Part:BBa_K518004:Experience

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UNIQ105121cc3b82d150-partinfo-00000000-QINU

UT-Tokyo 2011

We worked to show that this part enables bacteria to produce L-aspartate, but failed to do that. In the studies aiming at L-Asp over-production, the amount of L-Asp was determined by HPLC (1,2). We, however, were unable to use this method, so we tried to detect it in alternative ways, including ninhydrin reaction and ultraviolet-visible spectroscopy. For experimental details, see [http://2011.igem.org/Team:UT-Tokyo our result page]. -Reference- 1. Chao, Y. P., Lai, Z. J., Chen, P., & Chern, J. T. (1999). Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12. Biotechnol Prog, 15(3), 453-458. 2. Chao, Y., Lo, T., & Luo, N. (2000). Selective production of L-aspartic acid and L-phenylalanine by coupling reactions of aspartase and aminotransferase in Escherichia coli. Enzyme Microb Technol, 27(1-2), 19-25. UNIQ105121cc3b82d150-partinfo-00000002-QINU