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Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin

For a long time, high-pressure treatment has been used to destroy the compact structures of natural proteins in order to promote subsequent enzymatic hydrolysis. However, there are few reports evaluating the feasibility of directly improving the catalytic capability of proteases by using high-pressu...

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Detalles Bibliográficos
Autores principales: Wang, Jianan, Bai, Tenghui, Ma, Yaping, Ma, Hanjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6151815/
https://www.ncbi.nlm.nih.gov/pubmed/29019907
http://dx.doi.org/10.3390/molecules22101659
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author Wang, Jianan
Bai, Tenghui
Ma, Yaping
Ma, Hanjun
author_facet Wang, Jianan
Bai, Tenghui
Ma, Yaping
Ma, Hanjun
author_sort Wang, Jianan
collection PubMed
description For a long time, high-pressure treatment has been used to destroy the compact structures of natural proteins in order to promote subsequent enzymatic hydrolysis. However, there are few reports evaluating the feasibility of directly improving the catalytic capability of proteases by using high-pressure treatments. In this study, the effects of high-pressure treatment on the catalytic capacity and structure of pepsin were investigated, and the relationship between its catalytic properties and changes in its physicochemical properties was explored. It was found that high-pressure treatment could lead to changes of the sulfhydryl group/disulfide bond content, hydrophobicity, hydrodynamic radius, intrinsic viscosity, and subunit composition of pepsin, and the conformational change of pepsin resulted in improvement to its enzymatic activity and hydrolysis efficiency, which had an obvious relationship with the high-pressure treatment conditions.
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spelling pubmed-61518152018-11-13 Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin Wang, Jianan Bai, Tenghui Ma, Yaping Ma, Hanjun Molecules Article For a long time, high-pressure treatment has been used to destroy the compact structures of natural proteins in order to promote subsequent enzymatic hydrolysis. However, there are few reports evaluating the feasibility of directly improving the catalytic capability of proteases by using high-pressure treatments. In this study, the effects of high-pressure treatment on the catalytic capacity and structure of pepsin were investigated, and the relationship between its catalytic properties and changes in its physicochemical properties was explored. It was found that high-pressure treatment could lead to changes of the sulfhydryl group/disulfide bond content, hydrophobicity, hydrodynamic radius, intrinsic viscosity, and subunit composition of pepsin, and the conformational change of pepsin resulted in improvement to its enzymatic activity and hydrolysis efficiency, which had an obvious relationship with the high-pressure treatment conditions. MDPI 2017-10-11 /pmc/articles/PMC6151815/ /pubmed/29019907 http://dx.doi.org/10.3390/molecules22101659 Text en © 2017 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Wang, Jianan
Bai, Tenghui
Ma, Yaping
Ma, Hanjun
Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin
title Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin
title_full Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin
title_fullStr Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin
title_full_unstemmed Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin
title_short Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin
title_sort effect of high-pressure treatment on catalytic and physicochemical properties of pepsin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6151815/
https://www.ncbi.nlm.nih.gov/pubmed/29019907
http://dx.doi.org/10.3390/molecules22101659
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