A new enzymatic method of nitrile synthesis by Rhodococcus sp. strain YH3-3
A new enzymatic method of nitrile synthesis by Rhodococcus sp. strain YH3-3
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DOI：
10.1016/s1381-1177(98)00080-0
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发表时间：
1999-03-11
影响因子：
--
通讯作者：
Asano, Y
中科院分区：
文献类型：
--
作者：
Kato, Y;Ooi, R;Asano, Y
从E-吡啶-3-醛肟同化细菌中分离出的一种新的醛肟脱水酶的底物专一性。对菌株YH3-3进行了鉴定。该酶催化各种芳基和烷基缩醛的脱水反应生成相应的腈，但不作用于芳基和取代的烷基缩醛。在所测试的各种醛肟中，E-吡啶-3-醛肟是最适合该酶的底物。E-吡啶-3-醛肟类似物，如O-乙酰基-E-吡啶-3-醛、Z-吡啶-3-醛、E/Z-吡啶-3-醛-腙等也作为底物被转化为3-氰基吡啶。细胞的热处理增加了3-氰基吡啶从E-吡啶-3-醛肟中的积累，这是因为腈降解酶--腈水合酶失活。在优化的反应条件下(pH 7.0，30℃)，以该菌株的热处理细胞为原料，在制备规模上合成了不同的缩醛类化合物。这是首次报道了由缩醛肟微生物合成腈的方法。(C)1999 Elsevier Science B.V.Au版权所有。
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 degrees 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. (C) 1999 Elsevier Science B.V. AU rights reserved.