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Title 

Putative endoglucanase PcGH5 from Phanerochaete chrysosporium is a beta-xylosidase that cleaves xylans in synergistic action with endo-xylanase

Authors 

N D HuyC L NguyenJeong-Woo SeoD H KimS M Park

Publisher 

Elsevier

Issue Date 

2015

Citation 

Journal of Bioscience and Bioengineering, vol. 119, no. 4, pp. 416-420

Keywords 

Glycoside hydrolase family 5HemicellulosePhanerochaete chrysosporiumXylanXylosidase

Abstract 

A predicted endoglucanase gene (PcGH5) was cloned from Phanerochaete chysosporium, and expressed in Pichia pastoris. Although PcGH5 showed similarity with the conserved domains of a cellulase superfamily GH5, a β-glucosidase/6-phospho-β-glucosidase/β-galactosidase superfamily, and an endoglucanase, recombinant PcGH5 exhibited a β-xylosidase activity, rather than endoglucanase activity. Therefore, the predicted gene was named as PcXyl5. Further characterization of recombinant PcXyl5 showed not only catalysis of the hydrolysis of xylo-oligomers to xylose, but also displayed transglycosylation activity using alcohol as a receptor. Optimum pH of rPcXyl5 was found to be 5.5, whereas optimum temperature was 50°C. rPcXyl5 increased reducing sugar release of birchwood xylan, beechwood xylan, and arabinoxylan by 6.4%, 13%, 15.8%, respectively, in synergistic action with endo-xylanase. Interestingly, the late addition of rPcXyl5 into reaction with endo-xylanase resulted in a larger increase of reducing sugar release from pretreated barley straw that addition at the start or by treatment with endo-xylanases alone. The increases observed were 6.3% and 13.8%, respectively, showing a great potential application for hemicellulose saccharification.

ISSN 

1389-1723

Link 

http://dx.doi.org/10.1016/j.jbiosc.2014.09.012

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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