Isolation and characterization of antihypertensive peptides from soy bean protein
Autor(a) principal: | |
---|---|
Data de Publicação: | 2022 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Pharmaceutical Sciences |
DOI: | 10.1590/s2175-97902020000419061 |
Texto Completo: | https://www.revistas.usp.br/bjps/article/view/204213 |
Resumo: | Proteins and peptides are the most diverse biomolecules found in nature and make our interest due to their wide applications in food and pharmaceutical industry. Angiotensin Converting Enzyme (ACE) plays a major role in controlling blood pressure. The inhibition of ACE with peptides is a main target in the regulation of hypertension. The objective of the present study was to investigate the therapeutic potential of soy bean. This was accomplished by isolation of ACE inhibitory peptides using response surface methodology (RSM) and characterization of these bioactive peptides by mass spectrometry. 31 hydrolyzed fractions were isolated and evaluated for their ACE inhibition potential. Hydrolyzed fraction having highest ACE inhibitory activity was characterized by liquid chromatography-mass spectrometry (LC-MS) technique. RSM results showed maximum ACE inhibition potential (64%) by hydrolyzate was obtained at 45 ºC temperature, pH 8.0, E/S 0.2 in 2 hours hydrolysis time. Results of LC-MS analysis revealed Ser-Gly, Ser-Pro, Met-Ala, His-Ala, Lys-Pro, Phe-Thr, Met-Leu, Pro-Arg, Ala-Pro-Val, Pro-Ala-Leu, Val-Met-Gly, Pro-Leu-Val, Pro-Pro-Gln, His-Arg-Gly, Ser-Phe-Val-Leu, Ala-Val-His-Try, Arg-Thr-Val-Arg, His-His-Tyr-Leu-Val, Asp-Gly-Ala-Cys-Ser-Ala-Asn and MetVal-Thr-Gly-Pro-Gly-Cys-His bioactive peptides in hydrolyzed fraction of soy bean. Our data provide evidence that response surface methodology is a good approach for isolation of antihypertensive bioactive peptides with more potent activity as nutraceuticals or pharmaceuticals. Therefore soy bean can be use for industrial production of pharmaceutical grade natural medicines for handling high blood pressure. |
id |
USP-31_ce15c50001e76066c85b4afce555dae8 |
---|---|
oai_identifier_str |
oai:revistas.usp.br:article/204213 |
network_acronym_str |
USP-31 |
network_name_str |
Brazilian Journal of Pharmaceutical Sciences |
spelling |
Isolation and characterization of antihypertensive peptides from soy bean proteinResponse surface methodology; Antihypertensive peptides; Optimization; Hydrolysate; ACE inhibition potentialProteins and peptides are the most diverse biomolecules found in nature and make our interest due to their wide applications in food and pharmaceutical industry. Angiotensin Converting Enzyme (ACE) plays a major role in controlling blood pressure. The inhibition of ACE with peptides is a main target in the regulation of hypertension. The objective of the present study was to investigate the therapeutic potential of soy bean. This was accomplished by isolation of ACE inhibitory peptides using response surface methodology (RSM) and characterization of these bioactive peptides by mass spectrometry. 31 hydrolyzed fractions were isolated and evaluated for their ACE inhibition potential. Hydrolyzed fraction having highest ACE inhibitory activity was characterized by liquid chromatography-mass spectrometry (LC-MS) technique. RSM results showed maximum ACE inhibition potential (64%) by hydrolyzate was obtained at 45 ºC temperature, pH 8.0, E/S 0.2 in 2 hours hydrolysis time. Results of LC-MS analysis revealed Ser-Gly, Ser-Pro, Met-Ala, His-Ala, Lys-Pro, Phe-Thr, Met-Leu, Pro-Arg, Ala-Pro-Val, Pro-Ala-Leu, Val-Met-Gly, Pro-Leu-Val, Pro-Pro-Gln, His-Arg-Gly, Ser-Phe-Val-Leu, Ala-Val-His-Try, Arg-Thr-Val-Arg, His-His-Tyr-Leu-Val, Asp-Gly-Ala-Cys-Ser-Ala-Asn and MetVal-Thr-Gly-Pro-Gly-Cys-His bioactive peptides in hydrolyzed fraction of soy bean. Our data provide evidence that response surface methodology is a good approach for isolation of antihypertensive bioactive peptides with more potent activity as nutraceuticals or pharmaceuticals. Therefore soy bean can be use for industrial production of pharmaceutical grade natural medicines for handling high blood pressure.Universidade de São Paulo. Faculdade de Ciências Farmacêuticas2022-11-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://www.revistas.usp.br/bjps/article/view/20421310.1590/s2175-97902020000419061Brazilian Journal of Pharmaceutical Sciences; Vol. 57 (2021)Brazilian Journal of Pharmaceutical Sciences; v. 57 (2021)Brazilian Journal of Pharmaceutical Sciences; Vol. 57 (2021)2175-97901984-8250reponame:Brazilian Journal of Pharmaceutical Sciencesinstname:Universidade de São Paulo (USP)instacron:USPenghttps://www.revistas.usp.br/bjps/article/view/204213/187814Copyright (c) 2022 Brazilian Journal of Pharmaceutical Scienceshttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessMujtaba, Nosheen Jahan, NazishSultana, BushraZia, Muhammad Anjum2022-11-09T20:10:30Zoai:revistas.usp.br:article/204213Revistahttps://www.revistas.usp.br/bjps/indexPUBhttps://old.scielo.br/oai/scielo-oai.phpbjps@usp.br||elizabeth.igne@gmail.com2175-97901984-8250opendoar:2022-11-09T20:10:30Brazilian Journal of Pharmaceutical Sciences - Universidade de São Paulo (USP)false |
dc.title.none.fl_str_mv |
Isolation and characterization of antihypertensive peptides from soy bean protein |
title |
Isolation and characterization of antihypertensive peptides from soy bean protein |
spellingShingle |
Isolation and characterization of antihypertensive peptides from soy bean protein Isolation and characterization of antihypertensive peptides from soy bean protein Mujtaba, Nosheen Response surface methodology; Antihypertensive peptides; Optimization; Hydrolysate; ACE inhibition potential Mujtaba, Nosheen Response surface methodology; Antihypertensive peptides; Optimization; Hydrolysate; ACE inhibition potential |
title_short |
Isolation and characterization of antihypertensive peptides from soy bean protein |
title_full |
Isolation and characterization of antihypertensive peptides from soy bean protein |
title_fullStr |
Isolation and characterization of antihypertensive peptides from soy bean protein Isolation and characterization of antihypertensive peptides from soy bean protein |
title_full_unstemmed |
Isolation and characterization of antihypertensive peptides from soy bean protein Isolation and characterization of antihypertensive peptides from soy bean protein |
title_sort |
Isolation and characterization of antihypertensive peptides from soy bean protein |
author |
Mujtaba, Nosheen |
author_facet |
Mujtaba, Nosheen Mujtaba, Nosheen Jahan, Nazish Sultana, Bushra Zia, Muhammad Anjum Jahan, Nazish Sultana, Bushra Zia, Muhammad Anjum |
author_role |
author |
author2 |
Jahan, Nazish Sultana, Bushra Zia, Muhammad Anjum |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Mujtaba, Nosheen Jahan, Nazish Sultana, Bushra Zia, Muhammad Anjum |
dc.subject.por.fl_str_mv |
Response surface methodology; Antihypertensive peptides; Optimization; Hydrolysate; ACE inhibition potential |
topic |
Response surface methodology; Antihypertensive peptides; Optimization; Hydrolysate; ACE inhibition potential |
description |
Proteins and peptides are the most diverse biomolecules found in nature and make our interest due to their wide applications in food and pharmaceutical industry. Angiotensin Converting Enzyme (ACE) plays a major role in controlling blood pressure. The inhibition of ACE with peptides is a main target in the regulation of hypertension. The objective of the present study was to investigate the therapeutic potential of soy bean. This was accomplished by isolation of ACE inhibitory peptides using response surface methodology (RSM) and characterization of these bioactive peptides by mass spectrometry. 31 hydrolyzed fractions were isolated and evaluated for their ACE inhibition potential. Hydrolyzed fraction having highest ACE inhibitory activity was characterized by liquid chromatography-mass spectrometry (LC-MS) technique. RSM results showed maximum ACE inhibition potential (64%) by hydrolyzate was obtained at 45 ºC temperature, pH 8.0, E/S 0.2 in 2 hours hydrolysis time. Results of LC-MS analysis revealed Ser-Gly, Ser-Pro, Met-Ala, His-Ala, Lys-Pro, Phe-Thr, Met-Leu, Pro-Arg, Ala-Pro-Val, Pro-Ala-Leu, Val-Met-Gly, Pro-Leu-Val, Pro-Pro-Gln, His-Arg-Gly, Ser-Phe-Val-Leu, Ala-Val-His-Try, Arg-Thr-Val-Arg, His-His-Tyr-Leu-Val, Asp-Gly-Ala-Cys-Ser-Ala-Asn and MetVal-Thr-Gly-Pro-Gly-Cys-His bioactive peptides in hydrolyzed fraction of soy bean. Our data provide evidence that response surface methodology is a good approach for isolation of antihypertensive bioactive peptides with more potent activity as nutraceuticals or pharmaceuticals. Therefore soy bean can be use for industrial production of pharmaceutical grade natural medicines for handling high blood pressure. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-11-09 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://www.revistas.usp.br/bjps/article/view/204213 10.1590/s2175-97902020000419061 |
url |
https://www.revistas.usp.br/bjps/article/view/204213 |
identifier_str_mv |
10.1590/s2175-97902020000419061 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
https://www.revistas.usp.br/bjps/article/view/204213/187814 |
dc.rights.driver.fl_str_mv |
Copyright (c) 2022 Brazilian Journal of Pharmaceutical Sciences https://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Copyright (c) 2022 Brazilian Journal of Pharmaceutical Sciences https://creativecommons.org/licenses/by/4.0 |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Universidade de São Paulo. Faculdade de Ciências Farmacêuticas |
publisher.none.fl_str_mv |
Universidade de São Paulo. Faculdade de Ciências Farmacêuticas |
dc.source.none.fl_str_mv |
Brazilian Journal of Pharmaceutical Sciences; Vol. 57 (2021) Brazilian Journal of Pharmaceutical Sciences; v. 57 (2021) Brazilian Journal of Pharmaceutical Sciences; Vol. 57 (2021) 2175-9790 1984-8250 reponame:Brazilian Journal of Pharmaceutical Sciences instname:Universidade de São Paulo (USP) instacron:USP |
instname_str |
Universidade de São Paulo (USP) |
instacron_str |
USP |
institution |
USP |
reponame_str |
Brazilian Journal of Pharmaceutical Sciences |
collection |
Brazilian Journal of Pharmaceutical Sciences |
repository.name.fl_str_mv |
Brazilian Journal of Pharmaceutical Sciences - Universidade de São Paulo (USP) |
repository.mail.fl_str_mv |
bjps@usp.br||elizabeth.igne@gmail.com |
_version_ |
1822179243250941952 |
dc.identifier.doi.none.fl_str_mv |
10.1590/s2175-97902020000419061 |