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Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme

Glycosyltransferase (GTs) is a wide class of enzymes that transfer sugar moiety, playing a key role in the synthesis of bacterial exopolysaccharide (EPS) biopolymer. In recent years, increased demand for bacterial EPSs has been observed in pharmaceutical, food, and other industries. The application...

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Autores principales: González-Faune, Patricio, Sánchez-Arévalo, Ignacio, Sarkar, Shrabana, Majhi, Krishnendu, Bandopadhyay, Rajib, Cabrera-Barjas, Gustavo, Gómez, Aleydis, Banerjee, Aparna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8198650/
https://www.ncbi.nlm.nih.gov/pubmed/34071348
http://dx.doi.org/10.3390/polym13111771
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author González-Faune, Patricio
Sánchez-Arévalo, Ignacio
Sarkar, Shrabana
Majhi, Krishnendu
Bandopadhyay, Rajib
Cabrera-Barjas, Gustavo
Gómez, Aleydis
Banerjee, Aparna
author_facet González-Faune, Patricio
Sánchez-Arévalo, Ignacio
Sarkar, Shrabana
Majhi, Krishnendu
Bandopadhyay, Rajib
Cabrera-Barjas, Gustavo
Gómez, Aleydis
Banerjee, Aparna
author_sort González-Faune, Patricio
collection PubMed
description Glycosyltransferase (GTs) is a wide class of enzymes that transfer sugar moiety, playing a key role in the synthesis of bacterial exopolysaccharide (EPS) biopolymer. In recent years, increased demand for bacterial EPSs has been observed in pharmaceutical, food, and other industries. The application of the EPSs largely depends upon their thermal stability, as any industrial application is mainly reliant on slow thermal degradation. Keeping this in context, EPS producing GT enzymes from three different bacterial sources based on growth temperature (mesophile, thermophile, and hyperthermophile) are considered for in silico analysis of the structural–functional relationship. From the present study, it was observed that the structural integrity of GT increases significantly from mesophile to thermophile to hyperthermophile. In contrast, the structural plasticity runs in an opposite direction towards mesophile. This interesting temperature-dependent structural property has directed the GT–UDP-glucose interactions in a way that thermophile has finally demonstrated better binding affinity (−5.57 to −10.70) with an increased number of hydrogen bonds (355) and stabilizing amino acids (Phe, Ala, Glu, Tyr, and Ser). The results from this study may direct utilization of thermophile-origin GT as best for industrial-level bacterial polysaccharide production.
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spelling pubmed-81986502021-06-14 Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme González-Faune, Patricio Sánchez-Arévalo, Ignacio Sarkar, Shrabana Majhi, Krishnendu Bandopadhyay, Rajib Cabrera-Barjas, Gustavo Gómez, Aleydis Banerjee, Aparna Polymers (Basel) Article Glycosyltransferase (GTs) is a wide class of enzymes that transfer sugar moiety, playing a key role in the synthesis of bacterial exopolysaccharide (EPS) biopolymer. In recent years, increased demand for bacterial EPSs has been observed in pharmaceutical, food, and other industries. The application of the EPSs largely depends upon their thermal stability, as any industrial application is mainly reliant on slow thermal degradation. Keeping this in context, EPS producing GT enzymes from three different bacterial sources based on growth temperature (mesophile, thermophile, and hyperthermophile) are considered for in silico analysis of the structural–functional relationship. From the present study, it was observed that the structural integrity of GT increases significantly from mesophile to thermophile to hyperthermophile. In contrast, the structural plasticity runs in an opposite direction towards mesophile. This interesting temperature-dependent structural property has directed the GT–UDP-glucose interactions in a way that thermophile has finally demonstrated better binding affinity (−5.57 to −10.70) with an increased number of hydrogen bonds (355) and stabilizing amino acids (Phe, Ala, Glu, Tyr, and Ser). The results from this study may direct utilization of thermophile-origin GT as best for industrial-level bacterial polysaccharide production. MDPI 2021-05-28 /pmc/articles/PMC8198650/ /pubmed/34071348 http://dx.doi.org/10.3390/polym13111771 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
González-Faune, Patricio
Sánchez-Arévalo, Ignacio
Sarkar, Shrabana
Majhi, Krishnendu
Bandopadhyay, Rajib
Cabrera-Barjas, Gustavo
Gómez, Aleydis
Banerjee, Aparna
Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme
title Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme
title_full Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme
title_fullStr Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme
title_full_unstemmed Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme
title_short Computational Study on Temperature Driven Structure–Function Relationship of Polysaccharide Producing Bacterial Glycosyl Transferase Enzyme
title_sort computational study on temperature driven structure–function relationship of polysaccharide producing bacterial glycosyl transferase enzyme
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8198650/
https://www.ncbi.nlm.nih.gov/pubmed/34071348
http://dx.doi.org/10.3390/polym13111771
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