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Three amino acid changes contribute markedly to the thermostability of β-glucosidase BglC from Thermobifida fusca by Xiao-Qiong Pei; Zhuo-Lin Yi; Chuan-Gen Tang; Zhong-Liu Wu is a Engineering article available to read on EtoBox.

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Thermostability of b-glucosidase was enhanced by family shuffling, site saturation mutagenesis, and sitedirected mutagenesis. Family shuffling was carried out based on b-glucosidase BglC from Thermobifida fusca and b-glucosidase BglB from Paebibacillus polymxyxa with the help of synthetic primers. Highthroughput screening revealed mutants with higher thermostability than both parental enzymes. The most thermostable mutant VM2 containing three key amino acid changes in L444Y/G447S/A433V had a 144-fold increase in half-life of inactivation as compared to the parental enzyme BglC. The mutant VM2 showed 28% and 94% increase in k cat towards p-nitrophenyl-b-D-glucopyranoside (pNPG) and cellobiose, respectively. The mutant with enhanced stability would facilitate the recycle of b-glucosidase in the bioconversion of cellulosic biomass.

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Author

Xiao-Qiong Pei; Zhuo-Lin Yi; Chuan-Gen Tang; Zhong-Liu Wu

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0960-8524)

Published

2011

Language

EN

Field

Engineering (Physical Sciences)