Difference between revisions of "Part:BBa K518004:Experience"
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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].
 
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].
  
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=Reference=
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==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.
 
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.

Revision as of 19:48, 3 October 2011

This experience page is provided so that any user may enter their experience using this part.
Please enter how you used this part and how it worked out.

Applications of BBa_K518004

User Reviews

UNIQec37a1f73c441004-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.


UNIQec37a1f73c441004-partinfo-00000002-QINU