Structure–activity studies of protease activating, lipase inhibiting, bile acid binding and cholesterol-lowering effects of pre-screened cumin seed bioactive peptides
| Autor: | Sy Bing Choi, Chee-Yuen Gan, Hwee-Leng Siow |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
medicine.drug_class medicine.medical_treatment Allosteric regulation Medicine (miscellaneous) Peptide Bile acid Inhibition of cholesterol micellization Bile acid binding 03 medical and health sciences Pepsin medicine TX341-641 Lipase Protease activity chemistry.chemical_classification Cumin seed peptide Nutrition and Dietetics Cholestyramine Protease 030102 biochemistry & molecular biology biology Nutrition. Foods and food supply Lipase inhibition 030104 developmental biology chemistry Biochemistry biology.protein Food Science medicine.drug |
| Zdroj: | Journal of Functional Foods, Vol 27, Iss, Pp 600-611 (2016) |
| ISSN: | 1756-4646 |
| DOI: | 10.1016/j.jff.2016.10.013 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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