| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6531142 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 8 Pages |
Abstract
The thermostability of an esterase from Bacillus subtilis was enhanced by random mutagenesis and combination of beneficial mutations. The hydrolysis of racemic menthyl acetate by BSEV4 at elevated temperature indicates that better thermostability could reduce the enzyme dosage or reaction time. The modeled structure demonstrates the addition of ionic bonds, hydrogen bonds and/or hydrophobic interactions will contribute mostly to the structure stability.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Yi Gong, Guo-Chao Xu, Gao-Wei Zheng, Chun-Xiu Li, Jian-He Xu,