raw rice starch, but the truncated mutant (AmyPΔSBD) still retained similar substrate preference. Kinetic analyses revealed that the SBD plays an important role in soluble starch hydrolysis because different catalytic efficiencies have been observed in AmyP and the AmyPΔSBD.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Taka-Diastase from Aspergillus oryzae, powder, slightly beige, ~100 U/mg
Sigma-Aldrich
α-Amylase from Bacillus sp., powder, yellow-brown, ~50 U/mg
Sigma-Aldrich
Starch from potato, Soluble
Sigma-Aldrich
α-Amylase, heat-stable, solution, for use in Total Dietary Fiber Assay, TDF-100A
Sigma-Aldrich
α-Amylase from porcine pancreas, Type VI-B, ≥5 units/mg solid
Sigma-Aldrich
Starch from wheat, Unmodified
Sigma-Aldrich
α-Amylase from Bacillus sp., liquid
Sigma-Aldrich
α-Amylase from Aspergillus oryzae, ≥150 units/mg protein (biuret)
Sigma-Aldrich
α-Amylase from human saliva, Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
Sigma-Aldrich
α-Amylase from human saliva, Type IX-A, lyophilized powder, 1,000-3,000 units/mg protein
Sigma-Aldrich
α-Amylase from Aspergillus oryzae, powder, ~30 U/mg