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Cloning, expression and characterization of a novel acidic xylanase, XYL11B, from the acidophilic fungus Bispora sp. MEY-1

Paper ID Volume ID Publish Year Pages File Format Full-Text
17868 42702 2009 8 PDF Available
Title
Cloning, expression and characterization of a novel acidic xylanase, XYL11B, from the acidophilic fungus Bispora sp. MEY-1
Abstract

A xylanase gene (xyl11B) was cloned from Bispora sp. MEY-1 and expressed in Pichia pastoris. xyl11B, with a 66-bp intron, encodes a mature protein of 219 residues with highest identity (57.1%) to the Trichoderma reesei xylanase of glycoside hydrolase family 11. The purified recombinant XYL11B was acidophilic, exhibiting maximum activity at pH 2.6 and 65 °C. The enzyme was also thermostable, pH stable, and was highly resistant to both pepsin and trypsin, suggesting good performance in the digestive tract as a feed supplement to improve animal nutrition. The activity of XYL11B was enhanced by most metal ions but was inhibited weakly by Hg2+, Pb2+and Cu2+, which strongly inhibit many other xylanases. The specific activity of XYL11B for oat spelt xylan substrate was 2049 U mg−1. The main hydrolysis products of xylan were xylose and xylobiose.

Keywords
Acidophilic xylanase; Acidophilic fungus; Bispora sp. MEY-1; Overexpression; Pichia pastoris
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Cloning, expression and characterization of a novel acidic xylanase, XYL11B, from the acidophilic fungus Bispora sp. MEY-1
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 45, Issue 2, 7 August 2009, Pages 126–133
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us