Publications
- Année de publication : 2017-01-01
Référence
V. Perreault, L. Hénaux, L. Bazinet, A. Doyen. 2017. Pretreatment of flaxseed protein isolate by high hydrostatic pressure: impacts on protein structure, enzymatic hydrolysis and final hydrolysate antioxidant capacities. Food Chemistry, 221, 1805-1812.
Information Complémentaire
Lien vers l'article : https://www.sciencedirect.com/science/article/abs/pii/S0308814616317782
Mot(s) Clé(s)
Isolat de protéine Lin Hydrolyse enzymatique Hautes pressions hydrostatiques Structures protéiques Antioxydants
Résumé
The effect of high hydrostatic pressure (HHP) on flaxseed protein structure and peptide profiles, obtained after protein hydrolysis, was investigated. Isolated flaxseed protein (1%, m/v) was subjected to HHP (600 MPa, 5 min or 20 min at 20 °C) prior to hydrolysis with trypsin only and trypsin-pronase. The results demonstrated that HHP treatment induced dissociation of flaxseed proteins and generated higher molecular weight aggregates as a function of processing duration. Fluorescence spectroscopy showed that HHP treatment, as well as processing duration, had an impact on flaxseed protein structure since exposition of hydrophobic amino acid tyrosine was modified. Except for some specific peptides, the concentrations of which were modified, similar peptide profiles were obtained after hydrolysis of pressure-treated proteins using trypsin. Finally, hydrolysates obtained using trypsin-pronase had a greater antioxidant capacity (ORAC) than control samples; these results confirmed that HHP enhanced the generation of antioxidant peptides.
