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

  • Raheleh Jahanbani
  • Mahmood Ghaffari
  • Kourosh Vahdati
  • Maryam Salami
  • Mohammadreza Khalesi
  • Nader Sheibani
  • Ali Akbar Moosavi-Movahedi
Article
  • 141 Downloads

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.

Keywords

Walnut Bioactive peptide ACE-inhibitory Kinetics Trypsin 

Abbreviations

ACE

Angiotensin converting enzyme

FAPGG

N-(3-[2-furyl]acryloyl)-l-phenylalanylglycylglycine

Notes

Acknowledgements

The support of University of Tehran, International Scientific Studies & Collaboration (CISSC)-Ministry of Science, Research and Technology in Iran, Center of Excellence in Biothermodynamics (CEBiotherm), Center of Excellence for Walnut Improvement and Technology of Iran, Iran National Science Foundation (INSF) and Iran National Elites Foundation (INEF) and UNESCO Chair on Interdisciplinary Research in Diabetes, Iran Society of Biophysical Chemistry is gratefully acknowledged. The authors also acknowledge the Headquarter of Science and Technology Development in Medicinal Plants of Iran’s Vice-President for Science and Technology Affairs.

Compliance with Ethical Standards

Conflict of interest

All author declares that they have no conflict of interest.

Ethical Approval

This article does not contain any studies with human participants or animals performed by any of the authors.

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Copyright information

© Springer Science+Business Media New York 2017

Authors and Affiliations

  • Raheleh Jahanbani
    • 1
  • Mahmood Ghaffari
    • 1
  • Kourosh Vahdati
    • 2
  • Maryam Salami
    • 3
  • Mohammadreza Khalesi
    • 1
    • 4
  • Nader Sheibani
    • 5
  • Ali Akbar Moosavi-Movahedi
    • 1
    • 6
  1. 1.Institute of Biochemistry and BiophysicsUniversity of TehranTehranIran
  2. 2.Department of Horticulture, College of AburaihanUniversity of TehranPakdashtIran
  3. 3.Department of Food Science and Engineering, College of Agriculture & Natural ResourcesUniversity of TehranKarajIran
  4. 4.Department of Food Science and TechnologyShiraz UniversityShirazIran
  5. 5.Departments of Ophthalmology and Visual Sciences, and Biomedical Engineering, School of Medicine and Public HealthUniversity of WisconsinMadisonUSA
  6. 6.Center of Excellence in BiothermodynamicsUniversity of TehranTehranIran

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