Send to

Choose Destination
See comment in PubMed Commons below
Biochemistry (Mosc). 2013 Apr;78(4):424-30. doi: 10.1134/S0006297913040123.

Purification and characteristics of xyloglucanase and five other cellulolytic enzymes from Trichoderma reesei QM9414.

Author information

Qingdao Institute of Bioenergy and Bioprocess Technology and Key Laboratory of Bioenergy, Chinese Academy of Sciences, Qingdao, 266101, China.


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.

[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Biochemistry (Moscow)
    Loading ...
    Support Center