Difference between revisions of "Part:BBa K518004:Experience"

Latest revision as of 19:49, 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

UNIQe11ce8f0df8beacf-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.

UNIQe11ce8f0df8beacf-partinfo-00000002-QINU

@@ Line 14: / Line 14: @@
 <I>UT-Tokyo 2011</I>
 |width='60%' valign='top'|
-We have worked hard to demonstrate that this part enables bacteria to produce L-aspartate, but could not. Our sequencing results indicated a general sequence agreement, showing only a few mismatching bases. We have tried to detect the L-Asp by either ninhydrin staining or ultraviolet-visible spectroscopy, only to fail. Ninhydrin reactedwith not only amino acid (Asp) but indeed ammonium ion itself, and U-V spectroscopy detected large fumarate noise. We also tried to directly measure intracellular AspA over-expression, but have little days to this work. |};
+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-
+. 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.
+. 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.
 <!-- Template for a user review