Enzymatic production of D-glu from L-glu by Lactobacillus brevis ATCC 8287

Enzymatic production of D-Glu was investigated by the succesive reactions of a glutamate racemase (EC 5.1.1.3) and a glutamate decarboxylase (EC 4.1.1.15) on L-Glu.Lactobacillus brevis ATCC8287 was chosen as a source of glutamate racemase. This strain produced a glutamate decarboxylase simultaneousl...

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Bibliographic Details
Published inBioscience, biotechnology, and biochemistry Vol. 57; no. 9; pp. 1499 - 1502
Main Authors Yagasaki, Makoto, Ozaki, Akio, Hashimoto, Yukio
Format Journal Article
LanguageEnglish
Published Tokyo Taylor & Francis 1993
Japan Society for Bioscience Biotechnology and Agrochemistry
Oxford University Press
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Summary:Enzymatic production of D-Glu was investigated by the succesive reactions of a glutamate racemase (EC 5.1.1.3) and a glutamate decarboxylase (EC 4.1.1.15) on L-Glu.Lactobacillus brevis ATCC8287 was chosen as a source of glutamate racemase. This strain produced a glutamate decarboxylase simultaneously. The glutamate racemase activity in the cell free extracts was 0.035 units/mg protein. The enzyme kept its activity even at 500 Mm of L-Glu (74g/liter). The optimum pHs of the racemase and the decarboxylase were at around 8.5 and below 4.0, respectively. Both enzymes had no activity at the optimum pH for the other enzyme. L-Glu was racemized first by the glutamate racemase at pH 8.5, then the pH was shifted to 4.0 at which L-Glu was decarboxylated by the glutamate decarboxylase. Starting from 100 g/liter of L-Glu, 50 g/liter of D-Glu was produced and no L-Glu remained in the reaction mixture.
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ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.57.1499