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  • Title: Purification and characterization of novel thermostable and Ca-independent α-amylase produced by Bacillus amyloliquefaciens BH072.
    Author: Du R, Song Q, Zhang Q, Zhao F, Kim RC, Zhou Z, Han Y.
    Journal: Int J Biol Macromol; 2018 Aug; 115():1151-1156. PubMed ID: 29729336.
    Abstract:
    In the present study, a novel α-amylase produced by Bacillus amyloliquefaciens BH072 was purified and characterized. The molecular weight of purified α-amylase was approximately 68 kDa, determined by Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) and ten amino acid of N-terminal was NSGLNGYLTH. The kinetic parameters Km and Vmax were 4.27 ± 0.21 mg/mL and 987.34 ± 23.34 U/mg, respectively. Purified α-amylase showed maximal activity at pH 7 and 60 °C. Enzyme remained stable in pH range 6.0-7.0 and 50-80 °C. The activity of the α-amylase was Ca2+ independent and stability in the presence of surfactant, oxidizing and bleaching agents. The β-mercaptoethanol and EDTA greatly enhanced and reduced α-amylase activity, respectively. This enzyme has high hydrolysis rate toward corn, wheat and potato starch and hydrolyzes soluble starch to glucose, maltose, maltotriose and maltotetraose, indicating that the α-amylase represents a promising candidate for applications in the food industry.
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