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Improving the cellobiose-hydrolysis activity and glucose-tolerance of a thermostable β-glucosidase through rational design.

Abstract：

:β-Glucosidase is the rate-limiting component of a cellulase-hydrolyzing reaction. Thermostability and glucose-tolerance are two critical criteria of the enzyme, which practically determine its performance in industrial applications. In this study, a thermostable and glucose-tolerant β-glucosidase (named Bgl1317) belonging to the glycoside hydrolase family 1 was acquired from a metagenomic library of Turpan soil through functional screening. Bgl1317 showed excellent thermostability and glucose-tolerance and its crystal structure was subsequently determined at a high resolution. Rational design based on the structure was conducted, producing three beneficial mutations A397R, L188A and A262S. While A397R improved the cellobiose activity by 80%, L188A and A262S increased the IC50 value of glucose from 0.8 to 1.5 M. The residues that may play a role in glucose-tolerance of GH1 β-glucosidases were summarized and the performances of glucose-tolerant β-glucosidases reported in recent years were discussed and compared. This study provides insights into enzymatic properties of Bgl1317 for engineering it into a powerful catalyst and β-glucosidases in general.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Liu X,Cao L,Zeng J,Liu Y,Xie W

doi

10.1016/j.ijbiomac.2019.06.029

subject

Has Abstract

pub_date

2019-09-01 00:00:00

pages

1052-1059

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)31662-9

journal_volume

136

pub_type

杂志文章

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