Identification and Mutation Analysis of Nonconserved Residues on the TIM-Barrel Surface of GH5_5 Cellulases for Catalytic Efficiency and Stability Improvement-Reference-Cited by-同舟云学术

Identification and Mutation Analysis of Nonconserved Residues on the TIM-Barrel Surface of GH5_5 Cellulases for Catalytic Efficiency and Stability Improvement

Published:2022-09-13 Issue:17 Volume:88 Page:
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Zheng Jie¹²,Liu Han-qing³,Qin Xing¹,Yang Kun¹,Tian Jian³,Wang Xiao-lu¹,Wang Ya-ru¹,Wang Yuan¹,Yao Bin¹,Luo Hui-ying¹,Huang Huo-qing¹^ORCID

Affiliation:

1. State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing, People’s Republic of China

2. Institute of Radiation Technology, Beijing Academy of Science and Technology, Beijing, People’s Republic of China

3. Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People’s Republic of China

Abstract

A comprehensive understanding of the residues on the α-helices of the GH5_5 cellulases is important for catalytic efficiency and stability improvement. The main objective of this study was to use the evolutionary conservation and plasticity of the TIM-barrel fold to probe the relationship between nonconserved residues on the outer side of the α-helices and the catalytic efficiency of GH5_5 cellulases by conducting structure-guided protein engineering.

Funder

The State Key Laboratory of Animal Nutrition Project

Earmarked fund for China Agriculture Research System

National Natural Science Foundation of China

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.01046-22

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