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Purification and Characteristics of Xyloglucanase and Five Other Cellulolytic Enzymes from Trichoderma reesei QM9414

Huan Qi1,2, Fali Bai1, and Aihua Liu1,2*

1Qingdao Institute of Bioenergy and Bioprocess Technology and Key Laboratory of Bioenergy, Chinese Academy of Sciences, 189 Songling Road, Qingdao 266101, China; fax: +86-532-8066-2778; E-mail: liuah@qibebt.ac.cn

2University of Chinese Academy of Sciences, No. 19A Yuquan Road, Beijing 100049, China

* To whom correspondence should be addressed.

Received November 28, 2012; Revision received January 17, 2013
By combining anion-exchange chromatography with gel filtration, an effective method for purification of wild-type xyloglucanase and five other cellulolytic enzymes from strain QM9414 of Trichoderma reesei was established. Characterization by enzyme activity assay, SDS-PAGE, and mass spectrometry identified the purified proteins as cellobiohydrolases I and II, endoglucanases I and II, a xyloglucanase, and β-xylosidase, of which the xyloglucanase was purified for the first time from the mutant strain QM9414. This method holds great promise to study the mechanism of cellulolytic enzymes, to investigate the synergistic action between cellulase and other cellulolytic enzymes, and to better exploit enzyme preparations for degradation of lignocellulose.
KEY WORDS: xyloglucanase, cellulolytic enzymes, purification, Trichoderma reesei QM9414

DOI: 10.1134/S0006297913040123