Team:TU Delft/Project/alkane-degradation/results

From 2010.igem.org

Revision as of 19:08, 27 October 2010 by Hugo 87 (Talk | contribs)

CharacterizationResultsParts

Alkane Degradation Results & Conclusions

Figure 1 – Schematic description of the alkane degradation pathway with the corresponding genes.

Characterization of the alkane hydroxylase system

The following table contains the average ratio of the hexadecane/undecane surface areas. Strains numbers 1 and 2 are two positive colonies taken from the same plate.

Strain Ratio octane/undecane Standard deviation [%] Octane converted [umol] Protein [mg] Enzymatic activity [U/mg protein]
Blank 0.832 6.16 0.00 0.00 0.00
E.coli K12 negative control 0.821 13.3 1.34 1.51 1.23E-3
E.coli K12 strain #1 (AH-system) 0.652 14.4 21.6 1.70 1.77E-2
E.coli K12 strain #2 (AH-system) 0.439 3.96 47.0 1.46 4.49E-2

From the ratios we may conclude that the samples obtained from the E.coli strain, carrying the AH system, contain relatively less octane than the control strain. By comparing peak ratios we were able to estimate the specific enzymatic activity of the system, which was found to be 0.045 U/mg. For more information about our findings CLICK HERE.

Characterization of the long-chain alkane monooxygenase; LadA

Characterization of the Alcohol DeHydrogenase (ADH) system

Characterization of the ALdehyde DeHydrogenase system

USEFUL LITERATURE AND REFERENCES

  1. Kato T. et al. "Gene cloning and characterization of an aldehyde dehydrogenase from long-chain alkane-degrading Geobacillus thermoleovorans B23" Extremophiles (2010) 14:33-39.
  2. http://mbel.kaist.ac.kr/lab/research/protein_en1.html
  3. Hoffmann F. and Rinas U. "Stress Induced by Recombinant Protein Production in Escherichia coli" Advances in Biochemical Engineering/Biotechnology, 2004, Vol. 89/2004, pp. 73-92.

CharacterizationResultsParts

Retrieved from "http://2010.igem.org/Team:TU_Delft/Project/alkane-degradation/results"