Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis-Reference-Cited by-同舟云学术

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Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis

Published:2021-01 Issue: Volume:168 Page:442-452
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Lv Kemin,Shao Wenyu,Pedroso Marcelo Monteiro,Peng Jiayu,Wu Bin,Li Jiahuang,He Bingfang,Schenk Gerhard

Funder

National Key R&D Program of China

National Natural Science Foundation of China

Primary Research & Development Plan of Jiangsu

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference45 articles.

1. Biotransformation of lignocellulosic biomass into industrially relevant products with the aid of fungi-derived lignocellulolytic enzymes;Saldarriaga-Hermandez;Int. J. Biol. Macromol.,2020

2. Inter-domain synergism is required for efficient feeding of cellulose chain into active site of cellobiohydrolase Cel7A;Kont;J. Biol. Chem.,2016

3. Engineering enhanced cellobiohydrolase activity;Taylor;Nat. Commun.,2018

4. Processive and non-processive cellulases for biofuel production-lessons from bacterial genomes and structural analysis;Wilson;Appl. Microbiol. Biotechnol.,2012

5. Glycoside hydrolase processivity is directly related to oligosaccharide binding free energy;Payne;J. Am. Chem. Soc.,2013

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