FOOD AND BIOPROCESS TECHNOLOGY, cilt.18, sa.12, ss.10620-10635, 2025 (SCI-Expanded, Scopus)
Bioactive hydrolysates were generated from limpet (Patella vulgata) protein concentrate (LPC) utilising Alcalase (TM) and Flavourzyme (TM) followed by simulated gastrointestinal digestion (SGID). Samples were analysed using gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GP-HPLC), while in vitro antioxidant (FRAP, ORAC and ABTS(center dot+)) and angiotensin-converting enzyme (ACE) inhibitory activities were employed to evaluate bioactivity. Alcalase was more effective than Flavourzyme in hydrolysing LPC, achieving a significantly higher (p < 0.05) amino nitrogen content after digestion, i.e., 29.50 +/- 0.69 vs. 21.06 +/- 1.04 mg g(-1) protein, respectively. The hydrolysates exhibited enhancements in some biological activities following SGID, with significant (p < 0.05) increases in antioxidant (except for the ORAC and FRAP activities in the Alcalase hydrolysates) and ACE inhibitory activities. The antioxidant activity of Alcalase-generated hydrolysates declined significantly during gastric digestion but was subsequently enhanced in the intestinal digestion phase. In contrast, the Flavourzyme-generated hydrolysates exhibited a progressive increase in antioxidant activity throughout SGID, with the highest levels observed following pepsin and Pancreatin (TM) incubation. In comparison with digestion where only SGID was conducted, the inclusion of a pre-enzymatic hydrolysis step with Alcalase prior to SGID led to significant improvements in both antioxidant (as measured by the ABTS assay, 360.92 +/- 18.32 mu mol Trolox Equivalents g(-)(1) protein) and ACE inhibitory activity (81.5% inhibition, at a final sample concentration of 0.2 mg mL(-1)). These findings highlight the potential health benefits of protein hydrolysates from limpet and their applicability in the food and health industries, underscoring the value of marine-derived proteins in developing bioactive compounds.