Abstract
The optimal reaction conditions for the synthesis of γ-glutamylglutamine using γ-glutamyltranspeptidase from Escherichia coli were determined. The maximum yield of γ-glutamylglutamine (110 mM) was obtained using 250 mM l-glutamine and 1.1 U γ-glutamyltranspeptidase/ml at pH 10.5 and at 37°C for 7 h; the conversion of glutamine to γ-glutamylglutamine was 88%.
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Acknowledgements
We would like to thank Dr. Bunnta Watanabe and Prof. Jun Hiratake, Institute for Chemical Research, Kyoto University, for the NMR and MS analyses and for their productive discussion. This work was supported by a Grant-in-Aid for Scientific Research (no. 21380059) to HS from the Ministry of Education, Culture, Sports, Science and Technology of Japan. CY was supported by the 21st Century COE Program of the Ministry of Education, Culture, Sports, Science and Technology of Japan.
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All amino acids and peptides were used in this study were l-isomers.
Purpose of work: Glutamine has favorable effects on humans but is unstable in aqueous solution and easily forms pyroglutamic acid. γ-Glutamylglutamine is more stable than glutamine and is almost as stable as alanylglutamine. Moreover, the taste of γ-glutamylglutamine is preferable to that of alanylglutamine. Therefore, γ-glutamylglutamine is a promising candidate for use as a glutamine precursor in food additives.
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Sayed, A.S.A.F.E., Fujimoto, S., Yamada, C. et al. Enzymatic synthesis of γ-glutamylglutamine, a stable glutamine analogue, by γ-glutamyltranspeptidase from Escherichia coli K-12. Biotechnol Lett 32, 1877–1881 (2010). https://doi.org/10.1007/s10529-010-0364-z
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DOI: https://doi.org/10.1007/s10529-010-0364-z