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Updated: May 2, 2026

Sigma's Non-specific Protease Activity Assay - Casein as a Substrate
Published on: September 17, 2008
Antioxidant activity of bovine casein hydrolysates produced by Ficus carica L.-derived proteinase
Giovanna Di Pierro1, Martina B O'Keeffe2, Alexey Poyarkov3
1Department of Life Sciences, University of Limerick, Limerick, Ireland; Department of Agronomy, Food, Natural Resources, Animals and Environment - DAFNAE, Università di Padova, Legnaro, Padova, Italy.
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.
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