Journal
BIOTECHNOLOGY AND BIOENGINEERING
Volume 109, Issue 1, Pages 295-299Publisher
WILEY-BLACKWELL
DOI: 10.1002/bit.23299
Keywords
cellulase; Cel9; cellulase kinetics; crystalline cellulose; Thermobifida fusca
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Funding
- USDOE [GO18084]
- New York State Empire Development Corporation
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Detailed understanding of cell wall degrading enzymes is important for their modeling and industrial applications, including in the production of biofuels. Here we used Cel9A, a processive endocellulase from Thermobifida fusca, to demonstrate that cellulases that contain a catalytic domain (CD) attached to a cellulose binding module (CBM) by a flexible linker exist in three distinct molecular states. By measuring the ability of a soluble competitor to reduce Cel9A activity on an insoluble substrate, we show that the most common state of Cel9A is bound via its CBM, but with its CD unoccupied by the insoluble substrate. These findings are relevant for kinetic modeling and microscopy studies of modular glycoside hydrolases. Biotechnol. Bioeng. 2012;109: 295299. (c) 2011 Wiley Periodicals, Inc.
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