Biotechnology Division, North East Institute of Science and Technology, Council of Scientific and Industrial Research, Jorhat, 785006, Assam, India.
Curr Microbiol. 2011 Jul;63(1):94-9. doi: 10.1007/s00284-011-9955-8. Epub 2011 May 18.
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.
我们研究了烟曲霉 L-氨基酸氧化酶（L-aao）将 DL-氨基酸外消旋混合物拆分的能力，使用的底物是 DL-丙氨酸、DL-苯丙氨酸、DL-酪氨酸和 DL-天冬氨酸。我们采用 Crownpak CR+手性柱对氨基酸进行分析。实验结果表明，该酶能够拆分三种 DL-氨基酸，分别得到光学纯的 D-丙氨酸（100%拆分度）、D-苯丙氨酸（80.2%）和 D-酪氨酸（84.1%）。光学纯的 D-氨基酸有很多用途，因此可以进行工业化生产。这是首次报道烟曲霉 L-氨基酸氧化酶用于拆分 DL-氨基酸的外消旋混合物。
