Impact of holder, high temperature short time and high hydrostatic pressure pasteurization methods on protein structure and aggregation in a human milk protein concentrate

Food Chem. 2022 Apr 16:374:131808. doi: 10.1016/j.foodchem.2021.131808. Epub 2021 Dec 8.


This work evaluated the impact of high temperature short time (HTST, 72 °C, 15 s), high hydrostatic pressure (HHP, 400-600 MPa at 5 and 10 min) and Holder pasteurization (HoP, 62.5 °C, 30 min) on protein profile and aggregation in a human milk protein concentrate (HMPC). The structural changes induced in milk proteins were investigated in HMPC as well as in sedimentable and non-sedimentable fractions recovered after ultracentrifugation. The results showed that heat treatments induced more protein denaturation and aggregation than did HHP treatments. Indeed, heat-induced protein aggregates observed in HMPC and the sedimentable fraction were mainly composed of lactoferrin and α-lactalbumin. More specifically, the concentration of lactoferrin in HMPC decreased by 86% after HTST and HoP whereas no effect was observed after HHP treatment. These results show the potential of HHP processing as a pasteurization method for HMPC since it minimizes the impact on protein structure, which generally correlates to protein quality and bioactivity.

Keywords: Human milk protein concentrate; Lactoferrin; Protein denaturation and aggregation; Protein interaction; Thermal and high hydrostatic pressure treatments; α-Lactalbumin.

MeSH terms

  • Hot Temperature
  • Humans
  • Hydrostatic Pressure
  • Milk Proteins* / analysis
  • Milk, Human / chemistry
  • Pasteurization*
  • Temperature


  • Milk Proteins