Team:Bielefeld-Germany/Results/Laccases

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[[File:Bielefeld2012_Trametes_Laccase_klein.jpg|350px|center|thumb|'''Figure 1:''' The picture was done with [http://jmol.sourceforge.net/ Jmol-software] in combination with the data from the [http://www.rcsb.org/pdb/explore/explore.do?structureId=1GYC RCSB Protein Data Bank]]]
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[[File:Bielefeld2012_Trametes_Laccase_klein.jpg|350px|center|thumb|'''Figure 1:''' The figure was designed with [http://jmol.sourceforge.net/ Jmol-software] in combination with the data from the [http://www.rcsb.org/pdb/explore/explore.do?structureId=1GYC RCSB Protein Data Bank]]]
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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.
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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{{Team:Bielefeld/Sponsoren}}
{{Team:Bielefeld/Sponsoren}}

Latest revision as of 03:50, 27 October 2012

Laccases


Figure 1: The figure was designed 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.

55px Logo merck.jpg BioCircle.JPG Bielefeld2012 Evonik.jpg Bielefeld2012 Baxter.png Logo knauer.jpg Logo iit.jpg Bielefeld2012 BIEKUBA.jpg Logo biometra.jpg Logo bio-nrw.png Bielefeld2012 Logo ERASynbio.jpg