"
Team:Bielefeld-Germany/Results/Summary
From 2011.igem.org
(Difference between revisions)
| Line 2: | Line 2: | ||
<html><img src="https://static.igem.org/mediawiki/2011/3/3f/Bielefeld-header-results-summary.png"/><p></p></html> | <html><img src="https://static.igem.org/mediawiki/2011/3/3f/Bielefeld-header-results-summary.png"/><p></p></html> | ||
| - | We enabled ''E. coli'' to degrade BPA ''in vivo'' and improved the specific BPA degradation rate by creating an Fd<sub>bisd</sub>:CYP<sub>bisd</sub> fusion protein, changing the cytochrome P450 electron transport system from a putidalike bacterial class I type to a class V type. | + | '''Bisphenol A subproject''': We enabled ''E. coli'' to degrade BPA ''in vivo'' and improved the specific BPA degradation rate by creating an Fd<sub>bisd</sub>:CYP<sub>bisd</sub> fusion protein, changing the cytochrome P450 electron transport system from a putidalike bacterial class I type to a class V type. |
| + | |||
| + | '''S-layer subproject''': 4 different S-layer BioBricks with different lattice structures were created and sent to the partsregistry. The behaviour of these genes when expressed in ''E. coli'' were characterized and purification strategies for the expressed proteins were developed. Two purified fluorescent S-layer fusion proteins from different organisms were immobilized on beads, leading to a highly significant fluorescence enhancement of these beads (p < 10<sup>-12</sup>). | ||
Revision as of 17:31, 20 September 2011
Bisphenol A subproject: We enabled E. coli to degrade BPA in vivo and improved the specific BPA degradation rate by creating an Fdbisd:CYPbisd fusion protein, changing the cytochrome P450 electron transport system from a putidalike bacterial class I type to a class V type.
S-layer subproject: 4 different S-layer BioBricks with different lattice structures were created and sent to the partsregistry. The behaviour of these genes when expressed in E. coli were characterized and purification strategies for the expressed proteins were developed. Two purified fluorescent S-layer fusion proteins from different organisms were immobilized on beads, leading to a highly significant fluorescence enhancement of these beads (p < 10-12).
