Role of glycine 256 residue in improving the catalytic efficiency of mutant endoglucanase of family 5 glycoside hydrolase fromBacillus amyloliquefaciensSS35-Reference-Cited by-同舟云学术

Role of glycine 256 residue in improving the catalytic efficiency of mutant endoglucanase of family 5 glycoside hydrolase fromBacillus amyloliquefaciensSS35

Published:2020-06-30 Issue:9 Volume:117 Page:2668-2682
ISSN:0006-3592
Container-title:Biotechnology and Bioengineering
language:en
Short-container-title:Biotechnology and Bioengineering

Author:

Singh Shweta¹²,Kumar Krishan¹,Nath Priyanka¹²,Goyal Arun¹²^ORCID

Affiliation:

1. Carbohydrate Enzyme Biotechnology Laboratory, Department of Biosciences and BioengineeringIndian Institute of Technology Guwahati Guwahati Assam India

2. DBT PAN‐IIT Centre for BioenergyIndian Institute of Technology Guwahati Guwahati Assam India

Publisher

Wiley

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.27448

Reference48 articles.

1. LIGNOCELLULOSIC BIOMASS CHARACTERISTICS FOR BIOENERGY APPLICATION: AN OVERVIEW

2. A salt-bridge controlled by ligand binding modulates the hydrolysis reaction in a GH5 endoglucanase

3. Study and design of stability in GH5 cellulases

4. A machine learning approach to predicting protein–ligand binding affinity with applications to molecular docking

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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