The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids

Food Chem. 2013 Feb 15;136(3-4):1203-12. doi: 10.1016/j.foodchem.2012.09.022. Epub 2012 Sep 16.

Abstract

This study aimed to determine the kinetics of milk protein digestion and amino acid absorption after ingestion of four dairy matrices by six minipigs: unheated or heated skim milk and corresponding rennet gels. Digestive contents and plasma samples were collected over a 7 h-period after meal ingestion. Gelation of milk slowed down the outflow of the meal from the stomach and the subsequent absorption of amino acids, and decreased their bioavailability in peripheral blood. The gelled rennet matrices also led to low levels of milk proteins at the duodenum. Caseins and β-lactoglobulin, respectively, were sensitive and resistant to hydrolysis in the stomach with the unheated matrices, but showed similar digestion with the heated matrices, with a heat-induced susceptibility to hydrolysis for β-lactoglobulin. These results suggest a significant influence of the meal microstructure (resulting from heat treatment) and macrostructure (resulting from gelation process) on the different steps of milk proteins digestion.

MeSH terms

  • Amino Acids / analysis
  • Amino Acids / pharmacokinetics*
  • Animals
  • Digestion
  • Hot Temperature
  • Kinetics
  • Milk Proteins / chemistry*
  • Swine
  • Swine, Miniature

Substances

  • Amino Acids
  • Milk Proteins