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Current Microbiology

, 63:94 | Cite as

Racemic Resolution of some dl-Amino Acids using Aspergillus fumigatus l-Amino Acid Oxidase

  • Susmita Singh
  • Binod K. Gogoi
  • Rajib L. Bezbaruah
Article

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.

Keywords

Aspergillus Fumigatus Chiral Column Racemic Resolution Direct Enantiomer Separation Hydrophobic Aromatic Amino Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

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.

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Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Susmita Singh
    • 1
  • Binod K. Gogoi
    • 1
  • Rajib L. Bezbaruah
    • 1
  1. 1.Biotechnology Division, North East Institute of Science and TechnologyCouncil of Scientific and Industrial ResearchJorhatIndia

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