Identification by hydrophilic interaction and reversed-phase liquid chromatography-tandem mass spectrometry of peptides with antioxidant capacity in food residues
Identifiers
Permanent link (URI): http://hdl.handle.net/10017/24608DOI: 10.1016/j.chroma.2015.07.032
ISSN: 0021-9673
Publisher
Elsevier
Date
2016Embargo end date
2017-07-12Bibliographic citation
Journal of Chromatography A, 2016, v.1428, n.8, p.185-192
Keywords
Hydrophilic interaction
Reversed-phase
Liquid chromatography–tandem mass spectrometry
Peptides
Antioxidant
Peach seed
Project
info:eu-repo/grantAgreement/MINECO//AGL2012-36362/ES/VALORIZACION DE RESIDUOS SOLIDOS VEGETALES PROCEDENTES DE LA INDUSTRIA AGROALIMENTARIA/
S2013/ABI-3028/AVANSECAL (Comunidad de Madrid)
CCG2013/EXP-028 (Universidad de Alcalá)
Document type
info:eu-repo/semantics/article
Version
info:eu-repo/semantics/acceptedVersion
Publisher's version
http://dx.doi.org/10.1016/j.chroma.2015.07.032Rights
Atribución-NoComercial-SinDerivadas 3.0 España
© Elsevier, 2015
Access rights
info:eu-repo/semantics/openAccess
Abstract
HILIC- and RP-HPLC-ESI-Q-TOF identification of bioactive peptides with antioxidant capacity in peach by-products was carried out. Peach seeds contain more than 40% of proteins (as dried and defatted basis) and could constitute a cheap source of bioactive peptides. Extracted proteins were digested using four different commercial enzymes. Five assays based on different antioxidant mechanisms were employed for a reliable evaluation of the antioxidant capacity of the extracts. Thermolysin enzyme originated the extract with the most favorable antioxidant capacity. Probably due to a synergic effect among antioxidant peptides, it was not possible to find a peptide fraction with a higher antioxidant capacity than the whole extract. Eighteen peptides were identified in the whole hydrolysate when combining HILIC- and RP-HPLC-ESI-Q-TOF. A high percentage of hydrophobic amino acids were observed within their sequences which is a characteristic feature of the antioxidant nature of peptides.
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