Enzymatic Properties of Mesophilic α-Amylase from Bacillus amyloliquefaciens M23
Zhengxiang Wang
Abstract
Zhengxiang Wang
Abstract
α-Amylase from B. amyloliquefacens M23 was purified to electrophoretic homogeneity. The molecular weight of the purified α-amylase is 58 kD. Its optimum pH value of is in the range from 5.5 to 6.5,and the optimum temperature is 60 ℃. With in 24 h at room temperature 80% enzyme activity keeps in the pH range from 7.0 to 10.0. The most enzyme activity loses within 15 min at 55 ℃. But, the enzyme would be stable for 1 h with the presence of 10 mmol/L Ca2+. EDTA inhibits the enzyme activity, while, Ca2+, Mn2+ and Co2+ ions are activators. Km and Vmax of α-amylase to soluble starch is 4.33 g/L and 1.19 g/L· min, respectively. The main hydrolysates to soluble starch are oligosaccharides and dextrin.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
α-Amylase from B. amyloliquefacens M23 was purified to electrophoretic homogeneity. The molecular weight of the purified α-amylase is 58 kD. Its optimum pH value of is in the range from 5.5 to 6.5,and the optimum temperature is 60 ℃. With in 24 h at room temperature 80% enzyme activity keeps in the pH range from 7.0 to 10.0. The most enzyme activity loses within 15 min at 55 ℃. But, the enzyme would be stable for 1 h with the presence of 10 mmol/L Ca2+. EDTA inhibits the enzyme activity, while, Ca2+, Mn2+ and Co2+ ions are activators. Km and Vmax of α-amylase to soluble starch is 4.33 g/L and 1.19 g/L· min, respectively. The main hydrolysates to soluble starch are oligosaccharides and dextrin.
Key concepts: Dextrin, Amylase, Bacillus amyloliquefaciens, Chemistry, Enzyme, Starch, Chromatography, Hydrolysis