Journal
BIOTECHNOLOGY LETTERS
Volume 26, Issue 17, Pages 1329-1333Publisher
SPRINGER
DOI: 10.1023/B:BILE.0000045628.32242.99
Keywords
Cellulonionas biazotea; endo-glucanase; kinetics; mutation; thermodynamics
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The maximum product yield of endo-glucanase (650 IU g(-1) substrate) Cellulomonas biazotea mutant 51 Sm-r was 1.5- to 2.5-fold more than was produced by the wild type cells and was twice that reported by previous researchers. Mutation substantially improved the enthalpy (DeltaH*) and entropy of activation (DeltaS*) for product formation, turnover number, specificity constant activation energy, free energies for transition state formation and substrate binding for CMC hydrolysis respectively.
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