Thermal stability and activity improvements of a Ca‐independent α‐amylase from Bacillus subtilis CN7 by C‐terminal truncation and hexahistidine‐tag fusion. (26th February 2014)

• Record Type: Journal Article
• Authors: Wang, Chenghua; Wang, Qingyan; Liao, Siming; He, Bingfang; Huang, Ribo
• Is Part Of: Biotechnology and applied biochemistry. Volume 61:Number 2(2014)
• Page Start: 93
• Page End: 100
• Publication Date: 2014-02-26
• Subjects: Biotechnology -- Periodicals; Biochemical engineering -- Periodicals; Biochemistry -- Periodicals; Biochemistry -- Periodicals; Genetic Techniques -- Periodicals; Microbiological Techniques -- Periodicals; 660.6
• DOI: 10.1002/bab.1150
• Languages: English
• ISSNs: 0885-4513

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>Simultaneous improvements of thermostability and activity of a Ca‐independent α‐amylase from <italic>Bacillus subtilis</italic> 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 his₆‐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.</p> </abstract>