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PMID:11782200
| Citation |
Suzuki, H, Kajimoto, Y and Kumagai, H (2002) Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial gamma-glutamyltranspeptidase. J. Agric. Food Chem. 50:313-8 |
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| Abstract |
The tastes of several bitter amino acids and their gamma-glutamyl derivatives were compared. The bitterness of Phe, Val, Leu, and His was reduced, sourness was produced, and preferences were increased by gamma-glutamylization. Because the effect of gamma-glutamylization of bitter amino acids was most obvious for Phe, which is an atypical bitter amino acid, an enzymatic method for the synthesis of gamma-glutamylphenylalanine (gamma-Glu-Phe) involving bacterial gamma-glutamyltranspeptidase was developed. The optimum reaction conditions were 200 mM Gln, 200 mM Phe, and 0.5 unit/mL GGT, pH 10.4. After 1.5-h of incubation at 37 degrees C, 140 mM gamma-Glu-Phe was obtained, the yield being 70%. gamma-Glu-Phe was purified on a Dowex 1x8 column and then identified by NMR. |
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| Keywords |
Amino Acids/analysis; Amino Acids/chemistry; Dipeptides/chemical synthesis; Dipeptides/isolation & purification; Escherichia coli/enzymology; Magnetic Resonance Spectroscopy/methods; Taste; gamma-Glutamyltransferase/metabolism |
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