Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles

Detalhes bibliográficos
Autor(a) principal: Bezerra, Taliana Kênia Alencar; et al.
Data de Publicação: 2019
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório do Instituto de Tecnologia de Alimentos
Texto Completo: http://repositorio.ital.sp.gov.br/jspui/handle/123456789/419
Resumo: Peptides from protein hydrolysate of a mixture of chicken combs and wattles (CCWs) were obtained through enzymatic hydrolysis, and their anticoagulant and inhibitory effects on angiotensin I-converting enzyme (ACE) were investigated. The protein hydrolysate exhibited anticoagulant capacity by the intrinsic pathway (activated partial thromboplastin time) and potent ACE-inhibitory activity. The peptides were sequenced by LC-MS to identify those with higher inhibitory potential. From the pool of sequenced peptides, the following three peptides were selected and synthesized based on their low molecular weight and the presence of amino acids with ACE-inhibitory potential at the C-terminus: peptide I (APGLPGPR), peptide II (Piro-GPPGPT), and peptide III (FPGPPGP). Peptide III (FPGPPGP) showed the highest ACE-inhibitory capacity among the peptides selected. In conclusion, a peptide (FPGPPGP) of unknown sequence was identified as having potent ACEinhibitory capacity. This peptide originated from unconventional hydrolysates from poultry slaughter waste, including combs and wattles.
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spelling Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and WattlesBioactive assaysChicken collagenEnzymatic proteolysisPeptide sequencesPeptide synthesisPeptides from protein hydrolysate of a mixture of chicken combs and wattles (CCWs) were obtained through enzymatic hydrolysis, and their anticoagulant and inhibitory effects on angiotensin I-converting enzyme (ACE) were investigated. The protein hydrolysate exhibited anticoagulant capacity by the intrinsic pathway (activated partial thromboplastin time) and potent ACE-inhibitory activity. The peptides were sequenced by LC-MS to identify those with higher inhibitory potential. From the pool of sequenced peptides, the following three peptides were selected and synthesized based on their low molecular weight and the presence of amino acids with ACE-inhibitory potential at the C-terminus: peptide I (APGLPGPR), peptide II (Piro-GPPGPT), and peptide III (FPGPPGP). Peptide III (FPGPPGP) showed the highest ACE-inhibitory capacity among the peptides selected. In conclusion, a peptide (FPGPPGP) of unknown sequence was identified as having potent ACEinhibitory capacity. This peptide originated from unconventional hydrolysates from poultry slaughter waste, including combs and wattles.Bezerra, Taliana Kênia Alencar; et al.2022-09-01T13:59:43Z2022-09-01T13:59:43Z2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfJournal of Medicinal Food, v. 22, n. 12, 2019. DOI: 10.1089/jmf.2019.0066.http://repositorio.ital.sp.gov.br/jspui/handle/123456789/419reponame:Repositório do Instituto de Tecnologia de Alimentosinstname:Instituto de Tecnologia de Alimentos (ITAL)instacron:ITALenginfo:eu-repo/semantics/openAccess2022-09-01T13:59:44Zoai:http://repositorio.ital.sp.gov.br:123456789/419Repositório InstitucionalPUBhttp://repositorio.ital.sp.gov.br/oai/requestbjftsec@ital.sp.gov.br || bjftsec@ital.sp.gov.bropendoar:2022-09-01T13:59:44Repositório do Instituto de Tecnologia de Alimentos - Instituto de Tecnologia de Alimentos (ITAL)false
dc.title.none.fl_str_mv Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
title Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
spellingShingle Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
Bezerra, Taliana Kênia Alencar; et al.
Bioactive assays
Chicken collagen
Enzymatic proteolysis
Peptide sequences
Peptide synthesis
title_short Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
title_full Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
title_fullStr Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
title_full_unstemmed Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
title_sort Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
author Bezerra, Taliana Kênia Alencar; et al.
author_facet Bezerra, Taliana Kênia Alencar; et al.
author_role author
dc.contributor.none.fl_str_mv







dc.contributor.author.fl_str_mv Bezerra, Taliana Kênia Alencar; et al.
dc.subject.none.fl_str_mv

dc.subject.por.fl_str_mv Bioactive assays
Chicken collagen
Enzymatic proteolysis
Peptide sequences
Peptide synthesis
topic Bioactive assays
Chicken collagen
Enzymatic proteolysis
Peptide sequences
Peptide synthesis
description Peptides from protein hydrolysate of a mixture of chicken combs and wattles (CCWs) were obtained through enzymatic hydrolysis, and their anticoagulant and inhibitory effects on angiotensin I-converting enzyme (ACE) were investigated. The protein hydrolysate exhibited anticoagulant capacity by the intrinsic pathway (activated partial thromboplastin time) and potent ACE-inhibitory activity. The peptides were sequenced by LC-MS to identify those with higher inhibitory potential. From the pool of sequenced peptides, the following three peptides were selected and synthesized based on their low molecular weight and the presence of amino acids with ACE-inhibitory potential at the C-terminus: peptide I (APGLPGPR), peptide II (Piro-GPPGPT), and peptide III (FPGPPGP). Peptide III (FPGPPGP) showed the highest ACE-inhibitory capacity among the peptides selected. In conclusion, a peptide (FPGPPGP) of unknown sequence was identified as having potent ACEinhibitory capacity. This peptide originated from unconventional hydrolysates from poultry slaughter waste, including combs and wattles.
publishDate 2019
dc.date.none.fl_str_mv




2019
2022-09-01T13:59:43Z
2022-09-01T13:59:43Z
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.none.fl_str_mv

dc.identifier.uri.fl_str_mv Journal of Medicinal Food, v. 22, n. 12, 2019. DOI: 10.1089/jmf.2019.0066.
http://repositorio.ital.sp.gov.br/jspui/handle/123456789/419
identifier_str_mv
Journal of Medicinal Food, v. 22, n. 12, 2019. DOI: 10.1089/jmf.2019.0066.
url http://repositorio.ital.sp.gov.br/jspui/handle/123456789/419
dc.language.none.fl_str_mv
dc.language.iso.fl_str_mv eng
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language eng
dc.rights.none.fl_str_mv

dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv

application/pdf
dc.publisher.none.fl_str_mv

publisher.none.fl_str_mv

dc.source.none.fl_str_mv
reponame:Repositório do Instituto de Tecnologia de Alimentos
instname:Instituto de Tecnologia de Alimentos (ITAL)
instacron:ITAL
instname_str Instituto de Tecnologia de Alimentos (ITAL)
instacron_str ITAL
institution ITAL
reponame_str Repositório do Instituto de Tecnologia de Alimentos
collection Repositório do Instituto de Tecnologia de Alimentos
repository.name.fl_str_mv Repositório do Instituto de Tecnologia de Alimentos - Instituto de Tecnologia de Alimentos (ITAL)
repository.mail.fl_str_mv bjftsec@ital.sp.gov.br || bjftsec@ital.sp.gov.br
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