Abstract
Protein modifications occurring during sterilisation of infant formulas can affect protein digestibility and release of bioactive peptides. The effect of glycation and cross-linking on protein breakdown and release of β-casomorphins was evaluated during in vitro gastro-intestinal digestion (GID) of six sterilised model systems of infant formula. Protein degradation during in vitro GID was evaluated by SDS-PAGE and by measuring the nitrogen content of ultrafiltration (3kDa) permeates before and after in vitro GID of model IFs. Glycation strongly hindered protein breakdown, whereas cross-linking resulting from β-elimination reactions had a negligible effect. Only β-casomorphin 7 (β-CM7) was detected (0.187–0.858mgL−1) at the end of the intestinal digestion in all untreated IF model systems. The level of β-CM7 in the sterilised model systems prepared without addition of sugars ranged from 0.256 to 0.655mgL−1. The release of this peptide during GID was hindered by protein glycation.
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