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. 2016 Jan 8:1428:185-92.
doi: 10.1016/j.chroma.2015.07.032. Epub 2015 Jul 11.

Identification by hydrophilic interaction and reversed-phase liquid chromatography-tandem mass spectrometry of peptides with antioxidant capacity in food residues

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Identification by hydrophilic interaction and reversed-phase liquid chromatography-tandem mass spectrometry of peptides with antioxidant capacity in food residues

Romy Vásquez-Villanueva et al. J Chromatogr A. .

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.

Keywords: Antioxidant; Hydrophilic interaction; Liquid chromatography–tandem mass spectrometry; Peach seed; Peptides; Reversed-phase.

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