Team:Hong Kong CUHK/abstract
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<p> <strong> Polycyclic aromatic hydrocarbons (PAHs) are harmful to both environment and human health. We proposed the PAHs degradation system, which contains codon-optimized laccase from Bacillus sp. HR03 and catechol 1,2-dioxygenase from Pseudomonas putida KT2440 for Escherichia coli. The system was capable of degrading PAHs into less toxic simple carboxylic acid. Also, since quinones are intermediates in the pathway, we added quinone sensing and response repressor (QsrR) to regulate the degradation process. To accelerate the degradation, we used Voltage Switch (VS), the other great highlight of our project. We designed a novel transmembrane protein called Voltage Switch (VS), which is a fusion protein utilizing the voltage sensing domain from potassium ion channels. Triggered by change in potential across the cell membrane, VS can separate or bring targeting enzymes into proximity; thus allowing an instant control of enzymatic reaction.</strong></p> | <p> <strong> Polycyclic aromatic hydrocarbons (PAHs) are harmful to both environment and human health. We proposed the PAHs degradation system, which contains codon-optimized laccase from Bacillus sp. HR03 and catechol 1,2-dioxygenase from Pseudomonas putida KT2440 for Escherichia coli. The system was capable of degrading PAHs into less toxic simple carboxylic acid. Also, since quinones are intermediates in the pathway, we added quinone sensing and response repressor (QsrR) to regulate the degradation process. To accelerate the degradation, we used Voltage Switch (VS), the other great highlight of our project. We designed a novel transmembrane protein called Voltage Switch (VS), which is a fusion protein utilizing the voltage sensing domain from potassium ion channels. Triggered by change in potential across the cell membrane, VS can separate or bring targeting enzymes into proximity; thus allowing an instant control of enzymatic reaction.</strong></p> | ||
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Revision as of 08:43, 27 October 2013