Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity

Casein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC–MS/MS for peptide identification. A strain-dependent peptide profile could be observed, regardless of the casein ori...

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Detalhes bibliográficos
Autores: Zohra Bounouala, Fatima, Roudj, Salima, Karam, Nour-Eddine, Recio, Isidra, Miralles, Beatriz
Tipo de documento: artigo
Estado:Versión aceptada para publicación
Data de publicação:2017
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/194029
Acesso em linha:http://hdl.handle.net/10261/194029
Access Level:Acceso aberto
Palavra-chave:Lactic acid bacteria
Enzyme specificity
Bioactive peptides
Tandem mass spectrometry
Sheep milk
Casein hydrolysates
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spelling Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificityZohra Bounouala, FatimaRoudj, SalimaKaram, Nour-EddineRecio, IsidraMiralles, BeatrizLactic acid bacteriaEnzyme specificityBioactive peptidesTandem mass spectrometrySheep milkCasein hydrolysatesCasein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC–MS/MS for peptide identification. A strain-dependent peptide profile could be observed, regardless of the casein origin, and the specificity of these two proteases could be computationally ascribed. The cleavage pattern yielding phenylalanine, leucine, or tyrosine at C-terminal appeared both at L. lactis and Lb. brevis hydrolysates. However, the cleavage C-terminal to lysine was favored with Lb. brevis protease. The hydrolysates showed ACE-inhibitory activity with IC50 in the 16–70 μg/mL range. Ovine casein hydrolysates yielded greater ACE-inhibitory activity. Previously described antihypertensive and opioid peptides were found in these ovine and bovine casein hydrolysates and prediction of the antihypertensive activity of the sequences based on quantitative structure and activity relationship (QSAR) was performed. This approach might represent a useful classification tool regarding health-related properties prior to further purification.This work has received financial support from Project AGL2015-66886-R from the Spanish Ministry of Economy and Competitiveness (MINECO). F.Z.B. gratefully acknowledges the financial support of the DGRSDT (Grant 012/2000) and the Ministry of Higher Education and Scientific Research Government (MESRS) of Algeria.Peer reviewedAmerican Chemical SocietyMinisterio de Economía y Competitividad (España)Ministère de l'Enseignement Supérieur et de la Recherche Scientifique (Algerie)Miralles, Beatriz [0000-0003-4544-9074]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201920192017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/194029reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2015-66886-Rhttps://doi.org/10.1021/acs.jafc.7b03203Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1940292026-05-22T06:33:51Z
dc.title.none.fl_str_mv Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
title Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
spellingShingle Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
Zohra Bounouala, Fatima
Lactic acid bacteria
Enzyme specificity
Bioactive peptides
Tandem mass spectrometry
Sheep milk
Casein hydrolysates
title_short Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
title_full Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
title_fullStr Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
title_full_unstemmed Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
title_sort Casein hydrolysates by Lactobacillus brevis and Lactococcus lactis proteases: Peptide profile discriminates strain-dependent enzyme specificity
dc.creator.none.fl_str_mv Zohra Bounouala, Fatima
Roudj, Salima
Karam, Nour-Eddine
Recio, Isidra
Miralles, Beatriz
author Zohra Bounouala, Fatima
author_facet Zohra Bounouala, Fatima
Roudj, Salima
Karam, Nour-Eddine
Recio, Isidra
Miralles, Beatriz
author_role author
author2 Roudj, Salima
Karam, Nour-Eddine
Recio, Isidra
Miralles, Beatriz
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Ministère de l'Enseignement Supérieur et de la Recherche Scientifique (Algerie)
Miralles, Beatriz [0000-0003-4544-9074]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Lactic acid bacteria
Enzyme specificity
Bioactive peptides
Tandem mass spectrometry
Sheep milk
Casein hydrolysates
topic Lactic acid bacteria
Enzyme specificity
Bioactive peptides
Tandem mass spectrometry
Sheep milk
Casein hydrolysates
description Casein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC–MS/MS for peptide identification. A strain-dependent peptide profile could be observed, regardless of the casein origin, and the specificity of these two proteases could be computationally ascribed. The cleavage pattern yielding phenylalanine, leucine, or tyrosine at C-terminal appeared both at L. lactis and Lb. brevis hydrolysates. However, the cleavage C-terminal to lysine was favored with Lb. brevis protease. The hydrolysates showed ACE-inhibitory activity with IC50 in the 16–70 μg/mL range. Ovine casein hydrolysates yielded greater ACE-inhibitory activity. Previously described antihypertensive and opioid peptides were found in these ovine and bovine casein hydrolysates and prediction of the antihypertensive activity of the sequences based on quantitative structure and activity relationship (QSAR) was performed. This approach might represent a useful classification tool regarding health-related properties prior to further purification.
publishDate 2017
dc.date.none.fl_str_mv 2017
2019
2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/194029
url http://hdl.handle.net/10261/194029
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2015-66886-R
https://doi.org/10.1021/acs.jafc.7b03203
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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