Thermal stability and activity improvements of a Ca-independent α-amylase from Bacillus subtilis CN7 by C-terminal truncation and hexahistidine-tag fusion

Chenghua Wang, Qingyan Wang, Siming Liao, Bingfang He, Ribo Huang

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6 引用 (Scopus)

摘要

Simultaneous improvements of thermostability and activity of a Ca-independent α-amylase from Bacillus subtilis CN7 were achieved by C-terminal truncation and his6-tag fusion. C-terminal truncation, which eliminates C-terminal 194-amino-acid residues from the intact mature α-amylase, raised the turnover number by 35% and increased the thermostability in terms of half-life at 65 °C by threefold. A his 6-tag fusion at either the C- or N-terminus of truncated α-amylase further enhanced its turnover number by 59% and 37%, respectively. Molecular modeling revealed that these improvements could be attributed to structural rearrangement and reorientation of the catalytic residues.

源语言英语
页(从-至)93-100
页数8
期刊Biotechnology and Applied Biochemistry
61
2
DOI
出版状态已出版 - 2014

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