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Team:UCL/Science/Results
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| + | <p class="widthCorrect">Our characterisation was driven towards quantifying the toxicity of certain azo dyes and to what extent they can be degraded by bacterial enzymes, more specifically BsDyP, on its own and under the induction of a LacI promoter cassette.</p> | ||
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| + | <p class="widthCorrect">Also, the possible re-purposing of the pre-existing part from UCL 2009 team BBa_K239009 as an azo-dye sensing device was evaluated.</p> | ||
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| + | <p class="widthCorrect">Finally, two possible approaches to biosafety were tested; one of them, assaying the activity of UCL 2012 team nuclease BBa_K729004 in the presence of azo-dyes. The other, testing the performance of an RNAi sequence designed to knock down the expression of Octaprenyl diphosphate synthase, a crucial enzyme in one of the E. coli metabolic pathways, so that in the future we can develop a strain that is only able to use as a substrate synthetic compounds provided externally. More information on this on the Xenobiology page (link)</p> | ||
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Latest revision as of 01:33, 18 October 2014
Characterisation
Our characterisation was driven towards quantifying the toxicity of certain azo dyes and to what extent they can be degraded by bacterial enzymes, more specifically BsDyP, on its own and under the induction of a LacI promoter cassette.
Also, the possible re-purposing of the pre-existing part from UCL 2009 team BBa_K239009 as an azo-dye sensing device was evaluated.
Finally, two possible approaches to biosafety were tested; one of them, assaying the activity of UCL 2012 team nuclease BBa_K729004 in the presence of azo-dyes. The other, testing the performance of an RNAi sequence designed to knock down the expression of Octaprenyl diphosphate synthase, a crucial enzyme in one of the E. coli metabolic pathways, so that in the future we can develop a strain that is only able to use as a substrate synthetic compounds provided externally. More information on this on the Xenobiology page (link)
