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Rational pH-engineering of the thermostable xylanase based on computational model

Paper ID Volume ID Publish Year Pages File Format Full-Text
35493 45092 2009 4 PDF Available
Title
Rational pH-engineering of the thermostable xylanase based on computational model
Abstract

Locating sites of amino acids related to enzyme properties is still a challenge for rational engineering. Based on the strategy that sites of amino acids can be located by dipeptides, a computational model was made for pH-related dipeptides of xylanase. According to the dipeptide model, pH of a thermostable xylanase B from Thermotoga maritima was rationally designed by locating pH-related amino acids in its sequence and structure. In agreement with expectation, the optimum pH (pHopt) of the xylanase was improved by five amino acids substitutions: E70Q, E74Q, E77Q, G85Q and T87Q. In parallel assay reactions, at 90 °C, its pHopt increases to 5.5 from 5.1, and its whole pH profile also shifts 0.5 units towards alkaline area; at 80 °C, the relative activity decreases very little over a wide pH range from 5.25 to 6.0. This result demonstrated that the bioinformatics model is useful for pH rational design and engineering of xylanase, a model molecular of a large family of ∼10% proteins with (β/α)8-barrel structure.

Keywords
pHopt, optimum pH; Topt, optimum temperature for xylanase activitySite-location; Computational model; Rational design; pH-engineering; Thermostable xylanase
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Rational pH-engineering of the thermostable xylanase based on computational model
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 8, August 2009, Pages 912–915
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