Physicochemical properties and angiotensin-I converting enzyme inhibitory activity of lipid-free ribbon fish (Lepturacanthus savala) protein hydrolysate.

ABSTRACT: The study aims at removal of lipid from ribbon fish protein hydrolysate (FPH) to enhance the protein content and analyse its physicochemical and bioactive properties. Ribbon fish protein hydrolysate was prepared using commercially available papain enzyme (1.5% w/v for 4 h). The resulting supernatant was further treated with lipase (0.5-2.0% w/v for 1-5 h). The treatment used in this study reduced ~ 98% of lipids depending on the enzyme concentration, temperature, pH, and duration of the treatment. Lipase treatment for 2 h increased the protein content from 62.87 to 94.11%. FPH after lipase treatment showed 1.21 folds increase in angiotensin-converting enzyme-I (ACE-I) inhibitory activity and 1.7 folds increase in standard amino acids composition (32.193 to 61.493 g/100 g). The physicochemi

SUBMITTER: Yathisha UG 

PROVIDER: S-EPMC9813303 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature