Team:TU Delft/Project/alkane-degradation/results
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+ | <html><center><img src="https://static.igem.org/mediawiki/2010/0/00/TU_Delft_project_navigation.jpg" usemap="#projectnavigation" border="0" /></center><map id="projectnavigation" name="projectnavigation"><area shape="rect" alt="Characterization" title="" coords="309,3,591,45" href="https://2010.igem.org/Team:TU_Delft#page=Project/alkane-degradation/characterization" target="" /><area shape="rect" alt="Results" title="" coords="609,3,891,44" href="https://2010.igem.org/Team:TU_Delft#page=Project/alkane-degradation/results" target="" /><area shape="rect" alt="Parts" title="" coords="9,3,290,44" href="https://2010.igem.org/Team:TU_Delft#page=Project/alkane-degradation/parts" target="" /></map></html> | ||
==Alkane Degradation Results & Conclusions== | ==Alkane Degradation Results & Conclusions== | ||
- | + | [[Image:TUDelft_Alkane_degradation_route.png|600px|thumb|center|'''Figure 1''' – Schematic description of the alkane degradation pathway with the corresponding genes.]] | |
===Alkb2 Cluster=== | ===Alkb2 Cluster=== |
Revision as of 14:51, 22 October 2010
Alkane Degradation Results & Conclusions
Alkb2 Cluster
LadA
ADH
ADH was tested with Dodecanol (C12)
This yielded the following results:
Conditions | Native | Native | Heated | Heated |
Sample | J13002 | K398018 | J13002 | K398018 |
Total protein in well | 3.303E-02 | 3.180E-02 | 7.351E-03 | 7.994E-03 |
Specific activity (kat/mg) | 1.812E-11 | 2.606E-11 | 0.000E-00 | 5.041E-12 |
This shows two things. That E.Coli is partly able to degrade Dodecanol on it's own. And that this activity is greatly increased (43.83% normalized for the amount of protein) with the addition of the ADH gene. It is also clear that eventhough ADH is from a thermophilic organism it loses most (63.5%) of it's activity after heating. the raw data for these calculations can be seen below. (Although this decrease in activity could also be attributed to the host organism lacking the proper post translational modifications.)