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Optimal production of a novel endo-acting β-1,4-xylanase cloned from Saccharophagus degradans 2-40 into Escherichia coli BL21(DE3)

Paper ID Volume ID Publish Year Pages File Format Full-Text
33861 44994 2009 8 PDF Available
Title
Optimal production of a novel endo-acting β-1,4-xylanase cloned from Saccharophagus degradans 2-40 into Escherichia coli BL21(DE3)
Abstract

To date, gene xyn10C from Saccharophagus degradans 2-40 has only been identified to encode a potential xylanase. In the present study, xyn10C was cloned and overexpressed in Escherichia coli BL21(DE3). The protein produced by xyn10C, Xyn10C, was expressed in a soluble active form and found to be an endotype β-1,4-xylanase that preferentially produces xylobiose from xylan. Recombinant cell fermentation revealed that induction of the gene at low temperatures fostered expression of the recombinant xylanase with high volumetric and specific activities. Additionally, low growth rates were favorable for producing soluble active xylanase via a reduction in the formation of inclusion bodies. Furthermore, the optimal concentration of isopropyl-β-D-thiogalactopyranoside for induction was found to be 100 μm after two hours of precultivation at 37°C. Finally, enzyme production conducted using a fermentor with a working volume of 1.5-l resulted in slightly higher specific activities of xylanase when compared with the generation of enzymes in flasks with a working volume of 100 ml.

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Optimal production of a novel endo-acting β-1,4-xylanase cloned from Saccharophagus degradans 2-40 into Escherichia coli BL21(DE3)
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Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 26, Issues 3–4, 31 October 2009, Pages 157–164
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