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Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium

Paper ID Volume ID Publish Year Pages File Format Full-Text
20868 43195 2013 7 PDF Available
Title
Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium
Abstract

The cDNA of acetyl xylan esterase 2 (PcAxe2) gene containing a carbohydrate binding module (CBM) sequence from Phanerochaete chrysosporium was cloned and expressed in Pichia pastoris. The recombinant PcAxe2 protein (rPcAxe2) was efficiently produced, reaching a maximum of 1058 U l−1 after 6 days of cultivation. Molecular mass of the rPcAxe2 on SDS-PAGE was approximately 63 kDa under hyperglycosylation. Optimal activity of the purified rPcAxe2 enzyme was observed at pH and temperature of 7.0 and 30–35°C, respectively. In addition to acetyl xylan esterase activity, rPcAxe2 also exhibited a xylanase activity at an optimum pH and temperature of 5.0 and 80°C, respectively. The synergistic action of rPcAxe2 with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan enhanced the total reducing soluble sugar.

Keywords
Acetyl xylan esterase; Phanerochaete chrysosporium; Pichia pastoris; Synergisms; Xylanase
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Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 115, Issue 5, May 2013, Pages 507–513
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