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

 
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
−
 
 
__NOTOC__
 
__NOTOC__
 
This experience page is provided so that any user may enter their experience using this part.<BR>Please enter
 
This experience page is provided so that any user may enter their experience using this part.<BR>Please enter
Line 8: Line 7:
 
===User Reviews===
 
===User Reviews===
 
<!-- DON'T DELETE --><partinfo>BBa_K518004 StartReviews</partinfo>
 
<!-- DON'T DELETE --><partinfo>BBa_K518004 StartReviews</partinfo>
 +
 +
{|width='80%' style='border:1px solid gray'
 +
|-
 +
|width='10%'|
 +
<partinfo>BBa_K518004 AddReview 0</partinfo>
 +
<I>UT-Tokyo 2011</I>
 +
|width='60%' valign='top'|
 +
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.
 +
 +
 +
 
<!-- Template for a user review
 
<!-- Template for a user review
 
{|width='80%' style='border:1px solid gray'
 
{|width='80%' style='border:1px solid gray'

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

UNIQ18effb0e8c03e0d2-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.


UNIQ18effb0e8c03e0d2-partinfo-00000002-QINU