title: Racemic resolution of some DL-amino acids using Aspergillus fumigatus L-amino acid oxidase.
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.
authors: Biotechnology Division, North East Institute of Science and Technology, Council of Scientific and Industrial Research, Jorhat, 785006, Assam, India. susmitasingh123@gmail.com
authors: Susmita
authors: S
authors: Singh
authors: Binod K
authors: BK
authors: Gogoi
authors: Rajib L
authors: RL
authors: Bezbaruah
references: Biotechnol Bioeng. 1994 Dec;44(11):1288-94
references: 18618640
references: Biochem J. 1989 Jul 1;261(1):285-7
references: 2570568
references: Can J Microbiol. 2009 Sep;55(9):1096-102
references: 19898552
references: Trends Biotechnol. 1999 Jan;17(1):13-21
references: 10098273
references: Ann N Y Acad Sci. 1995 Mar 31;750:1-9
references: 7785836
references: Angew Chem Int Ed Engl. 2004 Feb 6;43(7):788-824
references: 14767950
references: J Mol Biol. 2007 Mar 16;367(1):234-48
references: 17234209
references: Biomed Chromatogr. 1996 Nov-Dec;10(6):303-12
references: 8949912
references: J Biochem. 1983 May;93(5):1313-9
references: 6885723