Effective formation of di- and tri-gamma-glutamates by gamma-glutamyltranspeptidase.
Using gamma-glutamyltranspeptidase, conditions for di- and tri-gamma-glutamates synthesis were studied with glutamine and glutamic acid esters as substrates. The reactivity of amino acid esters was higher than for free ones. The efficient conditions were the combination of glutamine ethyl and glutamate diethyl esters with a molar ratio of 1/10 at pH 7-8.
Watanabe
T
T
School of Food and Nutritional Sciences, University of Shizuoka, Japan.
Kohashi
M
M
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004952:Esters; D018698:Glutamic Acid / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D004952:Esters; D005973:Glutamine; D018698:Glutamic Acid; D005723:gamma-Glutamyltransferase