Peptidomics profiling and biological activities of grape pomace protein hydrolysates

Autores
Knuf, Franziska; Caspers Weiffenbach, Rita; Schieber, Andreas; Fontana, Ariel Ramón
Año de publicación
2025
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Grape pomace protein isolate was hydrolysed by Alcalase, Flavourzyme and Protease either individually or in combination to produce hydrolysates with antihypertensive and antimicrobial properties. The degree of hydrolysis (DH) ranged between 22 and 52 % for Protease and Flavourzyme, respectively. Among all treatments, hydrolysates prepared using Flavourzyme exhibited the highest angiotensin-converting enzyme inhibitory (ACEi) activity, with an IC50 value of 91 μg/mL. The peptidomics analysis revealed that the peptides identified in Flavourzyme hydrolysate presented molecular features compatible with its bioactivity, like a high density ofACEi sequences per peptide. The hydrolysates were also able to inhibit the growth of Escherichia coli in a range between 9 and 54 % for Alcalase and Alcalase + Flavourzyme, respectively. Peptides in the most active hydrolysate evidenced a high occurrence of proline residues, which is a structural feature of some antimicrobial peptides.
Fil: Knuf, Franziska. Universitat Bonn; Alemania
Fil: Caspers Weiffenbach, Rita. Universitat Bonn; Alemania
Fil: Schieber, Andreas. Universitat Bonn; Alemania
Fil: Fontana, Ariel Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
Materia
GRAPE POMACE
ENZYMATIC HYDROLYSIS
BIOACTIVE PEPTIDES
ANGIOTENSIN I CONVERTING ENZYME INHIBITORY ACTIVITY
ANTIMICROBIAL ACTIVITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/281433
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Peptidomics profiling and biological activities of grape pomace protein hydrolysatesKnuf, FranziskaCaspers Weiffenbach, RitaSchieber, AndreasFontana, Ariel RamónGRAPE POMACEENZYMATIC HYDROLYSISBIOACTIVE PEPTIDESANGIOTENSIN I CONVERTING ENZYME INHIBITORY ACTIVITYANTIMICROBIAL ACTIVITYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Grape pomace protein isolate was hydrolysed by Alcalase, Flavourzyme and Protease either individually or in combination to produce hydrolysates with antihypertensive and antimicrobial properties. The degree of hydrolysis (DH) ranged between 22 and 52 % for Protease and Flavourzyme, respectively. Among all treatments, hydrolysates prepared using Flavourzyme exhibited the highest angiotensin-converting enzyme inhibitory (ACEi) activity, with an IC50 value of 91 μg/mL. The peptidomics analysis revealed that the peptides identified in Flavourzyme hydrolysate presented molecular features compatible with its bioactivity, like a high density ofACEi sequences per peptide. The hydrolysates were also able to inhibit the growth of Escherichia coli in a range between 9 and 54 % for Alcalase and Alcalase + Flavourzyme, respectively. Peptides in the most active hydrolysate evidenced a high occurrence of proline residues, which is a structural feature of some antimicrobial peptides.Fil: Knuf, Franziska. Universitat Bonn; AlemaniaFil: Caspers Weiffenbach, Rita. Universitat Bonn; AlemaniaFil: Schieber, Andreas. Universitat Bonn; AlemaniaFil: Fontana, Ariel Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; ArgentinaElsevier2025-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/281433Knuf, Franziska; Caspers Weiffenbach, Rita; Schieber, Andreas; Fontana, Ariel Ramón; Peptidomics profiling and biological activities of grape pomace protein hydrolysates; Elsevier; Food Chemistry; 463; 1-2025; 1-100308-8146CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0308814624026827info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2024.141032info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-26T10:05:25Zoai:ri.conicet.gov.ar:11336/281433instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-02-26 10:05:25.672CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Peptidomics profiling and biological activities of grape pomace protein hydrolysates
title Peptidomics profiling and biological activities of grape pomace protein hydrolysates
spellingShingle Peptidomics profiling and biological activities of grape pomace protein hydrolysates
Knuf, Franziska
GRAPE POMACE
ENZYMATIC HYDROLYSIS
BIOACTIVE PEPTIDES
ANGIOTENSIN I CONVERTING ENZYME INHIBITORY ACTIVITY
ANTIMICROBIAL ACTIVITY
title_short Peptidomics profiling and biological activities of grape pomace protein hydrolysates
title_full Peptidomics profiling and biological activities of grape pomace protein hydrolysates
title_fullStr Peptidomics profiling and biological activities of grape pomace protein hydrolysates
title_full_unstemmed Peptidomics profiling and biological activities of grape pomace protein hydrolysates
title_sort Peptidomics profiling and biological activities of grape pomace protein hydrolysates
dc.creator.none.fl_str_mv Knuf, Franziska
Caspers Weiffenbach, Rita
Schieber, Andreas
Fontana, Ariel Ramón
author Knuf, Franziska
author_facet Knuf, Franziska
Caspers Weiffenbach, Rita
Schieber, Andreas
Fontana, Ariel Ramón
author_role author
author2 Caspers Weiffenbach, Rita
Schieber, Andreas
Fontana, Ariel Ramón
author2_role author
author
author
dc.subject.none.fl_str_mv GRAPE POMACE
ENZYMATIC HYDROLYSIS
BIOACTIVE PEPTIDES
ANGIOTENSIN I CONVERTING ENZYME INHIBITORY ACTIVITY
ANTIMICROBIAL ACTIVITY
topic GRAPE POMACE
ENZYMATIC HYDROLYSIS
BIOACTIVE PEPTIDES
ANGIOTENSIN I CONVERTING ENZYME INHIBITORY ACTIVITY
ANTIMICROBIAL ACTIVITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Grape pomace protein isolate was hydrolysed by Alcalase, Flavourzyme and Protease either individually or in combination to produce hydrolysates with antihypertensive and antimicrobial properties. The degree of hydrolysis (DH) ranged between 22 and 52 % for Protease and Flavourzyme, respectively. Among all treatments, hydrolysates prepared using Flavourzyme exhibited the highest angiotensin-converting enzyme inhibitory (ACEi) activity, with an IC50 value of 91 μg/mL. The peptidomics analysis revealed that the peptides identified in Flavourzyme hydrolysate presented molecular features compatible with its bioactivity, like a high density ofACEi sequences per peptide. The hydrolysates were also able to inhibit the growth of Escherichia coli in a range between 9 and 54 % for Alcalase and Alcalase + Flavourzyme, respectively. Peptides in the most active hydrolysate evidenced a high occurrence of proline residues, which is a structural feature of some antimicrobial peptides.
Fil: Knuf, Franziska. Universitat Bonn; Alemania
Fil: Caspers Weiffenbach, Rita. Universitat Bonn; Alemania
Fil: Schieber, Andreas. Universitat Bonn; Alemania
Fil: Fontana, Ariel Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
description Grape pomace protein isolate was hydrolysed by Alcalase, Flavourzyme and Protease either individually or in combination to produce hydrolysates with antihypertensive and antimicrobial properties. The degree of hydrolysis (DH) ranged between 22 and 52 % for Protease and Flavourzyme, respectively. Among all treatments, hydrolysates prepared using Flavourzyme exhibited the highest angiotensin-converting enzyme inhibitory (ACEi) activity, with an IC50 value of 91 μg/mL. The peptidomics analysis revealed that the peptides identified in Flavourzyme hydrolysate presented molecular features compatible with its bioactivity, like a high density ofACEi sequences per peptide. The hydrolysates were also able to inhibit the growth of Escherichia coli in a range between 9 and 54 % for Alcalase and Alcalase + Flavourzyme, respectively. Peptides in the most active hydrolysate evidenced a high occurrence of proline residues, which is a structural feature of some antimicrobial peptides.
publishDate 2025
dc.date.none.fl_str_mv 2025-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/281433
Knuf, Franziska; Caspers Weiffenbach, Rita; Schieber, Andreas; Fontana, Ariel Ramón; Peptidomics profiling and biological activities of grape pomace protein hydrolysates; Elsevier; Food Chemistry; 463; 1-2025; 1-10
0308-8146
CONICET Digital
CONICET
url http://hdl.handle.net/11336/281433
identifier_str_mv Knuf, Franziska; Caspers Weiffenbach, Rita; Schieber, Andreas; Fontana, Ariel Ramón; Peptidomics profiling and biological activities of grape pomace protein hydrolysates; Elsevier; Food Chemistry; 463; 1-2025; 1-10
0308-8146
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0308814624026827
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2024.141032
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.176822

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