Team:Hong Kong CUHK/abstract

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   <h2>Abstract</h2>
   <h2>Abstract</h2>
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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

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