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Description

Hypertension is a global health concern, and food-derived bioactive peptides are being explored as safer alternatives to synthetic antihypertensive drugs. In our previous study, peanut protein hydrolysate (PPH), produced via Alcalase© hydrolysis, showed significant ACE- and renin-inhibitory activities, suggesting potential antihypertensive benefits. However, its bioactivity may be influenced by digestion. This study investigates the effects of simulated gastrointestinal digestion on PPH’s ACE-inhibitory activity and secondary structure. PPH was digested using pepsin and pancreatin separately or sequentially at varying enzyme concentrations and digestion times. The antihypertensive potential of the digests was evaluated by ACE-inhibitory activity, and structural changes were characterized by FTIR. Results indicated that longer digestion times and higher enzyme concentrations enhanced ACE inhibition, suggesting the formation of smaller bioactive peptides. SDS-PAGE revealed protein degradation and the presence of peptides resistant to digestion. FTIR spectra revealed significant changes in PPH’s secondary structure post-digestion, which may also contribute to enhanced bioactivity. These findings suggest that gastrointestinal digestion enhances PPH’s bioavailability and antihypertensive potential, highlighting the role of structural changes in bioactivity improvement. Thus, PPH may serve as a promising and safer alternative to conventional drugs for hypertension management.

Publication Date

4-1-2025

Keywords

ACE: Angiotensinconverting enzyme, SDSPAGE: Sodium dodecyl sulfate– polyacrylamide gel electrophoresis, FTIR: Fourier transform infrared spectroscopy

Peanut Protein Hydrolysate: Its ACE-Inhibitory Activity and Secondary Structure as Affected by Simulated Gastrointestinal Digestion

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