Structure-based design of agarase AgWH50C from Agarivorans gilvus WH0801 to enhance thermostability

AgWH50C, an exo-β-agarase of GH50 isolated from Agarivorans gilvus WH0801, plays a key role in the enzymatic production of neoagarobiose, which has great application prospect in the cosmetics and pharmaceutical industry. In contrast, the poor thermostability becomes the main obstructive factor of gl...

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Published in:Applied microbiology and biotechnology 2019-02, Vol.103 (3), p.1289-1298
Main Authors: Zhang, Pujuan, Zhang, Jinru, Zhang, Lujia, Sun, Jianan, Li, Yuan, Wu, Lian, Zhou, Jiahai, Xue, Changhu, Mao, Xiangzhao
Format: Article
Language:English
Subjects:
Agarase
Agarivorans gilvus
Biomedical and Life Sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Chromatography
Cloning
Cosmetics
Crosslinking
Crystal structure
E coli
Enzymes
Gelation
Glycoside hydrolase
Hydrolase
Laboratories
Life Sciences
Microbial Genetics and Genomics
Microbiology
Pharmaceutical industry
Physiology
Plasmids
Proteins
Thermal stability
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cited_by cdi_FETCH-LOGICAL-c372t-c74e635be0b2506e9bc009df5b8d982b44200231cf240c4a9da34f318fee067c3
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creator Zhang, Pujuan
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Xue, Changhu
Mao, Xiangzhao
description AgWH50C, an exo-β-agarase of GH50 isolated from Agarivorans gilvus WH0801, plays a key role in the enzymatic production of neoagarobiose, which has great application prospect in the cosmetics and pharmaceutical industry. In contrast, the poor thermostability becomes the main obstructive factor of glycoside hydrolase (GH) family 50 agarases, including AgWH50C. Herein, based on the AgWH50C crystal structure, we designed several mutants by a multiple cross-linked rational design protocol used thermostability predicting softwares ETSS, PoPMuSiC, and HotMuSiC. To our surprise, the mutant K621F increased its relative activity by as much as 45% and the optimal temperature increased to 38 °C compared to that of wild-type, AgWH50C (30 °C). The thermostability of K621F also exhibited a substantial improvement. Considering that the gelling temperature of the agarose is higher than 35 °C, K621F can be used to hydrolyze agarose for neoagarobiose production.
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subjects Agarase
Agarivorans gilvus
Biomedical and Life Sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Chromatography
Cloning
Cosmetics
Crosslinking
Crystal structure
E coli
Enzymes
Gelation
Glycoside hydrolase
Hydrolase
Laboratories
Life Sciences
Microbial Genetics and Genomics
Microbiology
Pharmaceutical industry
Physiology
Plasmids
Proteins
Thermal stability
title Structure-based design of agarase AgWH50C from Agarivorans gilvus WH0801 to enhance thermostability
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