A new enzymatic method of nitrile synthesis by Rhodococcus sp. strain YH3-3 |
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| Affiliation: | 1. Institute of Geology and Nature Management, Far Eastern Branch of the Russian Academy of Sciences, 675000 Blagoveschensk, Amur Region, Russia;2. Amur State University, 675027 Blagoveschensk, Amur Region, Russia;3. Nikolaev Institute of Inorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia;4. Novosibirsk State University, 630090 Novosibirsk, Russia;1. Beijing Key Laboratory of Bio-inspired Energy Materials and Devices, School of Space and Environment, Beihang University, Beijing 100191, China;2. School of Energy and Power Engineering, Beihang University, Beijing 100191, China;3. School of Environment, Tsinghua University, Beijing 100084, China;1. School of Materials Science and Engineering, Beijing Institute of Technology, Beijing 100081, China;2. State Key Laboratory of New Ceramics and Fine Processing, School of Materials Science and Engineering, Tsinghua University, Beijing, 100084, China;1. Beijing Key Laboratory of Construction Tailorable Advanced Functional Materials and Green Applications, School of Materials Science & Engineering, Beijing Institute of Technology, Beijing 100081, China;2. State Key Laboratory of New Ceramics and Fine Processing, School of Materials Science and Engineering, Tsinghua University, Beijing 100084, PR China |
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| Abstract: | The substrate specificity of a novel aldoxime dehydratase from E-pyridine-3-aldoxime assimilating bacterium, Rhodococcus sp. strain YH3-3, was examined. The enzyme catalyzed a dehydration reaction of various aryl- and alkyl-aldoximes to form the corresponding nitriles, but did not act on arylalkyl- and substituted alkyl-aldoximes. Of various aldoximes tested, E-pyridine-3-aldoxime was the most suitable substrate for the enzyme. E-Pyridine-3-aldoxime analogs such as O-acetyl-E-pyridine-3-aldoxime, Z-pyridine-3-aldoxime, and E/Z-pyridine-3-aldehyde-hydrazone also acted as substrates and were converted to 3-cyanopyridine. Heat-treatment of the cells increased the accumulation of 3-cyanopyridine from E-pyridine-3-aldoxime because the nitrile degrading enzyme, nitrile hydratase was inactivated. Under the optimized reaction conditions (pH 7.0, 30°C), various nitriles were synthesized from the corresponding aldoximes in preparative scales with heat-treated cells of the strain. This is the first report on the microbial synthesis of nitriles from aldoximes. |
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