Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications

Detalhes bibliográficos
Autor(a) principal: Oliveira, Mara Rose de
Data de Publicação: 2018
Outros Autores: Silva, Thaís Jordânia, Barros, Edvaldo, Guimarães, Valéria Monteze, Baracat-Pereira, Maria Cristina, Eller, Monique Renon, Coimbra, Jane Sélia dos Reis, Oliveira, Eduardo Basílio de
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://www.ncbi.nlm.nih.gov/pubmed/29372419
http://www.locus.ufv.br/handle/123456789/19234
Resumo: This review is focused on the state-of-art of peptides with inhibitory activity towards angiotensin I-converting enzyme (ACE) — thus, with anti-hypertensive potential — derived from enzymatic hydrolysis of caseins. Firstly, molecular characteristics of caseins relevant to a better understanding of this subject were concisely commented. Next, a brief description of the pathophysiology of hypertension was explained, focusing on the ACE role in regulation of blood pressure in human body. Then, casein-derived peptides with ACE inhibitory capacity were specifically addressed. The main in vitro and in vivo bioassays often reported in literature to assess the anti-hypertensive potential of peptides were presented, illustrated with recently published studies, and discussed in terms of advantages and limitations of both approaches. Characteristics related to amino acid composition and sequence of peptides with high ACE-inhibitory potential were also commented. Process parameters of enzymatic hydrolysis (types and origins of casein substrates, types of enzymes, pH, temperature, and times of reactions) were discussed. Patents dealing with casein-derived anti-hypertensive peptides were examined not only in terms of amino acid sequences, but also regarding their novelty claims in hydrolysis process parameters. Finally, some trends, challenges, and opportunities inferred from this literature analysis were commented, emphasizing the importance of this research topic in food products development.
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spelling Oliveira, Mara Rose deSilva, Thaís JordâniaBarros, EdvaldoGuimarães, Valéria MontezeBaracat-Pereira, Maria CristinaEller, Monique RenonCoimbra, Jane Sélia dos ReisOliveira, Eduardo Basílio de2018-05-02T13:08:34Z2018-05-02T13:08:34Z2018-01-031559-0291https://www.ncbi.nlm.nih.gov/pubmed/29372419http://www.locus.ufv.br/handle/123456789/19234This review is focused on the state-of-art of peptides with inhibitory activity towards angiotensin I-converting enzyme (ACE) — thus, with anti-hypertensive potential — derived from enzymatic hydrolysis of caseins. Firstly, molecular characteristics of caseins relevant to a better understanding of this subject were concisely commented. Next, a brief description of the pathophysiology of hypertension was explained, focusing on the ACE role in regulation of blood pressure in human body. Then, casein-derived peptides with ACE inhibitory capacity were specifically addressed. The main in vitro and in vivo bioassays often reported in literature to assess the anti-hypertensive potential of peptides were presented, illustrated with recently published studies, and discussed in terms of advantages and limitations of both approaches. Characteristics related to amino acid composition and sequence of peptides with high ACE-inhibitory potential were also commented. Process parameters of enzymatic hydrolysis (types and origins of casein substrates, types of enzymes, pH, temperature, and times of reactions) were discussed. Patents dealing with casein-derived anti-hypertensive peptides were examined not only in terms of amino acid sequences, but also regarding their novelty claims in hydrolysis process parameters. Finally, some trends, challenges, and opportunities inferred from this literature analysis were commented, emphasizing the importance of this research topic in food products development.engApplied Biochemistry and Biotechnologyp. 1-25, January 2018Springer Science+Business Media, LLC, part of Springer Natureinfo:eu-repo/semantics/openAccessAngiotensin-converting enzyme (ACE)BioprocessesHypertensionMilk proteinsNutraceuticalProteolysisAnti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applicationsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdftexto completoapplication/pdf1133238https://locus.ufv.br//bitstream/123456789/19234/1/artigo.pdf2cce3ea037d0865ccf6d952b352a5642MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/19234/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg4602https://locus.ufv.br//bitstream/123456789/19234/3/artigo.pdf.jpgc306893c998a70fd71788da7cc89b1b3MD53123456789/192342018-05-02 23:00:45.242oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-05-03T02:00:45LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
title Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
spellingShingle Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
Oliveira, Mara Rose de
Angiotensin-converting enzyme (ACE)
Bioprocesses
Hypertension
Milk proteins
Nutraceutical
Proteolysis
title_short Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
title_full Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
title_fullStr Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
title_full_unstemmed Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
title_sort Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
author Oliveira, Mara Rose de
author_facet Oliveira, Mara Rose de
Silva, Thaís Jordânia
Barros, Edvaldo
Guimarães, Valéria Monteze
Baracat-Pereira, Maria Cristina
Eller, Monique Renon
Coimbra, Jane Sélia dos Reis
Oliveira, Eduardo Basílio de
author_role author
author2 Silva, Thaís Jordânia
Barros, Edvaldo
Guimarães, Valéria Monteze
Baracat-Pereira, Maria Cristina
Eller, Monique Renon
Coimbra, Jane Sélia dos Reis
Oliveira, Eduardo Basílio de
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Oliveira, Mara Rose de
Silva, Thaís Jordânia
Barros, Edvaldo
Guimarães, Valéria Monteze
Baracat-Pereira, Maria Cristina
Eller, Monique Renon
Coimbra, Jane Sélia dos Reis
Oliveira, Eduardo Basílio de
dc.subject.pt-BR.fl_str_mv Angiotensin-converting enzyme (ACE)
Bioprocesses
Hypertension
Milk proteins
Nutraceutical
Proteolysis
topic Angiotensin-converting enzyme (ACE)
Bioprocesses
Hypertension
Milk proteins
Nutraceutical
Proteolysis
description This review is focused on the state-of-art of peptides with inhibitory activity towards angiotensin I-converting enzyme (ACE) — thus, with anti-hypertensive potential — derived from enzymatic hydrolysis of caseins. Firstly, molecular characteristics of caseins relevant to a better understanding of this subject were concisely commented. Next, a brief description of the pathophysiology of hypertension was explained, focusing on the ACE role in regulation of blood pressure in human body. Then, casein-derived peptides with ACE inhibitory capacity were specifically addressed. The main in vitro and in vivo bioassays often reported in literature to assess the anti-hypertensive potential of peptides were presented, illustrated with recently published studies, and discussed in terms of advantages and limitations of both approaches. Characteristics related to amino acid composition and sequence of peptides with high ACE-inhibitory potential were also commented. Process parameters of enzymatic hydrolysis (types and origins of casein substrates, types of enzymes, pH, temperature, and times of reactions) were discussed. Patents dealing with casein-derived anti-hypertensive peptides were examined not only in terms of amino acid sequences, but also regarding their novelty claims in hydrolysis process parameters. Finally, some trends, challenges, and opportunities inferred from this literature analysis were commented, emphasizing the importance of this research topic in food products development.
publishDate 2018
dc.date.accessioned.fl_str_mv 2018-05-02T13:08:34Z
dc.date.available.fl_str_mv 2018-05-02T13:08:34Z
dc.date.issued.fl_str_mv 2018-01-03
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv https://www.ncbi.nlm.nih.gov/pubmed/29372419
http://www.locus.ufv.br/handle/123456789/19234
dc.identifier.issn.none.fl_str_mv 1559-0291
identifier_str_mv 1559-0291
url https://www.ncbi.nlm.nih.gov/pubmed/29372419
http://www.locus.ufv.br/handle/123456789/19234
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartofseries.pt-BR.fl_str_mv p. 1-25, January 2018
dc.rights.driver.fl_str_mv Springer Science+Business Media, LLC, part of Springer Nature
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Springer Science+Business Media, LLC, part of Springer Nature
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dc.publisher.none.fl_str_mv Applied Biochemistry and Biotechnology
publisher.none.fl_str_mv Applied Biochemistry and Biotechnology
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