Cargando…
High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review
The interest in high hydrostatic pressure (HHP) is mostly focused on the inactivation of deleterious enzymes, considering the quality-related issues associated with enzymes in foods. However, more recently, HHP has been increasingly studied for several biotechnological applications, including the po...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10223222/ https://www.ncbi.nlm.nih.gov/pubmed/37241913 http://dx.doi.org/10.3390/molecules28104172 |
_version_ | 1785049890128134144 |
---|---|
author | Scepankova, Hana Galante, Diogo Espinoza-Suaréz, Edelman Pinto, Carlos A. Estevinho, Letícia M. Saraiva, Jorge |
author_facet | Scepankova, Hana Galante, Diogo Espinoza-Suaréz, Edelman Pinto, Carlos A. Estevinho, Letícia M. Saraiva, Jorge |
author_sort | Scepankova, Hana |
collection | PubMed |
description | The interest in high hydrostatic pressure (HHP) is mostly focused on the inactivation of deleterious enzymes, considering the quality-related issues associated with enzymes in foods. However, more recently, HHP has been increasingly studied for several biotechnological applications, including the possibility of carrying out enzyme-catalyzed reactions under high pressure. This review aims to comprehensively present and discuss the effects of HHP on the kinetic catalytic action of enzymes and the equilibrium of the reaction when enzymatic reactions take place under pressure. Each enzyme can respond differently to high pressure, mainly depending on the pressure range and temperature applied. In some cases, the enzymatic reaction remains significantly active at high pressure and temperature, while at ambient pressure it is already inactivated or possesses minor activity. Furthermore, the effect of temperature and pressure on the enzymatic activity indicated a faster decrease in activity when elevated pressure is applied. For most cases, the product concentration at equilibrium under pressure increased; however, in some cases, hydrolysis was preferred over synthesis when pressure increased. The compiled evidence of the effect of high pressure on enzymatic activity indicates that pressure is an effective reaction parameter and that its application for enzyme catalysis is promising. |
format | Online Article Text |
id | pubmed-10223222 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-102232222023-05-28 High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review Scepankova, Hana Galante, Diogo Espinoza-Suaréz, Edelman Pinto, Carlos A. Estevinho, Letícia M. Saraiva, Jorge Molecules Review The interest in high hydrostatic pressure (HHP) is mostly focused on the inactivation of deleterious enzymes, considering the quality-related issues associated with enzymes in foods. However, more recently, HHP has been increasingly studied for several biotechnological applications, including the possibility of carrying out enzyme-catalyzed reactions under high pressure. This review aims to comprehensively present and discuss the effects of HHP on the kinetic catalytic action of enzymes and the equilibrium of the reaction when enzymatic reactions take place under pressure. Each enzyme can respond differently to high pressure, mainly depending on the pressure range and temperature applied. In some cases, the enzymatic reaction remains significantly active at high pressure and temperature, while at ambient pressure it is already inactivated or possesses minor activity. Furthermore, the effect of temperature and pressure on the enzymatic activity indicated a faster decrease in activity when elevated pressure is applied. For most cases, the product concentration at equilibrium under pressure increased; however, in some cases, hydrolysis was preferred over synthesis when pressure increased. The compiled evidence of the effect of high pressure on enzymatic activity indicates that pressure is an effective reaction parameter and that its application for enzyme catalysis is promising. MDPI 2023-05-18 /pmc/articles/PMC10223222/ /pubmed/37241913 http://dx.doi.org/10.3390/molecules28104172 Text en © 2023 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 | Review Scepankova, Hana Galante, Diogo Espinoza-Suaréz, Edelman Pinto, Carlos A. Estevinho, Letícia M. Saraiva, Jorge High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review |
title | High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review |
title_full | High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review |
title_fullStr | High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review |
title_full_unstemmed | High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review |
title_short | High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review |
title_sort | high hydrostatic pressure in the modulation of enzymatic and organocatalysis and life under pressure: a review |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10223222/ https://www.ncbi.nlm.nih.gov/pubmed/37241913 http://dx.doi.org/10.3390/molecules28104172 |
work_keys_str_mv | AT scepankovahana highhydrostaticpressureinthemodulationofenzymaticandorganocatalysisandlifeunderpressureareview AT galantediogo highhydrostaticpressureinthemodulationofenzymaticandorganocatalysisandlifeunderpressureareview AT espinozasuarezedelman highhydrostaticpressureinthemodulationofenzymaticandorganocatalysisandlifeunderpressureareview AT pintocarlosa highhydrostaticpressureinthemodulationofenzymaticandorganocatalysisandlifeunderpressureareview AT estevinholeticiam highhydrostaticpressureinthemodulationofenzymaticandorganocatalysisandlifeunderpressureareview AT saraivajorge highhydrostaticpressureinthemodulationofenzymaticandorganocatalysisandlifeunderpressureareview |