A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking

Detalhes bibliográficos
Autor(a) principal: LI,Haitao
Data de Publicação: 2022
Outros Autores: CHEN,Xiaoyan, GUO,Yan, HOU,Tao, HU,Jun
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Food Science and Technology (Campinas)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100782
Resumo: Abstract Salted duck egg white was desalted and hydrolyzed to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Single factor test and response surface design were performed to determine the best hydrolysis conditions: enzyme dosage 11875.99 U/g, substrate concentration 33.04 g/L and hydrolysis time 4 h. The fraction V (MW < 1 kDa), which exhibited the strongest ACE inhibitory activity, was characterized by HPLC-ESI-MS/MS. Eighty-three peptides were identified, and among them Ile-Leu-Lys-Pro, Ile-Asn-Ser-Trp, Ile-Arg and His-Pro-Ala were synthesized for further research. Ile-Leu-Lys-Pro exhibited the highest ACE inhibitory activity (IC50: 0.355 mM). The molecular docking studies revealed that nine amino acids contributed to stabilize the docking complex. The ACE inhibition of Ile-Leu-Lys-Pro and Ile-Asn-Ser-Trp were mainly attributed to Ile in N-terminal. The residues Glu362 and Ala332 were the important binding sites in molecular docking. This research expands the understanding of ACE inhibitory peptides from duck egg white as well as highlights an opportunity for recycling an otherwise discarded byproduct.
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spelling A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular dockingdesalted duck egg white peptides (DPs)enzymatic hydrolysisangiotensin I-converting enzyme (ACE) inhibitory peptideelectrospray ionization mass spectrometry (ESI-MS)molecular dockingAbstract Salted duck egg white was desalted and hydrolyzed to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Single factor test and response surface design were performed to determine the best hydrolysis conditions: enzyme dosage 11875.99 U/g, substrate concentration 33.04 g/L and hydrolysis time 4 h. The fraction V (MW < 1 kDa), which exhibited the strongest ACE inhibitory activity, was characterized by HPLC-ESI-MS/MS. Eighty-three peptides were identified, and among them Ile-Leu-Lys-Pro, Ile-Asn-Ser-Trp, Ile-Arg and His-Pro-Ala were synthesized for further research. Ile-Leu-Lys-Pro exhibited the highest ACE inhibitory activity (IC50: 0.355 mM). The molecular docking studies revealed that nine amino acids contributed to stabilize the docking complex. The ACE inhibition of Ile-Leu-Lys-Pro and Ile-Asn-Ser-Trp were mainly attributed to Ile in N-terminal. The residues Glu362 and Ala332 were the important binding sites in molecular docking. This research expands the understanding of ACE inhibitory peptides from duck egg white as well as highlights an opportunity for recycling an otherwise discarded byproduct.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100782Food Science and Technology v.42 2022reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.66121info:eu-repo/semantics/openAccessLI,HaitaoCHEN,XiaoyanGUO,YanHOU,TaoHU,Juneng2022-02-22T00:00:00Zoai:scielo:S0101-20612022000100782Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2022-02-22T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false
dc.title.none.fl_str_mv A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
title A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
spellingShingle A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
LI,Haitao
desalted duck egg white peptides (DPs)
enzymatic hydrolysis
angiotensin I-converting enzyme (ACE) inhibitory peptide
electrospray ionization mass spectrometry (ESI-MS)
molecular docking
title_short A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
title_full A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
title_fullStr A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
title_full_unstemmed A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
title_sort A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking
author LI,Haitao
author_facet LI,Haitao
CHEN,Xiaoyan
GUO,Yan
HOU,Tao
HU,Jun
author_role author
author2 CHEN,Xiaoyan
GUO,Yan
HOU,Tao
HU,Jun
author2_role author
author
author
author
dc.contributor.author.fl_str_mv LI,Haitao
CHEN,Xiaoyan
GUO,Yan
HOU,Tao
HU,Jun
dc.subject.por.fl_str_mv desalted duck egg white peptides (DPs)
enzymatic hydrolysis
angiotensin I-converting enzyme (ACE) inhibitory peptide
electrospray ionization mass spectrometry (ESI-MS)
molecular docking
topic desalted duck egg white peptides (DPs)
enzymatic hydrolysis
angiotensin I-converting enzyme (ACE) inhibitory peptide
electrospray ionization mass spectrometry (ESI-MS)
molecular docking
description Abstract Salted duck egg white was desalted and hydrolyzed to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Single factor test and response surface design were performed to determine the best hydrolysis conditions: enzyme dosage 11875.99 U/g, substrate concentration 33.04 g/L and hydrolysis time 4 h. The fraction V (MW < 1 kDa), which exhibited the strongest ACE inhibitory activity, was characterized by HPLC-ESI-MS/MS. Eighty-three peptides were identified, and among them Ile-Leu-Lys-Pro, Ile-Asn-Ser-Trp, Ile-Arg and His-Pro-Ala were synthesized for further research. Ile-Leu-Lys-Pro exhibited the highest ACE inhibitory activity (IC50: 0.355 mM). The molecular docking studies revealed that nine amino acids contributed to stabilize the docking complex. The ACE inhibition of Ile-Leu-Lys-Pro and Ile-Asn-Ser-Trp were mainly attributed to Ile in N-terminal. The residues Glu362 and Ala332 were the important binding sites in molecular docking. This research expands the understanding of ACE inhibitory peptides from duck egg white as well as highlights an opportunity for recycling an otherwise discarded byproduct.
publishDate 2022
dc.date.none.fl_str_mv 2022-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100782
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100782
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/fst.66121
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
dc.source.none.fl_str_mv Food Science and Technology v.42 2022
reponame:Food Science and Technology (Campinas)
instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron:SBCTA
instname_str Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron_str SBCTA
institution SBCTA
reponame_str Food Science and Technology (Campinas)
collection Food Science and Technology (Campinas)
repository.name.fl_str_mv Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
repository.mail.fl_str_mv ||revista@sbcta.org.br
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