Development of a human milk protein concentrate from donor milk: Impact of the pasteurization method on static in vitro digestion in a preterm newborn model.

The impact of high temperature short time (HTST, 72 °C, 15 s), Holder pasteurization- (63 °C, 30 min) and high hydrostatic pressure (HHP, 600 MPa-10 min) was evaluated on the digestibility of human milk protein concentrate (HMPC) by using a static in vitro gastrointestinal digestion system. The results showed that the processing steps used to produce the HMPC induced a decrease in readily available nitrogen (non-protein nitrogen and peptides). Overall, digestibility was similar between pasteurized and raw HMPC (degree of hydrolysis ranged from 26 to 34 %). Lactoferrin was more susceptible to gastric and intestinal digestion after thermal pasteurization. Additionally, the resistance of β-casein to digestion increased after HHP and Holder pasteurization due to aggregation and changes in protein structure. During intestinal digestion, Holder pasteurization induced a higher release of arginine, phenylalanine and tyrosine from HMPC compared to raw and HHP-treated HMPC. Overall, protein structural changes induced by human milk (HM) processing (freeze-thawing and filtration) and pasteurization treatments affected HMPC proteolysis during in vitro digestion. However, protein digestion behaviors were quite similar for raw and HHP-treated HMPC compared to the thermal-treated HMPC, with no effect on lactoferrin digestion. Consequently, pasteurization of HMPC by HHP represents an interesting non-thermal process that preserves the HM bioactive proteins during digestion.