Abstract
The work was designed to assess the amelioration effect of papain hydrolysis on the biochemical, techno-functional, 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 α-helix to β-turn structure, indicating the unfolding of protein structure. This structural alteration positively influenced the functional characteristics, 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 α-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 α-glucosidase and ACE was more effective than pancreatic lipase, suggesting their usefulness as a functional ingredient, particularly in type II diabetes and hypertension management.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: International Journal of Biological Macromolecules
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
