Abstract
Transglutaminase-catalyzed incorporation of L-lysine into wheat gliadin rendered the lysine-fortified protein poorly digestible in the in vitro tests. In rat feeding tests, however, the luminal leavings and excreta collected after administration of the [14C]lysine-fortified gliadin contained less than one-tenth of the radioactivity originally administered to rats. The enzymes, γ-glutamylamine cyclotransferase and 5-oxoprolinase, known to occur in animal kidney are at least in part responsible for the observed high availability of isopeptide bound lysine. A novel enzyme which is capable of directly hydrolyzing the cross-linked isopeptide into component amino acids and peptides, “Nε-(γ-glutamyl)lysine hydrolase” was found in the isolated microorganisms which can use the synthesized Nε-(γ-glutamyl)lysine as their only source of carbon and nitrogen. The enzyme(s) appear to be effectively used for improving digestibility and availability of protein matrixes formed in normal metabolism and by heat and/or shear treatment commonly used in food processing.
