Jahanbani, Raheleh and Ghaffari, Mahmood and Vahdati, Kourosh and Salami, Maryam and Khalesi, Mohammadreza and Sheibani, Nader and Moosavi-Movahedi, Ali Akbar

2018

January

Kinetics Study of Protein Hydrolysis and Inhibition of Angiotensin Converting Enzyme by Peptides Hydrolysate Extracted from Walnut

Published

()

24

1

77

85

Bioactive peptides are defined as protein-based components having nutritional value and have proved roles important for the human health. In this study inhibition of angiotensin converting enzyme (ACE) by protein-based hydrolysate extracted from walnut (Juglanse regia. L.) seeds was evaluated. The peptide fraction obtained by enzymatic hydrolysis with trypsin showed higher ACE-inhibitory and lower IC50 value (0.39 ± 0.05 mg/mL) than obtained by hydrolysis with chymotrypsin and proteinase K. The study of kinetics showed that by increasing the concentration of the trypsin hydrolysate from 0.01¿0.5 mg/mL, Km increased, while Vmax decreased. Also the value of Ki was found to be 0.17 ± 0.01 mg/mL, which means that binding affinity for the substrate decreased in the presence of inhibitor. The structural studies of ACE demonstrated that, in comparison with a commercial antihypertension drug (enalapril), the trypsin hydrolysate had no effect on secondary structure and less tertiary structure changes of protein was observed.

10.1007/s10989-017-9594-4