Structure–activity studies of protease activating, lipase inhibiting, bile acid binding and cholesterol-lowering effects of pre-screened cumin seed bioactive peptides

• Main Authors: Hwee-Leng Siow, Sy-Bing Choi, Chee-Yuen Gan
• Format: Article
• Language: English
• Published: Elsevier 2016-12-01
• Series: Journal of Functional Foods
• Subjects: Cumin seed peptide; Bile acid; Lipase inhibition; Inhibition of cholesterol micellization; Protease activity
• Online Access: http://www.sciencedirect.com/science/article/pii/S1756464616303267

The objective of this study was to evaluate the in vitro physiological properties of pre-screened cumin seed peptides (CSPs) based on in vitro and in silico studies. Results showed that CSPs were capable of increasing the protein digestibility up to 400%. Apart from that, CSP1 and CSP2 showed >50% inhibition of pancreatic lipase activity. These peptides also exerted a similar or greater affinity to bind bile acid than cholestyramine, in addition to giving inhibitory effect (up to 80%) in the formation of cholesterol micelle. Based on the structure–activity relationship studies, the results have postulated that the interaction of peptides at non-catalytic region induced allosteric effects to enhance the pepsin proteolytic activity; the direct contact of the peptide with lipase active sites rendered inhibitory action; and the binding between peptide and bile acids was relied on the hydrophilic and hydrophobic interactions.