Putative endoglucanase PcGH5 from Phanerochaete chrysosporium is a β-xylosidase that cleaves xylans in synergistic action with endo-xylanase
Summary: 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 b-glucosidase/ 6-phospho-b-glucosidase/b-galactosidase superfamily, and an endoglucanase, recombinant PcGH5 exhibited a b-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.
Type: Non-ISI/SCOPUS listed journals with ISSB/ISBN
Author: Nguyễn Đức Huy, Cu Le Nguyen, Jeong-Woo Seo, Dae-Hyuk Kim, Seung-Moon Park
Unit: Director board of Institute
Journal:Journal of Bioscience and Bioengineering
Issue, Number, Pages119, 4, 416–420
ISSN/ISBN:1389 - 1723, E - ISSN: 1347-4421
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Year of publication: 2015
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