Abstract
The in vitro digestibility of synthetic model tripeptides Ala-Glu-Ala, Ala-D-Glu-Ala, Ala-Asp-Ala, Ala-D-Asp-Ala, Val-Asp-Val, Val-D-Asp-Val, Ala-Phe-Leu and Ala-D-Phe-Leu was examined using intestinal brush border mucosal peptidases. Peptides containing a D-amino acid as the internal residue were not hydrolyzed by intestinal peptidases. As would be expected, 100% hydrolysis was observed with epimeric, L-amino acid- containing peptides. Hence racemization of an amino acid residue would yield an indigestible tripeptide at the very least.
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