Cargando…
Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps
Food-derived hypotensive peptides have attracted attention in the field of active peptide research in recent years. In this study, based on ACE inhibition rate and using the Box–Behnken central combination design principle to optimise the process of ACE inhibitor peptides prepared by double-enzyme h...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8834213/ https://www.ncbi.nlm.nih.gov/pubmed/35159545 http://dx.doi.org/10.3390/foods11030394 |
_version_ | 1784649130662952960 |
---|---|
author | Wang, Rui Yun, Jianmin Wu, Shujuan Bi, Yang Zhao, Fengyun |
author_facet | Wang, Rui Yun, Jianmin Wu, Shujuan Bi, Yang Zhao, Fengyun |
author_sort | Wang, Rui |
collection | PubMed |
description | Food-derived hypotensive peptides have attracted attention in the field of active peptide research in recent years. In this study, based on ACE inhibition rate and using the Box–Behnken central combination design principle to optimise the process of ACE inhibitor peptides prepared by double-enzyme hydrolysis. The amino acid sequences of ACE inhibitor peptides were determined by liquid chromatography mass spectrometry (LC-MS/MS), and their binding to ACE was studied by molecular docking. The optimal processing conditions were 1:1 alkaline protease: compound protease, pH was 8.43, enzymolysis temperature was 44.32 °C, and enzymolysis time was 3.52 h. Under these conditions, the ACE inhibition rate reached 65.12%, and the inhibition rate after separation and purification was 80.68% (IC(50) = 0.9 mg/mL). Three novel peptides with ACE inhibitory activity were detected by LC-MS/MS, with sequences LVYP (Leu-Val-Tyr-Pro), VYPW(Val-Tyr-Pro-Trp) and YPWT(Tyr-Pro-Trp-Thr). Molecular docking revealed that the three novel peptides all established hydrogen bonds with the S1(Tyr523, Glu384, Ala354) and S2 (His353) pockets of ACE. Among them, LVYP, VYPW and YPWT, respectively, formed eleven hydrogen bonds, six hydrogen bonds and nine hydrogen bonds with ACE. The study revealed that these peptides have the potential for the development of novel ACE inhibitor drugs and provide a new avenue for high-value utilisation of mushrooms scraps. |
format | Online Article Text |
id | pubmed-8834213 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88342132022-02-12 Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps Wang, Rui Yun, Jianmin Wu, Shujuan Bi, Yang Zhao, Fengyun Foods Article Food-derived hypotensive peptides have attracted attention in the field of active peptide research in recent years. In this study, based on ACE inhibition rate and using the Box–Behnken central combination design principle to optimise the process of ACE inhibitor peptides prepared by double-enzyme hydrolysis. The amino acid sequences of ACE inhibitor peptides were determined by liquid chromatography mass spectrometry (LC-MS/MS), and their binding to ACE was studied by molecular docking. The optimal processing conditions were 1:1 alkaline protease: compound protease, pH was 8.43, enzymolysis temperature was 44.32 °C, and enzymolysis time was 3.52 h. Under these conditions, the ACE inhibition rate reached 65.12%, and the inhibition rate after separation and purification was 80.68% (IC(50) = 0.9 mg/mL). Three novel peptides with ACE inhibitory activity were detected by LC-MS/MS, with sequences LVYP (Leu-Val-Tyr-Pro), VYPW(Val-Tyr-Pro-Trp) and YPWT(Tyr-Pro-Trp-Thr). Molecular docking revealed that the three novel peptides all established hydrogen bonds with the S1(Tyr523, Glu384, Ala354) and S2 (His353) pockets of ACE. Among them, LVYP, VYPW and YPWT, respectively, formed eleven hydrogen bonds, six hydrogen bonds and nine hydrogen bonds with ACE. The study revealed that these peptides have the potential for the development of novel ACE inhibitor drugs and provide a new avenue for high-value utilisation of mushrooms scraps. MDPI 2022-01-29 /pmc/articles/PMC8834213/ /pubmed/35159545 http://dx.doi.org/10.3390/foods11030394 Text en © 2022 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 Wang, Rui Yun, Jianmin Wu, Shujuan Bi, Yang Zhao, Fengyun Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps |
title | Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps |
title_full | Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps |
title_fullStr | Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps |
title_full_unstemmed | Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps |
title_short | Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps |
title_sort | optimisation and characterisation of novel angiotensin-converting enzyme inhibitory peptides prepared by double enzymatic hydrolysis from agaricus bisporus scraps |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8834213/ https://www.ncbi.nlm.nih.gov/pubmed/35159545 http://dx.doi.org/10.3390/foods11030394 |
work_keys_str_mv | AT wangrui optimisationandcharacterisationofnovelangiotensinconvertingenzymeinhibitorypeptidespreparedbydoubleenzymatichydrolysisfromagaricusbisporusscraps AT yunjianmin optimisationandcharacterisationofnovelangiotensinconvertingenzymeinhibitorypeptidespreparedbydoubleenzymatichydrolysisfromagaricusbisporusscraps AT wushujuan optimisationandcharacterisationofnovelangiotensinconvertingenzymeinhibitorypeptidespreparedbydoubleenzymatichydrolysisfromagaricusbisporusscraps AT biyang optimisationandcharacterisationofnovelangiotensinconvertingenzymeinhibitorypeptidespreparedbydoubleenzymatichydrolysisfromagaricusbisporusscraps AT zhaofengyun optimisationandcharacterisationofnovelangiotensinconvertingenzymeinhibitorypeptidespreparedbydoubleenzymatichydrolysisfromagaricusbisporusscraps |