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Engineering of Clostridium phytofermentans Endoglucanase Cel5A for Improved Thermostability
Author(s) -
Wenjin Liu,
Xiaozhou Zhang,
Zuoming Zhang,
Y.H. Percival Zhang
Publication year - 2010
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00958-10
Subject(s) - cellulase , thermostability , cellulose , glycoside hydrolase , mutant , escherichia coli , carboxymethyl cellulose , chemistry , cellulosic ethanol , biochemistry , hydrolase , cell wall , enzyme , gene , organic chemistry , sodium
A family 5 glycoside hydrolase fromClostridium phytofermentans was cloned and engineered through a cellulase cell surface display system inEscherichia coli . The presence of cell surface anchoring, a cellulose binding module, or a His tag greatly influenced the activities of wild-type and mutant enzymes on soluble and solid cellulosic substrates, suggesting the high complexity of cellulase engineering. The best mutant had 92%, 36%, and 46% longer half-lives at 60°C on carboxymethyl cellulose, regenerated amorphous cellulose, and Avicel, respectively.