Enhancing the soluble expression of an amylase in Escherichia coli by the mutations related to its domain interactions.

doi:10.1016/j.pep.2015.12.010

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Article

Enhancing the soluble expression of an amylase in Escherichia coli by the mutations related to its domain interactions.

Protein expression and purification - 1 Apr 2016

Wang Peili, Qin Weitong, Xu Jiangtao, Yan Yaru, Tian Jian, Wu Ningfeng, Yao Bin

Abstract excerpt

The sequence and structure of the target protein exert a marked effect on its soluble expression in Escherichia coli. The effects of the mutation of an amylase isolated from Bacillus licheniformis (BLA) on its soluble expression in E. coli were investigated. A random mutation library of BLA was constructed to screen for mutations that resulted in enhanced soluble expression in E. coli. Two interesting mutations...

Topics

Amylases
Bacillus
Escherichia coli
Gene Expression
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Structure, Tertiary
Recombinant Proteins
Solubility

Source

Open in PubMed

Identifiers

PMID: 26707400
DOI: 10.1016/j.pep.2015.12.010

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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