Angiotensin-converting enzyme inhibitory and antioxidative activities and functional characterization of protein hydrolysates of hard-to-cook chickpeas

Sergio Medina-Godoy, Dulce L. Ambriz-Pérez, Cindy I. Fuentes-Gutiérrez, Lourdes J. Germán-Báez, Roberto Gutiérrez-Dorado, Cuauhtémoc Reyes-Moreno, Angel Valdez-Ortiz

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Background: The potential use of hard-to-cook (hardened) chickpeas to obtain value-added functional food ingredients was evaluated. For that purpose, some nutraceutical and functional attributes of several chickpea protein hydrolysates (CPHs) prepared from both fresh and hard-to-cook grains were evaluated. Results: All the CPHs prepared from both fresh and hard-to-cook grains, with the enzymes alcalase, pancreatin and papain, showed high angiotensin converting enzyme inhibitory (ACE-I) activity with IC 50 values ranging from 0.101 to 37.33 μg mL -1; similarly, high levels of antioxidant activity (around 18.17-95.61 μmol Trolox equivalent antioxidant capacity μg -1 CPH) were obtained through both the 2,2-diphenyl-1-picrylhydrazyl and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) methods. Regarding functional characterization of the CPHs, oil absorption values ranged from 1.91 to 2.20 mL oil g -1 CPH, with water solubility almost 100% from pH 7 to 10. Conclusion: The high antioxidant and ACE-I activities as well as the good functional properties of the CPH prepared from both fresh and hard-to-cook grains, suggest its use in food formulations with value added in human health.

Original languageEnglish
Pages (from-to)1974-1981
Number of pages8
JournalJournal of the Science of Food and Agriculture
Volume92
Issue number9
DOIs
StatePublished - Jul 2012
Externally publishedYes

Keywords

  • ACE-I activity
  • Antioxidant activity
  • Bioactive peptides
  • Chickpea protein hydrolysates
  • Functional properties
  • Value added

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