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Hydrophobic interaction network analysis for thermostabilization of a mesophilic xylanase

Paper ID Volume ID Publish Year Pages File Format Full-Text
23706 43465 2012 11 PDF Available
Title
Hydrophobic interaction network analysis for thermostabilization of a mesophilic xylanase
Abstract

One widely known drawback of enzymes is their instability in diverse conditions. The thermostability of enzymes is particularly relevant for industrial applications because operation at high temperatures has the advantage of a faster reaction rate. Protein stability is mainly determined in this study by intra-molecular hydrophobic interactions that have a collective and 3-dimensional clustering effect. To interpret the thermostability of enzymes, network analysis was introduced into the protein structure, and a network parameter of structural hierarchy, k of k-clique, was used to discern more developed hydrophobic interaction clusters in the protein structure. The favorable clustering conformations of hydrophobic residues, which seemed to be important for protein thermostability, were discovered by the application of a network analysis to hydrophobic interactions of GH11 xylanases. Coordinating higher k-clique hydrophobic interaction clusters through the site-directed mutagenesis of the model enzyme, Bacillus circulans xylanase, stabilized the local structure and thus improved thermostability, such that the enzyme half-life and melting temperature increased by 78 fold and 8.8 °C, respectively. This study highlights the advantages of interpreting collective hydrophobic interaction patterns and their structural hierarchy and the possibility of applying network analysis to the thermostabilization of enzymes.

► We developed new hydrophobic interaction network analysis for thermostabilization. ► Coordinating hydrophobic residues were attempted by network analysis. ► Hydrophobic network of thermophilic enzyme was transplanted into mesophilic xylanase. ► Mutant designed by network analysis showed 75-fold improvement of thermostability. ► This easy and powerful enzyme design strategy could be applied to other enzymes.

Keywords
Protein; Thermostability; Hydrophobic interaction; Network analysis; Structural hierarchy; Cluster; Xylanase
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Hydrophobic interaction network analysis for thermostabilization of a mesophilic xylanase
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 161, Issue 1, 15 September 2012, Pages 49–59
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