Design of highly efficient cellulase mixtures for enzymatic hydrolysis of cellulose
β Scribed by Alexander V. Gusakov; Tatyana N. Salanovich; Alexey I. Antonov; Boris B. Ustinov; Oleg N. Okunev; Richard Burlingame; Mark Emalfarb; Marco Baez; Arkady P. Sinitsyn
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 222 KB
- Volume
- 97
- Category
- Article
- ISSN
- 0006-3592
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β¦ Synopsis
Abstract
An extremely highly active cellobiohydrolase (CBH IIb or Cel6B) was isolated from Chrysosporium lucknowense UV18β25 culture filtrate. The CBH IIb demonstrated the highest ability for a deep degradation of crystalline cellulose amongst a few cellobiohydrolases tested, including C. lucknowense CBH Ia, Ib, IIa, and Trichoderma reesei CBH I and II. Using purified C. lucknowense enzymes (CBH Ia, Ib, and IIb; endoglucanases II and V; Ξ²βglucosidase, xylanase II), artificial multienzyme mixtures were reconstituted, displaying an extremely high performance in a conversion of different cellulosic substrates (Avicel, cotton, pretreated Douglas fir wood) to glucose. These mixtures were much or notably more effective in hydrolysis of the cellulosic substrates than the crude multienzyme C. lucknowense preparation and other crude cellulase samples produced by T. reesei and Penicillium verruculosum. Highly active cellulases are a key factor in bioconversion of plant lignocellulosic biomass to ethanol as an alternative to fossil fuels. Biotechnol. Bioeng. 2007; 97: 1028β1038. Β© 2007 Wiley Periodicals, Inc.
π SIMILAR VOLUMES
A new functionally based kinetic model for enzymatic hydrolysis of pure cellulose by the Trichoderma cellulase system is presented. The model represents the actions of cellobiohydrolases I, cellobiohydrolase II, and endoglucanase I; and incorporates two measurable and physically interpretable substr