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Team:TU Darmstadt/Results
From 2012.igem.org
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* successful overexpression of all proteins of our metabolic pathway | * successful overexpression of all proteins of our metabolic pathway | ||
* confirming the suggested oligomerization of the homodimer of TphB | * confirming the suggested oligomerization of the homodimer of TphB | ||
| + | * confirming the suggested oligomerization of the homotrimer of TphA3 | ||
* confirming the suggested oligomerization of the homopentamer of AroY | * confirming the suggested oligomerization of the homopentamer of AroY | ||
* improved characterization of the BioBrick XylE from the parts registry | * improved characterization of the BioBrick XylE from the parts registry | ||
** e.g. discovering protocatechuic acid to be an alternative substrate for XylE or including a striking difference in its kinetics | ** e.g. discovering protocatechuic acid to be an alternative substrate for XylE or including a striking difference in its kinetics | ||
* using XylE to prove AroY's activity in catalyzing our final step from protocatechuate to catechol. | * using XylE to prove AroY's activity in catalyzing our final step from protocatechuate to catechol. | ||
Latest revision as of 03:36, 27 September 2012
Results
The following page features links and details on all information on the TU Darmstadt iGEM 2012 teams results. Although we didn't manage to complete PET.er we went far. Far beyond the point of what many people thought we could achieve.
At this point we want to thank everyone that knowing and unknowingly supported us. Participating at iGEM was a great adventure and certainly the right thing to do.
What we managed:
- controling and reproducing the expression of our chimeric protein on the bacterial surface in three different E.coli strains, including the ethylene glycol metabolizing strain Mg1655
- quantifying the enzmyatic activity of our membrane bound fusion protein in vivo
- quantifying the enzmyatic activity of our two PET-cleaving enzymes FsC/pNB-Est13 on selected substrates
- characterization of the AraC-Pbad regulation unit
- designing two putative terephtalate uptake operons under the control of a Arabinose inducible promotor(AraC-Pbad)
- developing a new method (ATS-method) to detect TPA with GC-MS
- successful overexpression of all proteins of our metabolic pathway
- confirming the suggested oligomerization of the homodimer of TphB
- confirming the suggested oligomerization of the homotrimer of TphA3
- confirming the suggested oligomerization of the homopentamer of AroY
- improved characterization of the BioBrick XylE from the parts registry
- e.g. discovering protocatechuic acid to be an alternative substrate for XylE or including a striking difference in its kinetics
- using XylE to prove AroY's activity in catalyzing our final step from protocatechuate to catechol.
