Difference between revisions of "Part:BBa K5443013:Experience"
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We showed that the ECH-Ppu enzyme from <i>Pseudomonas putida</i> was functional in <i>E. coli</i> as part of a vanillin biosynthetic pathway. This was evidenced by detectable production of vanillin (0.2 ppm), determined by LC-MS analysis of our tested clone pMQ3C-11 (Fig. 1).
 
We showed that the ECH-Ppu enzyme from <i>Pseudomonas putida</i> was functional in <i>E. coli</i> as part of a vanillin biosynthetic pathway. This was evidenced by detectable production of vanillin (0.2 ppm), determined by LC-MS analysis of our tested clone pMQ3C-11 (Fig. 1).
  
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As functional Ech-Ppu is essential for vanillin production in this pathway, detectable presence of vanillin shows at least partial success of our construct pMQ3C-11.
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As functional ECH-Ppu is essential for vanillin production in this pathway, detectable presence of vanillin shows at least partial success of our construct pMQ3C-11.
  
  

Latest revision as of 13:08, 2 October 2024

Applications of BBa_K5443013

We showed that the ECH-Ppu enzyme from Pseudomonas putida was functional in E. coli as part of a vanillin biosynthetic pathway. This was evidenced by detectable production of vanillin (0.2 ppm), determined by LC-MS analysis of our tested clone pMQ3C-11 (Fig. 1).

As functional ECH-Ppu is essential for vanillin production in this pathway, detectable presence of vanillin shows at least partial success of our construct pMQ3C-11.


Figure 1. LCMS analysis of compounds produced using pMQ3C-11.
The graph shows the detected presence of all 6 tested compounds, validating successful expression of all parts within pMQ3C-11, including ECH-Ppu.