Multifunctional apple seed protein hydrolysates: Impact of enzymolysis on the biochemical, techno-functional and in vitro -glucosidase, pancreatic lipase and angiotensin-converting enzyme inhibition activities

The work was designed to assess the amelioration effect of papain hydrolysis on the biochemical, technofunctional, and biological properties of apple seed protein isolate (API) after 0-90 min of hydrolysis. Hydrolysis significantly enhanced the nutritional value (protein content > 90 %) while decreasing the average particle size. With increasing hydrolysis time, FTIR analysis revealed a transition from alpha-helix to beta-turn structure, indicating the unfolding of protein structure. This structural alteration positively influenced the functional charac-teristics, with samples hydrolyzed for 90 min exhibiting excellent solubility, higher water and oil absorption capacity, foaming capacity, and increased emulsifying activity index. Moreover, samples hydrolyzed for 90 min displayed the highest alpha-glucosidase (29.62-57.43 %), pancreatic lipase inhibition (12.87-31.08 %), and ACE inhibition (25.32-62.70 %) activity. Interestingly, the inhibiting ability of protein hydrolysates against alpha-glucosidase and ACE was more effective than pancreatic lipase, suggesting their usefulness as a functional ingredient, particularly in type II diabetes and hypertension management.