Angiotensin Converting Enzyme (ACE)-peptide interactions: inhibition kinetics, in silico molecular docking and stability study of three novel peptides generated from palm kernel cake proteins. Biomolecules, 9 (569). pp. 1-12. ISSN 2218-273X (2019)
Abstract
Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and GVQEGAGHYALL (increased ACE-inhibitory activity).
| Item Type: | Article |
|---|---|
| Keywords: | Peptide, Kinetics, Molecular docking, Angiotensin converting enzyme inhibitory activity |
| Taxonomy: | By Niche > Food Technology > Food Industry and Trade > Nutrition By Niche > Food Technology > Food Industry and Trade > Research By Niche > Food Technology > Food Industry and Trade > Technological Innovations |
| Local Content Hub: | Niche > Food Technology |
| Depositing User: | Mohd Hafiz Kasirun |
| Date Deposited: | 07 Dec 2023 09:31 |
| Last Modified: | 07 Dec 2023 09:31 |
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