Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes

Defatted grape seed meal (DGSM) is a residue obtained from grape pomace and is an important source of protein. The aim of this study was to select peptides with optimal antioxidant and colour properties, obtained using enzymes of different origins and proteolytic character, for application in winema...

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Main Authors: María del Rosario Rodríguez-Muñoz, Ana Belén Mora-Garrido, Francisco J. Heredia, María Jesús Cejudo-Bastante, María Lourdes González-Miret
Format: Article
Language:English
Published: MDPI AG 2025-04-01
Series:Foods
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Online Access:https://www.mdpi.com/2304-8158/14/7/1248
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author María del Rosario Rodríguez-Muñoz
Ana Belén Mora-Garrido
Francisco J. Heredia
María Jesús Cejudo-Bastante
María Lourdes González-Miret
author_facet María del Rosario Rodríguez-Muñoz
Ana Belén Mora-Garrido
Francisco J. Heredia
María Jesús Cejudo-Bastante
María Lourdes González-Miret
author_sort María del Rosario Rodríguez-Muñoz
collection DOAJ
description Defatted grape seed meal (DGSM) is a residue obtained from grape pomace and is an important source of protein. The aim of this study was to select peptides with optimal antioxidant and colour properties, obtained using enzymes of different origins and proteolytic character, for application in winemaking. For this purpose, the assay was performed using novo-ProD (NP), alcalase (AL), novozym (NZ), pepsin (PE), flavourzyme (FZ), and papain (PA) enzymes. The peptide percentage, peptide yield, molecular size of the peptide fractions, total amino acid, peptide content, antioxidant activity, and CIELAB colour coordinates of the hydrolysates were determined. The peptide hydrolysates obtained using PE showed the significantly (<i>p</i> < 0.05) highest percentages of peptides (93%), amino acid content (188 mg aa/g hydrolysate), and lightness (L*, 70.3). On the other hand, NP peptide hydrolysates displayed the significantly (<i>p</i> < 0.05) highest antioxidant activity (154 µmol TE/g hydrolysate) and peptide yield (39%). Regarding molecular weight (MW), PE led to hydrolysates with a lower proportion of low-MW peptides (MW < 1 kDa). In conclusion, the peptide hydrolysates obtained by NP and PE exhibited the greatest chemical characteristics for further application, both separately and combined in targeted hydrolysis, as colour stabilisers and antioxidant capacity enhancers in warm climate winemaking.
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spelling doaj-art-a987c0e85b2f4fe29d168fb3c19e76df2025-08-20T03:08:53ZengMDPI AGFoods2304-81582025-04-01147124810.3390/foods14071248Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different EnzymesMaría del Rosario Rodríguez-Muñoz0Ana Belén Mora-Garrido1Francisco J. Heredia2María Jesús Cejudo-Bastante3María Lourdes González-Miret4Food Colour & Quality Laboratory, Facultad de Farmacia, Universidad de Sevilla, 41012 Sevilla, SpainFood Colour & Quality Laboratory, Facultad de Farmacia, Universidad de Sevilla, 41012 Sevilla, SpainFood Colour & Quality Laboratory, Facultad de Farmacia, Universidad de Sevilla, 41012 Sevilla, SpainFood Colour & Quality Laboratory, Facultad de Farmacia, Universidad de Sevilla, 41012 Sevilla, SpainFood Colour & Quality Laboratory, Facultad de Farmacia, Universidad de Sevilla, 41012 Sevilla, SpainDefatted grape seed meal (DGSM) is a residue obtained from grape pomace and is an important source of protein. The aim of this study was to select peptides with optimal antioxidant and colour properties, obtained using enzymes of different origins and proteolytic character, for application in winemaking. For this purpose, the assay was performed using novo-ProD (NP), alcalase (AL), novozym (NZ), pepsin (PE), flavourzyme (FZ), and papain (PA) enzymes. The peptide percentage, peptide yield, molecular size of the peptide fractions, total amino acid, peptide content, antioxidant activity, and CIELAB colour coordinates of the hydrolysates were determined. The peptide hydrolysates obtained using PE showed the significantly (<i>p</i> < 0.05) highest percentages of peptides (93%), amino acid content (188 mg aa/g hydrolysate), and lightness (L*, 70.3). On the other hand, NP peptide hydrolysates displayed the significantly (<i>p</i> < 0.05) highest antioxidant activity (154 µmol TE/g hydrolysate) and peptide yield (39%). Regarding molecular weight (MW), PE led to hydrolysates with a lower proportion of low-MW peptides (MW < 1 kDa). In conclusion, the peptide hydrolysates obtained by NP and PE exhibited the greatest chemical characteristics for further application, both separately and combined in targeted hydrolysis, as colour stabilisers and antioxidant capacity enhancers in warm climate winemaking.https://www.mdpi.com/2304-8158/14/7/1248grape seed peptide hydrolysatesenzymeswarm climatemolecular weight distributionantioxidant peptides
spellingShingle María del Rosario Rodríguez-Muñoz
Ana Belén Mora-Garrido
Francisco J. Heredia
María Jesús Cejudo-Bastante
María Lourdes González-Miret
Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes
Foods
grape seed peptide hydrolysates
enzymes
warm climate
molecular weight distribution
antioxidant peptides
title Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes
title_full Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes
title_fullStr Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes
title_full_unstemmed Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes
title_short Obtention and Characterisation of Antioxidant-Rich Peptides from Defatted Grape Seed Meal Using Different Enzymes
title_sort obtention and characterisation of antioxidant rich peptides from defatted grape seed meal using different enzymes
topic grape seed peptide hydrolysates
enzymes
warm climate
molecular weight distribution
antioxidant peptides
url https://www.mdpi.com/2304-8158/14/7/1248
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