Insights into digestibility, biological activity, and peptide profiling of flaxseed protein isolates treated by ultrasound coupled with alkali cycling.

ABSTRACT

This study aims to investigate the effects of ultrasound coupled with alkali cycling on the structural properties, digestion characteristics, biological activity, and peptide profiling of flaxseed protein isolates (FPI). The digestibility of FPI obtained by ultrasound coupled with pH 10/12 cycling (UFPI-10/12) (74.56 % and 79.12 %) was significantly higher than that of native FPI (64.40 %), and UFPI-10 showed higher hydrolysis degree (35.76 %) than FPI (30.65 %) after intestinal digestion. The combined treatment induced transition from α-helix to ß-sheet with an orderly structure. Large FPI aggregates broke down into small-sized FPI particles, which induced the increase of specific surface area of particles. This might expose more cutting sites and contact area with enzymes. Furthermore, UFPI-10 showed high antioxidant activity (29.18 %) and lipid-lowering activity (70.52 %). Peptide profiling revealed that UFPI-10 exhibited a higher proportion of 300-600 Da peptides and significantly higher abundance of antioxidant peptides than native FPI, which might promote its antioxidant activity. Those results suggest that the combined treatment is a promising modification method to improve the digestion characteristics and biological activity of FPI. This work provides new ideas for widespread use of FPI as an active stabilizer in food systems.