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Increased alkali stability in Trichoderma reesei endo-1,4-β-xylanase II by site directed mutagenesis

Paper ID Volume ID Publish Year Pages File Format Full-Text
25796 43601 2006 6 PDF Available
Title
Increased alkali stability in Trichoderma reesei endo-1,4-β-xylanase II by site directed mutagenesis
Abstract

A number of engineered Trichoderma reesei endo-β-1,4-xylanase (Xyn II) mutants were created and activity tests were performed for increased stability. The stability of the earlier characterized mutant Y5 (T2C, T28C, K58R, +191D) was further increased by the mutations creating the constructs P9 (N97R + F93W + H144K), P12 (H144C + N92C), P15 (F180Q + H144C + N92C) and P21 (H22K + F180Q + H144C + N92C). The resistance towards thermal inactivation at alkaline pH was increased in all of the mutants. Residual activity T50% was increased 4–5 °C for P9 at pH 9. The performance of the P9 mutant in sulphate pulp bleaching was also tested and was shown to increase brightness markedly compared to the reference. The bleaching results showed the industrial potential of the obtained mutant.

Keywords
Endo-1,4-β-xylanase; Trichoderma reesei; Alkali stability
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Increased alkali stability in Trichoderma reesei endo-1,4-β-xylanase II by site directed mutagenesis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 121, Issue 1, 2 January 2006, Pages 102–107
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