Team:Bielefeld-Germany/Results/Laccases

From 2012.igem.org

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:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/thermo ''Thermus thermophilus'' laccase TTHL]
:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/thermo ''Thermus thermophilus'' laccase TTHL]
:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/tvel5 ''Trametes versicolor'' laccase TVEL5]
:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/tvel5 ''Trametes versicolor'' laccase TVEL5]
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:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/comparison Comparison of the different bacterial laccases]
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:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/comparison Comparison of the different bacterial laccases
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:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/trametis Purchased positive control ''Trametes versicolor'' laccase TVEL0]
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:* [http://2012.igem.org/Team:Bielefeld-Germany/Results/trametis Purchased positive control TVEL0]
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Revision as of 03:07, 27 October 2012

Laccases


Figure 1: The picture was done with Jmol-software in combination with the data from the RCSB Protein Data Bank


The iGEM Team successfully produced four active bacterial laccases and an eukaryotic laccase (click for the results):




All four laccases (ECOL, BPUL, BHAL and TTHL) we accomplished to purify. Besides the successfully scale-up fermentation, those laccases could be purified in a high amount to characterize the optimal activity conditions regarding pH, temperature, buffer solutions and organic solvent resistance. Furthermore the iGEM Team Bielefeld demonstrated that the produced laccases can be immobilized maintaining their activity and the degradation capacity was screened for several micro-contaminants. These tests indicate that the ECOL and BPUL are able to degrade ethinyl estradiol and estradiol.

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