Racemic Resolution of some DL-Amino Acids using Aspergillus fumigatus L-Amino Acid Oxidase

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 enzym...

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Bibliographic Details
Published in:Current microbiology 2011-07, Vol.63 (1), p.94-99
Main Authors: Singh, Susmita, Gogoi, Binod K, Bezbaruah, Rajib L
Format: Article
Language:English
Subjects:
acids
Amino acids
Amino Acids - chemistry
Amino Acids - metabolism
Aspergillus fumigatus
Aspergillus fumigatus - chemistry
Aspergillus fumigatus - enzymology
Aspergillus fumigatus - metabolism
Biotransformation
Enzymes
Fungal Proteins - metabolism
Fungi
L-Amino Acid Oxidase - metabolism
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Summary: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.
ISSN:0343-8651
1432-0991
DOI:10.1007/s00284-011-9955-8