[Absorption of enzymatic protein hydrolysates and equimolar amino acid mixtures in the perfused small intestine of the rat].

Casein, wheat gluten or field-bean protein isolate (vicia faba) was hydrolyzed enzymatically by trypsin or thermitase (proteinase from Thermoactinomyces vulgaris). The degree of splitting of the protein peptide bounds was, resp., 18% or 30% for casein, 8% or 30% for wheat gluten and 16% or 29% for the field-bean protein isolate. The peptide pattern of the protein hydrolysates was measured by gel chromatography. The absorption of the enzymatic protein hydrolysates was compared with the absorption of the equimolar mixtures of free amino acids by perfusion of the distal or proximal part of the small intestine of nonanaesthesized rats. The absorption was measured on the basis of the amino acid disappearance from the perfused part of the small intestine and expressed as absorption of the total amino acids, of each single amino acid and as coefficient of variation of amino acid absorption. There are no differences in the total amino acid absorption of the tryptic casein hydrolysate and the three thermitatic protein hydrolysates compared with their corresponding mixtures of free amino acids. The absorption is decreased in case of larger oligopeptides. Their preceding mucosal hydrolysis is slower than the absorption of the splitting products. This is true for tryptic hydrolysates of wheat gluten and field-bean protein. The absorption patterns of the single amino acids are different for protein hydrolysates compared with their equimolar mixtures of amino acids in case of a same total absorption, too. The coefficient of variation is low (more equal amino acid absorption) in hydrolysates consisting of a homogeneous mixture of low molecular weight peptides. It is more increased in mixtures of free amino acids or in hydrolysates containing longer-chain peptides.