...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of environmental science and health >Benzoate degradation by Rhodococcus opacus 1CP after dormancy: Characterization of dioxygenases involved in the process
【24h】

Benzoate degradation by Rhodococcus opacus 1CP after dormancy: Characterization of dioxygenases involved in the process

机译：休眠后不透明红球菌1CP对苯甲酸酯的降解：该过程中涉及的双加氧酶的表征

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The process of benzoate degradation by strain Rhodococcus opacus 1 CP after a five-year dormancy was investigated and its peculiarities were revealed. The strain was shown to be capable of growth on benzoate at a concentration of up to 10 g L~(-1) The substrate specificity of benzoate dioxygenase (BDO) during the culture growth on a medium with a low (200-250 mg L~(-1)) and high (4 g L~(-1)) concentration of benzoate was assessed. BDO of R. opacus 1CP was shown to be an extremely narrow specificity enzyme. Out of 31 substituted benzoates, only with one, 3-chlorobenzoate, its activity was higher than 9% of that of benzoate. Two dioxygenases, catechol 1,2-dioxygenase (Cat 1,2-DO) and protocatechuate 3,4-dioxygenase (PCA 3,4-DO), were identified in a cell-free extract, purified and characterized. The substrate specificity of Cat 1,2-DO isolated from cells of strain 1CP after the dormancy was found to differ significantly from that of Cat 1,2-DO isolated earlier from cells of this strain grown on benzoate. By its substrate specificity, the described Cat 1,2-DO was close to the Cat 1,2-DO from strain 1 CP grown on 4-methylbenzoate. Neither activity nor inhibition by protocatechuate was observed during the reaction of Cat 1,2-DO with catechol, and catechol had no inhibitory effect on the reaction of PCA 3,4-DO with protocatechuate.
机译：研究了五年休眠后菌株Ropadococcus opacus 1 CP对苯甲酸盐的降解过程，并揭示了其独特性。已显示该菌株能够以高达10 g L〜（-1）的浓度在苯甲酸盐上生长。在低（200-250 mg L）的培养基上培养生长期间，苯甲酸盐双加氧酶（BDO）的底物特异性评估了〜（-1））和高浓度（4 g L〜（-1））的苯甲酸酯。 R. opacus 1CP的BDO被证明是一种非常窄的特异性酶。在31个取代的苯甲酸酯中，只有一种3-氯苯甲酸酯的活性高于苯甲酸酯的9％。在无细胞提取物中鉴定了两种二加氧酶，儿茶酚1,2-二加氧酶（Cat 1,2-DO）和原儿茶酸3,4-二加氧酶（PCA 3,4-DO），进行了纯化和鉴定。发现在休眠后从菌株1CP的细胞中分离的Cat 1,2-DO的底物特异性与之前从在苯甲酸盐上生长的该菌株的细胞中分离的Cat 1,2-DO的底物特异性显着不同。通过其底物特异性，所述的Cat 1,2-DO与在4-甲基苯甲酸酯上生长的菌株1 CP的Cat 1,2-DO接近。 Cat 1,2-DO与邻苯二酚的反应过程中未观察到活性或原儿茶酸的抑制作用，而儿茶酚对PCA 3,4-DO与原儿茶酸的反应没有抑制作用。

著录项

  • 来源
    《Journal of environmental science and health》 |2016年第3期|182-191|共10页
  • 作者

    Inna P. Solyanikova; Elena V. Emelyanova; Oksana V. Borzova; Ludmila A.Golovleva;

  • 作者单位

    FSBIS G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Russia;

    FSBIS G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Russia;

    FSBIS G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Russia,Pushchino State Natural Science Institute, Pushchino, Russia;

    FSBIS G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Russia,Pushchino State Natural Science Institute, Pushchino, Russia,Laboratory of Enzymatic Degradation of Organic Compounds, Institute of Biochemistry and Physiology of Microorganisms, Russian Acad. Sci., Prospekt Nauki, 5, Pushchino, Moscow Region 142290, Russia;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    Rhodococcus opacus 1CP; benzoate; benzoate dioxygenase; catechol 1; 2-dioxygenase; protocatechuate 3; 4-dioxygenase; substrate specificity;

    机译：不透明红球菌1CP;苯甲酸酯苯甲酸酯双加氧酶;儿茶酚1;2-双加氧酶;原儿茶酸3;4-双加氧酶;底物特异性;

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号