Anti-hypertensive peptides derived from caseins: mechanism of physiological action, production bioprocesses, and challenges for food applications
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , |
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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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 |
format |
article |
status_str |
publishedVersion |
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 |
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Springer Science+Business Media, LLC, part of Springer Nature info:eu-repo/semantics/openAccess |
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Springer Science+Business Media, LLC, part of Springer Nature |
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openAccess |
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Applied Biochemistry and Biotechnology |
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Applied Biochemistry and Biotechnology |
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