Studies from University of Belgrade Add New Findings in the Area of Escherichia Coli [Chemoselective biocatalytic reduction of conjugated...

Life Science Weekly |

Studies from University of Belgrade Add New Findings in the Area of Escherichia Coli [Chemoselective biocatalytic reduction of conjugated nitroalkenes: New application for an Escherichia coli BL21(DE3) expression strain] By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Proteobacteria. According to news reporting out of Belgrade, Serbia, by NewsRx editors, research stated, "Chemoselective reduction of activated carbon-carbon double bond in conjugated nitroalkenes was achieved using Escherichia coli BL21(DE3) whole cells. Nine different substrates have been used furnishing the reduced products in moderate to good yields. 1-Nitro-4-phenyl-1,3-butadiene and (2-nitro-1-propenyl)benzene were successfully biotransformed with corresponding product yields of 54\% and 45\% respectively." Our news journalists obtained a quote from the research from the University of Belgrade, "Using this simple and environmentally friendly system 2-(2-nitropropyl)pyridine and 2-(2-nitropropyl)naphthalene were synthesized and characterized for the first time. High substrate conversion efficiency was coupled with low enantioselectivity, however 29\% enantiomeric excess was detected in the case of 2-(2-nitropropyl)pyridine. It was shown that electronic properties of the aromatic ring, which affected polarity of the double bond, were not highly influential factors in the reduction process, but the presence of the nitro functionality was essential for the reaction to proceed. 1-Phenyl-4-nitro-1,3-butadiene could not be biotransformed by whole cells of Pseudomonas putida KT2440 or Bacillus subtilis 168 while it was successfully reduced by E. coli DH5 alpha but with lower efficiency in comparison to E. coli BL21(DE3). Knockout mutant affected in nemA gene coding for N-ethylmaleimide reductase (BL21 Delta nemA) could still catalyze bioreductions suggesting multiple active reductases within E. coil BL21(DE3) biocatalyst." According to the news editors, the research concluded: "The described biocatalytic reduction of substituted nitroalkenes provides an efficient route for the preparation of the corresponding nitroalkanes and introduces the new application of the strain traditionally utilized for recombinant protein expression." For more information on this research see: Chemoselective biocatalytic reduction of conjugated nitroalkenes: New application for an Escherichia coli BL21(DE3) expression strain. Enzyme and Microbial Technology, 2014;60():16-23. Enzyme and Microbial Technology can be contacted at: Elsevier Science Inc, 360 Park Ave South, New York, NY 10010-1710, USA. (Elsevier - www.elsevier.com; Enzyme and Microbial Technology - www.elsevier.com/wps/product/cws_home/525004) Our news journalists report that additional information may be obtained by contacting P. Jovanovic, University of Belgrade, Fac Pharm, Dept. of Pharmaceut Chem, Belgrade 11221, Serbia. Additional authors for this research include S. Jeremic, L. Djokic, V. Savic, J. Radivojevic, V. Maslak, B. Ivkovic, B. Vasiljevic and J. Nikodinovic-Runic (see also Proteobacteria). Keywords for this news article include: Serbia, Europe, Belgrade, Escherichia coli, Enterobacteriaceae, Gammaproteobacteria, Gram-Negative Bacteria Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC

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