Stability enhancement of urethanase from Lysinibacillus fusiformis by site-directed mutagenesis / 生物工程学报
Chinese Journal of Biotechnology
; (12): 1233-1242, 2016.
Article
in Chinese
| WPRIM (Western Pacific)
| ID: wpr-310544
Responsible library:
WPRO
ABSTRACT
Ethyl carbamate as a potential carcinogen commonly exists in traditional fermented foods and beverages. Enzymatic removal of ethyl carbamate from fermented foods and beverages is an efficient and safe method. In this study, we mutated urethanase from Lysinibacillus fusiformis SC02 on the Q328 site through computer aided design approaches. The half-life of resulting mutants Q328C and Q328V was detected to be 7.46 and 1.96 folds higher than that of the original enzyme, and Q328R presented better thermal-tolerance than the original urethanase when incubated at high temperature. The tolerance of Q328C to ethanol and acid also increased when compared with that of the original enzyme. The stability and tolerance to acid and ethanol of urethanase could be improved by modification on its Q328 site.
Full text:
Available
Database:
WPRIM (Western Pacific)
Main subject:
Bacillaceae
/
Bacterial Proteins
/
Enzyme Stability
/
Protein Engineering
/
Mutagenesis, Site-Directed
/
Computer-Aided Design
/
Ethanol
/
Amidohydrolases
/
Genetics
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2016
Document type:
Article