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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, gamma-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, "N epsilon-(gamma-glutamyl)lysine hydrolase" was found in the isolated microorganisms which can use the synthesized N epsilon-(gamma-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.
K Yasumoto, and
F Suzuki
December 1994,
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K Yasumoto, and
F Suzuki
August 1976,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
K Yasumoto, and
F Suzuki
November 1976,
Journal of the science of food and agriculture,
K Yasumoto, and
F Suzuki
January 1988,
Advances in experimental medicine and biology,
K Yasumoto, and
F Suzuki
June 2022,
ACS omega,
K Yasumoto, and
F Suzuki
January 1997,
Biochemistry and cell biology = Biochimie et biologie cellulaire,
K Yasumoto, and
F Suzuki
January 1996,
The Journal of organic chemistry,
K Yasumoto, and
F Suzuki
October 1992,
Biochemical and biophysical research communications,
K Yasumoto, and
F Suzuki
November 1994,
Mutation research,
