Identification by hydrophilic interaction and reversed-phase liquid chromatography-tandem mass spectrometry of peptides with antioxidant capacity in food residues
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 us...
| Autores: | , , |
|---|---|
| Formato: | artículo |
| Fecha de publicación: | 2016 |
| País: | España |
| Recursos: | Universidad de Alcalá (UAH) |
| Repositorio: | e_Buah Biblioteca Digital Universidad de Alcalá |
| Idioma: | inglés |
| OAI Identifier: | oai:ebuah.uah.es:10017/24608 |
| Acesso em linha: | http://hdl.handle.net/10017/24608 https://dx.doi.org/10.1016/j.chroma.2015.07.032 |
| Access Level: | acceso abierto |
| Palavra-chave: | Hydrophilic interaction Reversed-phase Liquid chromatography–tandem mass spectrometry Peptides Antioxidant Peach seed Ciencia Química Science Chemistry |
| Resumo: | 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. |
|---|