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- W2946391132 abstract "A novel maltooligosaccharide-forming amylase (MFAse) from Bacillus stearothermophilus (Bst-MFAse) was heterologously expressed in B. subtilis and purified by hydrophobic and ion-exchange chromatographies. Bst-MFAse, an approximately 58 kDa monomer, could effectively hydrolyze linear α-glucan with DP > 6 and slightly hydrolyze maltohexaose. In addition, Bst-MFAse was proved to majorly produce maltopentaose and maltohexaose from starch and categorized as a maltopentaose-forming amylase. The action pattern was analyzed using amylopectin and amylose as substrate, showing that Bst-MFAse could rapidly reduce iodine blue value. Thus, Bst-MFAse was categorized as both a maltopentaose-forming amylase and an endo-amylase. During the initial period (2 h) of amylolysis, Bst-MFAse mainly cleaved amylopectin (18.7%) than amylose (14.0%). However, the final conversion rate (24 h) of amylose (68.8%) was slightly higher than that of amylopectin (64.8%). Bst-MFAse may have great potential applications in industry due to its highly specific activity, unique substrate specificity, and end-type product pattern." @default.
- W2946391132 created "2019-05-29" @default.
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- W2946391132 date "2019-08-01" @default.
- W2946391132 modified "2023-10-18" @default.
- W2946391132 title "A novel maltooligosaccharide-forming amylase from Bacillus stearothermophilus" @default.
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- W2946391132 doi "https://doi.org/10.1016/j.fbio.2019.100415" @default.
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