Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial gamma-glutamyltranspeptidase

J Agric Food Chem. 2002 Jan 16;50(2):313-8. doi: 10.1021/jf010726u.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Amino Acids / chemistry*
  • Dipeptides / chemical synthesis
  • Dipeptides / isolation & purification
  • Escherichia coli / enzymology
  • Magnetic Resonance Spectroscopy / methods
  • Taste*
  • gamma-Glutamyltransferase / metabolism*

Substances

  • Amino Acids
  • Dipeptides
  • gamma-glutamylphenylalanine
  • gamma-Glutamyltransferase