Identification of Casein Phosphopeptides Released after Simulated Digestion of Milk-Based Infant Formulas

Abstract

Adapted, follow-up, probiotic follow-up, toddler, and probiotic toddler infant formulas were subjected to an in vitro enzymatic procedure simulating physiological digestion. The formation and identification of casein phosphopeptides (CPPs) in the milk-based infant formulas were studied using reversed phase high-performance liquid chromatography coupled on line to an ion trap mass spectrometer. Most CPPs formed contained the cluster sequence SpSpSpEE, a mineral binding site. Phosphopeptide alpha(s2)-CN(1-19)4P was present in all formulas analyzed. Probiotic formulas released CPPs not detected in nonprobiotic formulas and probably formed by bifidobacteria action. These observations suggest that physiological digestion of these products promotes the formation of bioactive peptides with mineral carrier properties in the gastrointestinal tract, which resist further proteolysis.

Health-promoting properties of bioactive peptides derived from milk proteins in infant food: a review

“…According to the authors, calcium could be bound preferentially to CPPs with the cluster sequence SpSpSpEE and iron and zinc to CPPs with the phosphorylated cluster and phosphoserine residues. The release of CPPs with metal-chelating properties following SGID of infant formulas was also reported in previous studies (Miquel et al 2005). Many of these CPPs were only detected in probiotic formulas indicating that they are formed by the action of bifidobacteria.…”

Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications

“…This is also consistent with the literature results [53] showing that multi-phosphorylated ␣ s1 -and ␣ s2 -CN peptides were hydrolysislabile in contrast to the significantly resistant ␤-CN f1-25 3/4P and f33-52 1P, even dephosphorylated. On the other hand, using a different procedure for in vitro digestion, the cluster regions of ␣ s1 -and ␣ s2 -CN were found to survive proteolysis of milk-based infant formulas [54]. It is noteworthy that peptides from the N-terminal region of ␤-CN accumulate during cheese ripening, resisting to the proteolytic system of acid lactic bacteria [44].…”

Bioactive milk proteins, peptides and lipids and other functional components derived from milk and bovine colostrum

“…Calcium-binding casein phosphopeptides (CPPs) have been identifi ed in casein hydrolysates, milk-based infant formulae, and fermented dairy products, such as cheese and yoghurt (Gagnaire et al , 2001;Kawahara et al , 2005;Miquel et al , 2005;Dupas et al , 2009). CPPs may also arise from α s 1 -, α s 2 -, and β -casein digestion in the gut (FitzGerald, 1998).…”