Current Microbiology 2011-07-01

Racemic resolution of some DL-amino acids using Aspergillus fumigatus L-amino acid oxidase.

Susmita Singh, Binod K Gogoi, Rajib L Bezbaruah

Index: Curr. Microbiol. 63 , 94-99, (2011)

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Abstract

The ability of Aspergillus fumigatus L-amino acid oxidase (L-aao) to cause the resolution of racemic mixtures of DL-amino acids was investigated with DL-alanine, DL-phenylalanine, DL-tyrosine, and DL-aspartic acid. A chiral column, Crownpak CR+ was used for the analysis of the amino acids. The enzyme was able to cause the resolution of the three DL-amino acids resulting in the production of optically pure D-alanine (100% resolution), D-phenylalanine (80.2%), and D-tyrosine (84.1%), respectively. The optically pure D-amino acids have many uses and thus can be exploited industrially. This is the first report of the use of A. fumigatus L: -amino acid oxidase for racemic resolution of DL-amino acids.