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Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium

Paper ID Volume ID Publish Year Pages File Format Full-Text
20613 43183 2013 8 PDF Available
Title
Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium
Abstract

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 l−1. 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. Cu2+ and Zn2+ 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.

Keywords
Phanerochaete chrysosporium; Pichia pastoris; Xylosidase; Arabinofuranosidase; Xylan; Xylose
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Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 116, Issue 2, August 2013, Pages 152–159
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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