Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium
Summary: A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141 U lL1. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45 C and 50 C. SDS-PAGE revealed a single band of purified rPcXyl of 83 kDa. Cu2D and Zn2D completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5 mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.
Type: International
Author: Nguyễn Đức Huy, Thayumanavan Palvannan, Tae-Ho Kwon, Seung-Moon Park
Unit: Director board of Institute
Journal:Journal of Bioscience and Bioengineering
Issue, Number, Pages116, 2, 152-159
ISSN/ISBN:1398-1723, E-ISSN: 1347-4421
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Year of publication: 2013
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