Characterization of Bromelain-Soluble Sheepskin (Ovis aries) Proteins and Effect of In Vitro Gastrointestinal Digestion on Angiotensin Converting Enzyme Inhibition Activity.

ABSTRACT: This work characterizes proteins extracted from sheepskin using bromelain and examines angiotensin converting enzyme (ACE) inhibition activity of the peptides generated by in vitro gastrointestinal digestion (GID). Gel electrophoresis revealed three major protein bands corresponding to keratin and collagen. In vitro gastrointestinal digestion facilitated protein breakdown into peptides, yielding below 3 kDa of molecular weight peptides. Arginine, tyrosine, lysine, and leucine were identified as the major residues of amino acids in the bromelain-soluble protein hydrolysate (BSPH). The action of inhibiting ACE of 1 mg/mL of BSPH was 48.99%, whereas the activity of the < 3 kDa ultra-filtrated fractions obtained before and after in vitro GID were 0% and 19.94%, respectively. To acquire the pep

SUBMITTER: Putri DPT 

PROVIDER: S-EPMC12848775 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature