Evidence map›Paper›PMID 37241913›Full record

ReviewMolecules (Basel, Switzerland)2023

High Hydrostatic Pressure in the Modulation of Enzymatic and Organocatalysis and Life under Pressure: A Review.

Hana Scepankova, Diogo Galante, Edelman Espinoza-Suaréz, Carlos A Pinto, Letícia M Estevinho, Jorge Saraiva

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
3.2field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. HighHydrostaticPressure-Assisted Curing ofFoods (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Hana ScepankovaLAQV-REQUIMTE, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.
Diogo GalanteLAQV-REQUIMTE, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.
Edelman Espinoza-SuarézLAQV-REQUIMTE, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.
Carlos A PintoLAQV-REQUIMTE, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0002-5742-706X
Letícia M EstevinhoCIMO, Mountain Research Center Polytechnic Institute of Bragança, Campus Santa Apolónia, 5301-855 Bragança, Portugal.
Jorge SaraivaLAQV-REQUIMTE, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0002-5536-6056
Rede de Química e Tecnologia · PTPolytechnic Institute of Bragança · PT

Funding

Fundação para a Ciência e Tecnologia COVID/BD/153220/2023Fundação para a Ciência e Tecnologia LA/P/0007/2021Fundação para a Ciência e Tecnologia SFRH/BD/137036/2018Fundação para a Ciência e Tecnologia SFRH/BD/88133/2012Fundação para a Ciência e Tecnologia UIDB/00690/2020Fundação para a Ciência e Tecnologia UIDB/50006/2020Fundação para a Ciência e Tecnologia UIDP/00690/2020Fundação para a Ciência e Tecnologia UIDP/50006/2020
6 · The paper itself

Abstract

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.

Indexed as

Hydrostatic PressureCatalysisHydrolysisKineticsTemperatureactivityenzymeequilibriumhigh hydrostatic pressuresubstrate

Identifiers

PMID37241913
PMCPMC10223222
OpenAlexW4377103426

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.