Industrial biotransformations for the production of d-amino acids
Optically pure d-amino acids are industrially manufactured by biotransformations of cheap starting materials produced by chemical synthesis or fermentation in combination with the development of enzyme catalysts suitable for the starting materials. dl-Alaninamide, an intermediate of the chemical syn...
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Veröffentlicht in: | Journal of Molecular Catalysis. B, Enzymatic Enzymatic, 1998-01, Vol.4 (1), p.1-11 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Optically pure
d-amino acids are industrially manufactured by biotransformations of cheap starting materials produced by chemical synthesis or fermentation in combination with the development of enzyme catalysts suitable for the starting materials.
dl-Alaninamide, an intermediate of the chemical synthesis of
dl-alanine, was efficiently converted to
d-alanine by stereoselective hydrolysis with a
d-isomer specific amidohydrolase produced by
Arthrobacter sp. NJ-26. The total utilization system of
dl-alaninamide for the production of optically pure
d- and
l-alanine was constructed by stereospecific amidohydrolases. On the other hand,
d-amino acids were also produced from corresponding
l-isomers, which are efficiently manufactured by fermentation.
d-Glutamic acid was produced from
l-glutamic acid.
l-Glutamate was converted to the
dl-form by the recombinant glutamate racemase of
Lactobacillus brevis ATCC8287. Then
l-glutamate in a racemic mixture was selectively decarboxylated to γ-aminobutyrate by the
l-glutamate decarboxylase of
E. coli ATCC11246. As a result of successive enzymatic reactions,
d-glutamate was efficiently produced from
l-glutamate by a one-pot reaction.
d-Proline was produced by the same strategy from
l-proline using the recombinant proline racemase of
Clostridium sticklandii ATCC12262. In this case,
l-proline was degraded by
Candida sp. PRD-234. The strategy from
l-amino acids to
d-amino acids could be applicable to the manufacture of many
d-amino acids. |
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ISSN: | 1381-1177 1873-3158 |
DOI: | 10.1016/S1381-1177(97)00011-8 |