Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis
<p>Abstract</p> <p>Background</p> <p>The generation of focused mutant libraries at hotspot residues is an important strategy in directed protein evolution. Existing methods, such as combinatorial active site testing and residual coupling analysis, depend primarily on th...
Main Authors: | Wang Chenghua, Huang Ribo, He Bingfang, Du Qishi |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2012-10-01
|
Series: | BMC Bioinformatics |
Online Access: | http://www.biomedcentral.com/1471-2105/13/263 |
Similar Items
-
Thermostable mutant variants of Bacillus sp. 406 α-amylase generated by site-directed mutagenesis
by: Kachan Alexandr, et al.
Published: (2013-04-01) -
Protein engineering of alpha-amylase from anoxbacillus sp, SK3-4 with saturation mutagenesis /
by: Mohammad Emad Olya, 1986-, et al.
Published: (2013) -
Protein engineering of alpha-amylase from anoxbacillus sp, SK3-4 with saturation mutagenesis
by: Olya, Mohammad Emad
Published: (2013) -
Protein engineering of alpha-amylase from anoxbacillus sp, SK3-4 with saturation mutagenesis [electronic resource] /
by: Mohammad Emad Olya, 1986-
Published: (2013) -
Improving the thermostability of GH49 dextranase AoDex by site-directed mutagenesis
by: Zhen Wei, et al.
Published: (2023-01-01)