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 |
卷 | 61 |
期 | 2 |
DOI | |
出版状态 | 已出版 - 2014 |