Kinetics Study of Protein Hydrolysis and Inhibition of Angiotensin Converting Enzyme by Peptides Hydrolysate Extracted from Walnut |
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| Authors: | Raheleh Jahanbani Mahmood Ghaffari Kourosh Vahdati Maryam Salami Mohammadreza Khalesi Nader Sheibani Ali Akbar Moosavi-Movahedi |
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| Affiliation: | 1.Institute of Biochemistry and Biophysics,University of Tehran,Tehran,Iran;2.Department of Horticulture, College of Aburaihan,University of Tehran,Pakdasht,Iran;3.Department of Food Science and Engineering, College of Agriculture & Natural Resources,University of Tehran,Karaj,Iran;4.Department of Food Science and Technology,Shiraz University,Shiraz,Iran;5.Departments of Ophthalmology and Visual Sciences, and Biomedical Engineering, School of Medicine and Public Health,University of Wisconsin,Madison,USA;6.Center of Excellence in Biothermodynamics,University of Tehran,Tehran,Iran |
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| 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 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. |
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