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[[Cfrenchlabpage|French Lab Main Page]]
[[Cfrenchlabpage|French Lab Main Page]]
Revision as of 08:49, 30 November 2006
- Lecturer in Microbial Biotechnology
- Institute of Cell Biology
- School of Biological Sciences
- University of Edinburgh
- Darwin Building
- King's Buildings
- EH9 3JR
- United Kingdom
- tel +44 (0)131 650 7098
- fax +44 (0)131 650 8650
- e-mail C.French@ed.ac.uk
I am a lecturer in the School of Biological Sciences, University of Edinburgh. My first degree was from Massey University, New Zealand, in Biotechnology and Bioprocess Engineering (basically chemical engineering plus a couple of papers in microbiology). I worked for a while at the Dairy Research Institute in New Zealand, developing methods for purification of high value proteins from whey, and then did a Ph.D. at the University of Cambridge, UK, at the Institute of Biotechnology, working under Neil Bruce (now a professor at the Centre for Novel Agricultural Products, University of York). My thesis topic was 'Biotransformations of the morphine alkaloids'. Basically I purified and characterised an enzyme involved in morphine transformation in soil bacteria, and developed a recombinant E. coli strain for the manufacture of higher value morphine alkaloids (hydrocodone and hydromorphone). I then worked briefly on biotransformations of tropane alkaloids, especially benzoyl ecgonine methyl ester (aka cocaine) before moving on to a postdoc on biotransformations of explosives. I purified and characterized an enzyme involved in the degradation of nitrate ester explosives (nitroglycerine and PETN, pentaerythritol tetranitrate) and nitroaromatic explosives (TNT) and developed transgenic plants which could be used to degrade explosive residues in contaminated soil. I was then offered a lectureship at the University of Edinburgh. Initially I continued work on transgenic plants for phytoremediation of contaminated soil, developing plants able to degrade toxic chlorinated compounds to harmless products, but I have now ceased this work due to a lack of funding (though the plants are still being characterised at Neil Bruce's laboratory in York, publication in preparation). My current research interests include:
- magnetosome synthesis in magnetotactic bacteria (Magnetospirillum spp.). In collaboration with Bruce Ward, also in this department, I have a Ph.D. student (Jen Bell) working on characterisation of proteins involved in the synthesis of magnetite and subcellular localisation of magnetosomes. From what I heard at iGEM2006, I understand that a lot of people are interested in magnetotactic bacteria; however, they are quite tricky to grow. When I have some time to develop this site, I hope to add a section on protocols which Jen has found successful for culturing these organisms.
- biosensors. I have been interested in whole-cell biosensors for some time, and in collaboration with Jim Philp at Napier University (who has now moved to Saudi Arabia), developed recombinant organisms able to detect arsenic, copper and zinc with varying degrees of sensitivity (no luck with nickel so far). I was an instructor for the University of Edinburgh team in iGEM2006. The team used biobrick techniques to develop a novel biosensor for arsenic detection. This was quite a revelation to me. It seems to me that synthetic biology has the potential to revolutionise biosensors, allowing a degree of in vivo signal processing as well as improved output modalities. I hope to develop this idea further in the near future.
- microbial degradation of thiocyanate. This is a minor project which I have been running for some time as a series of undergraduate final year projects. Thiocyanate (SCN-) is a cyanide-like ion used as a lixiviant in gold mining (ie, it dissolves gold). The various different molecules containing the -CN functional group (cyanides, nitriles, cyanate and thiocyanate) are all degraded in soil bacteria via quite different pathways. There are two known pathways for thiocyanate degradation in bacteria. One (cleavage to carbonyl sulphide and ammonia) is well understood, but the other, apparently mor common pathway (generally believed to be cleavage to hydrogen sulfide and cyanate) is not well understood, and no enzymes catalysing this reaction are known (as far as I know; please let me know if you know otherwise). I have a theory that the reaction is more complicated than this, but have so far been unable to prove it. However, I do have a large collection of thiocyanate-degrading bacteria, if anyone would like some. The work has potential practical applications in phytoextraction of gold from low grade ore.