Antioxidant Properties of Casein Phosphopeptides (CPP) and Maillard-Type Conjugated Products

A casein phosphopeptide (CPP) fraction derived from tryptic hydrolysis of bovine casein was evaluated for antioxidant activity. Conjugations or mixtures of CPP with polysaccharide, galactomannan (Gal), or xyloglucan (Xyl) were prepared to evaluate potential enhancement of CPP antioxidant activity. The effect of calcium was also investigated. The CPP preparation alone was effective at scavenging hydroxyl radicals and sequestering Fe to protect against Fenton reaction-induced deoxyribose oxidation in non-site-specific (up 63.3% inhibition) and site-specific (up 32.1% inhibition) binding assays, respectively. CPP also effectively quenched 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonic acid radicals (ABTS) to an extent of 67.6% scavenging in an aqueous system. In a soybean lecithin liposome system, CPP exhibited effective protection against peroxyl radical-induced liposomal peroxidation (38.3% of control in terms of rate of propagation). Conjugating CPP with Gal or Xyl polysaccharides using Maillard reaction conditions significantly reduced activity in the Fenton reaction-deoxyribose assays, while exhibiting no effect on the antioxidant activity of native CPP in both the ABTS and liposome assays, respectively. These results represent comparative antioxidant capacity of the native CPP and associated conjugates in phases that varied in relative hydrophilic and hydrophobic character. We conclude that CPP has the potential to act as both a primary and secondary antioxidant by displaying transition metal ion sequestering activity and free radical quenching activity. Improvements in antioxidant activity of CPP by Maillard-type conjugation with Xyl or Gal were relatively small and model-specific.