Rhodococcus boritolerans FW815具有高效水合2,2-二甲基环丙甲腈活性，利用蛋白质柱层析技术从中分离得到R. boritolerans FW815腈水合酶。实验结果表明，该腈水合酶分子量为40 kDa，由大小分别为24 kDa、22 kDa两种亚基构成。R. boritolerans FW815腈水合酶最适作用温度为37℃，最适作用pH值7.0。Cu2+、Zn2+、Ni2+等金属离子及EDTA对该腈水合酶有较强的抑制作用。除2,2-二甲基环丙甲腈、2-氨基-2,3-二甲基丁腈之外，R. boritolerans FW815腈水合酶对2-氧代-1-吡咯烷基丁腈、丙烯腈、2-氨基-4-甲硫基丁腈也表现出腈水合酶活性。% Rhodococcus boritolerans FW815 has strong nitrile hydratase activity towards racemic 2,2-dimethylcyclopropanecarbonitrile. In this work, the nitrile hydratase enzyme (NHase)was purified from R. boritolerans FW815. Results demonstrate that the purified NHase consists of two different subunits with molecular weights of 24 kDa and 22 kDa, respectively. Analytical size exclusion chromatography analysis reveals that this NHase has a molecular weight of 40 kDa. The purified nitrile hydratase enzyme is most active at 37℃, pH 7.0, while Cu2+, Zn2+, Ni2+ and ethylenediaminetertaacetic acid (EDTA) display inhibitory effects on its activity. In addition to 2,2-dimethylcyclopropanecarbonitrile and 2-amino-2,3-dimethylbutyronitrile, it can efficiently hydrate 2-(2-oxopyrrolidin-1-yl) butyronitrile, acrylonitrile and 2-amino-4-methylthio-1-butyronitrile.
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