Improving the thermostability and modulating the inulin profile of inulosucrase through rational glycine-to-proline substitution-Reference-Cited by-同舟云学术

Improving the thermostability and modulating the inulin profile of inulosucrase through rational glycine-to-proline substitution

Published:2024 Issue:4 Volume:14 Page:2346-2353
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Charoenwongpaiboon Thanapon¹^ORCID,Sommanat Nawapat¹,Wangpaiboon Karan²³,Puangpathanachai Manatsanan²,Pongsawasdi Piamsook²,Pichyangkura Rath²

Affiliation:

1. Department of Chemistry, Faculty of Science, Silpakorn University, Nakhon Pathom, 73000, Thailand

2. Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand

3. Center of Excellence in Structural and Computational Biology, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand

Abstract

MD simulations pinpointed temperature-sensitive glycine residues in LrInu. Substituting these glycines with proline significantly improved stability and levan yield.

Funder

Thailand Science Research and Innovation

Silpakorn University

Ministry of Higher Education, Science, Research and Innovation, Thailand

Chulalongkorn University

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/RA/D3RA06896J

Reference34 articles.

1. Energy- and evolution-based design of inulosucrase for enhanced thermostability and inulin production

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3. Role of Glycine 212 in the Allosteric Behavior of Phosphofructokinase from Bacillus stearothermophilus

4. Site-Directed Mutagenesis of a Regulatory Site ofEscherichia coliADP-Glucose Pyrophosphorylase: The Role of Residue 336 in Allosteric Behavior

5. The effects of amino acid replacements of glycine 20 on conformational stability and catalysis of staphylococcal nuclease