Synthesis of theanine from glutamic acid gamma-methyl ester and ethylamine catalyzed by Escherichia coli having gamma-glutamyltranspeptidase activity.
Glutamic acid gamma-methyl ester (GAME) was used as substrate for theanine synthesis catalyzed by Escherichia coli cells possessing gamma-glutamyltranspeptidase activity. The yield was about 1.2-fold higher than with glutamine as substrate. The reaction was optimal at pH 10 and 45 degrees C, and the optimal substrate ratio of GAME to ethylamine was 1:10 (mol/mol). With GAME at 100 mmol, 95 mmol theanine was obtained after 8 h.
Zhang
Fei
F
State Key Laboratory of Pharmaceutical Biotechnology, School of Life Science, Nanjing University, Nanjing 210093, People's Republic of China. zhangfeiluck@126.com
Zheng
Qing-Zhong
QZ
Jiao
Qing-Cai
QC
Liu
Jun-Zhong
JZ
Zhao
Gen-Hai
GH
D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005021:Ethylamines / Q000737:chemistry*; D005971:Glutamates / Q000138:chemical synthesis* / Q000737:chemistry; D018698:Glutamic Acid / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008738:Methyl Ethers / Q000737:chemistry*; D013379:Substrate Specificity; D013696:Temperature; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D005021:Ethylamines; D005971:Glutamates; D008738:Methyl Ethers; D018698:Glutamic Acid; C026166:theanine; D005723:gamma-Glutamyltransferase; C041564:ethylamine