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Purification and Characterization of Novel Thermostable and Ca-independent α-amylase Produced by Bacillus Amyloliquefaciens BH072

Purification and Characterization of Novel Thermostable and Ca-independent α-amylase Produced by Bacillus Amyloliquefaciens BH072

Renpeng Du, Qiaozhi Song, Qiaoge Zhang, Fangkun Zhao, Rak-Chon Kim, Zhijiang Zhou, Ye Han

Int J Biol Macromol. 2018 Aug;115:1151-1156.

PMID: 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9000855-B	α-Amylase from Bacillus amyloliquefaciens		9000-85-5	Price

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