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

July 28, 2017

Title

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

Author

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

Year

2017

Journal

International Journal of Peptide Research and Therapeutics

Abstract

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 Vmaxdecreased. 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.

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Chemical stability, Biochemistry