Antioxidant activity of bovine casein hydrolysates produced by Ficus carica L.-derived proteinase

Food Chem. 2014 Aug 1:156:305-11. doi: 10.1016/j.foodchem.2014.01.080. Epub 2014 Feb 5.

Abstract

A Ficus carica L. latex proteinase preparation was investigated for its ability to produce antioxidant hydrolysates/peptides from bovine casein (CN). The Oxygen Radical Absorbance Capacity (ORAC) values for NaCN and β-CN hydrolysates ranged from 0.06 to 0.18, and from 0.51 to 1.19μmol Trolox equivalents/mg freeze-dried sample, respectively. Gel permeation HPLC showed that the β-CN hydrolysate with a degree of hydrolysis of 21% had 65% of peptide material with a molecular mass <500Da. The RP-UPLC profiles also indicated that β-CN was substantially hydrolysed during the early stages of hydrolysis. Analysis of the 4h β-CN hydrolysate by LC-ESI-MS/MS allowed identification of 8 peptide sequences with potential antioxidant properties.

Keywords: Antioxidant activity; Bioactive peptides; Degree of hydrolysis; Ficus carica L.; Mass spectrometry; ORAC(FL) assay; Sodium caseinate; β-Casein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antioxidants / chemistry
  • Caseins / chemistry*
  • Cattle
  • Chromatography, High Pressure Liquid / methods*
  • Chromatography, Liquid / methods*
  • Ficus / chemistry*
  • Oxidation-Reduction
  • Tandem Mass Spectrometry / methods*

Substances

  • Antioxidants
  • Caseins
  • casein hydrolysate