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Chimeric Cellulase Matrix for Investigating Intramolecular Synergism between Non-hydrolytic Disruptive Functions of Carbohydrate-binding Modules and Catalytic Hydrolysis*

Yuguo Wang,Rentao Tang,Jin Tao,Xiaonan Wang,B. Zheng,Yan Feng

Published 2012 in Journal of Biological Chemistry

ABSTRACT

Background: Disruptive functions of carbohydrate-binding modules (CBMs) toward crystalline cellulose and their synergism with hydrolases are important. Results: Chimeric cellulases derived from the cellulase matrix have activities toward crystalline cellulose. Conclusion: Analysis of chimeric cellulase activities allows quantification of the disruptive functions of CBMs. Significance: An efficient strategy was established to investigate non-hydrolytic disruptive functions and their synergism with hydrolysis. The conversion of renewable cellulosic biomass is of considerable interest for the production of biofuels and materials. The bottleneck in the efficient conversion is the compactness and resistance of crystalline cellulose. Carbohydrate-binding modules (CBMs), which disrupt crystalline cellulose via non-hydrolytic mechanisms, are expected to overcome this bottleneck. However, the lack of convenient methods for quantitative analysis of the disruptive functions of CBMs have hindered systematic studies and molecular modifications. Here we established a practical and systematic platform for quantifying and comparing the non-hydrolytic disruptive activities of CBMs via the synergism of CBMs and a catalytic module within designed chimeric cellulase molecules. Bioinformatics and computational biology were also used to provide a deeper understanding. A convenient vector was constructed to serve as a cellulase matrix into which heterologous CBM sequences can be easily inserted. The resulting chimeric cellulases were suitable for studying disruptive functions, and their activities quantitatively reflected the disruptive functions of CBMs on crystalline cellulose. In addition, this cellulase matrix can be used to construct novel chimeric cellulases with high hydrolytic activities toward crystalline cellulose.

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