Racemic Resolution of some dl-Amino Acids using Aspergillus fumigatus l-Amino Acid Oxidase
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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.
KeywordsAspergillus Fumigatus Chiral Column Racemic Resolution Direct Enantiomer Separation Hydrophobic Aromatic Amino Acid
The financial and laboratory assistance received from CSIR in the form of Senior Research Fellowship and NEIST, Jorhat for carrying out the work is duly acknowledged. The financial assistance received from CSIR in the form of Senior Research Fellowship is duly acknowledged. The authors thank Dr.P.G.Rao, Director, NEIST for providing the facilities for carrying out the work.
- 10.Koyama H (1983) Further characterization of novel l-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. J Biochem (Tokyo) 93:1313–1319Google Scholar
- 12.Ogawa JM, Shimizu S (1999) Microbial enzymes: new industrial applications from traditional screening methods. TIBTECH 17:13–21Google Scholar