Three novel peptide sequences identified from palm kernel cake (PKC) generated protein\nhydrolysate including YLLLK,WAFS and GVQEGAGHYALL were used for stability study against\nangiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies.\nResults showed that the peptides were degraded at different cleavage degrees of 94%, 67% and\n97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE.\nYLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and\nGVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest Ki (1.51 mM) in\ninhibition kinetics study when compared to WAFS and GVQEGAGHYALL with Ki of 2 mM and\n3.18 mM, respectively. In addition, ACE revealed the lowest Kapp\nm and Vapp\nmax and higher catalytic\nefficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme\ncatalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK showed the lowest\ndocking score of -8.224 and seven interactions with tACE, while peptide GVQEGAGHYALL showed\nthe higher docking score of -7.006 and five interactions with tACE.
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