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Shifting pH optimum of Bacillus circulans xylanase based on molecular modeling

Paper ID Volume ID Publish Year Pages File Format Full-Text
24804 43538 2008 7 PDF Available
Title
Shifting pH optimum of Bacillus circulans xylanase based on molecular modeling
Abstract

Although hydrolases are used in several industrial processes, its industrial applications have some limitations in specific cases since some industrial processes are carried out at pH value which is different from optimum pH of the enzyme. Alkaline side optimum pH of hydrolases is always desirable, and it is proved difficult to achieve that by mutation only. Hence, molecular modeling was applied to select the promising mutants. The changes in electrostatic potential, which was calculated using Delphi, were compared to the changes in pH optimum of four hydolases and their mutants. The results showed that the change in electrostatic potential can be used as an indicator for selecting relevant candidates of mutation. Bacillus circulans xylanase was selected as a model system, and the promising mutants were picked up by the molecular modeling. Q167M and R73V, had a higher pH optimum than the wild type, while K175Q had a similar pH-activity profile of the wild type.

Keywords
Xylanase; pH optimum; Electrostatic potential; Protein engineering; Hydrolase; Enzyme
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Shifting pH optimum of Bacillus circulans xylanase based on molecular modeling
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 133, Issue 3, 1 February 2008, Pages 294–300
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