- 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
PMID24613924
摘要
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.
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Sigma-Aldrich
α-淀粉酶 来源于地衣芽孢杆菌, lyophilized powder, 500-1,500 units/mg protein, 93-100% (SDS-PAGE)
Sigma-Aldrich
α-淀粉酶 来源于猪胰腺, PMSF Treated, Type I-A, saline suspension, ≥1000 units/mg protein (E1%/280)
Sigma-Aldrich
α-淀粉酶 来源于猪胰腺, Type I-A, PMSF treated, saline suspension, 700-1400 units/mg protein (E1%/280)
Sigma-Aldrich
淀粉 来源于玉米, Unmodified waxy corn starch of essentially pure amylopectin; contains only trace amounts of amylose.
Supelco
淀粉 来源于玉米, analytical standard, analytical standard for Starch Assay Kits SA-20 and STA-20