Specificity of Rhodococcus opacus 1CP cells' responses to benzoate and 3-chlorobenzoate.

Elena V Emelyanova, Inna P Solyanikova
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引用次数: 2

Abstract

Background: Halogenated aromatic compounds are more resistant to microbial degradation than non-halogenated aromatic compounds. Microbial degradation of sodium benzoate in the presence of sodium 3-chlorobenzoate is of interest. The ability to degrade aromatic compounds is largely determined by the substrate specificity of the first enzyme that initiates degradation, namely, benzoate 1,2-dioxygenase for benzoate degradation, and 3-chlorobenzoate 1,2-dioxygenase for 3-chlorobenzoate degradation. In this study, the perspective of immobilized cells of Rhodococcus opacus 1CP actinobacterium for degradation of benzoate and 3-chlorobenzoate was explored.

Methods: The biosensor approach (a membrane microbial sensor based on immobilized cells of Rhodococcus opacus 1CP and the Clark-type oxygen electrode as a transducer) was applied to evaluate the actinobacterial cells' responses to benzoate and 3-chlorobenzoate in the absence of both enzymes, benzoate 1,2-dioxygenase and 3-chlorobenzoate 1,2-dioxygenase, or in the presence of one of the said enzymes.

Results: Data obtained show that 1CP actinobacterium possessed a constitutive system for the transport of benzoate and 3-chlorobenzoate into culture cells. The affinity of the transport system for benzoate was higher than that for 3-chlorobenzoate. Moreover, adaptation to one substrate did not preclude the use of the second substrate. Probably, porins facilitated the penetration of benzoate and 3-chlorobenzoate into 1CP cells. Analyzing V vs. S dependencies, negative cooperativity was found, when benzoate 1,2-dioxygenase bound substrate (3-chlorobenzoate), while positive cooperativity was determined at benzoate binding. The observed difference could be associated with the presence of at least two systems of 3-chlorobenzoate transport into actinobacterial cells and allosteric interaction of active sites of benzoate 1,2-dioxygenase in the presence of 3-chlorobenzoate.

Conclusions: The membrane microbial sensor based on immobilized Rhodococcus opacus 1CP cells could be useful as a perspective tool for comparative evaluation of enzymes of complex structure such as benzoate- and 3-chlorobenzoate 1,2-dioxygenase.

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不透明红球菌1CP细胞对苯甲酸盐和3-氯苯甲酸盐反应的特异性
背景:卤代芳香族化合物比非卤代芳香族化合物更耐微生物降解。微生物降解苯甲酸钠在3-氯苯酸钠的存在是感兴趣的。降解芳香族化合物的能力在很大程度上取决于启动降解的第一种酶的底物特异性,即降解苯甲酸酯的苯甲酸酯1,2-双加氧酶和降解3-氯苯酸酯的3-氯苯酸酯1,2-双加氧酶。本研究探讨了不透明红球菌1CP放线菌固定化细胞降解苯甲酸盐和3-氯苯甲酸盐的前景。方法:采用生物传感器方法(一种基于固定化不透明红球菌1CP细胞和clark型氧电极作为传感器的膜微生物传感器)评估放线菌细胞在不含苯甲酸酯1,2-双加氧酶和3-氯苯甲酸酯1,2-双加氧酶或存在其中一种酶的情况下对苯甲酸酯和3-氯苯甲酸酯的反应。结果:1CP放线菌具有向培养细胞输送苯甲酸酯和3-氯苯甲酸酯的组成系统。转运系统对苯甲酸盐的亲和力高于对3-氯苯甲酸盐的亲和力。此外,对一种底物的适应并不排除对第二种底物的使用。可能,孔蛋白促进了苯甲酸盐和3-氯苯甲酸盐渗透到1CP细胞中。分析V与S的依赖关系,发现苯甲酸1,2-双加氧酶与底物(3-氯苯甲酸酯)结合时呈负协同性,而苯甲酸酯与底物(3-氯苯甲酸酯)结合时呈正协同性。观察到的差异可能与至少两种系统的存在有关- 3-氯苯甲酸酯转运到放线菌细胞和苯甲酸1,2-双加氧酶活性位点在3-氯苯甲酸酯存在下的变抗相互作用。结论:基于固定化不透明红球菌1CP细胞的膜微生物传感器可作为比较评价苯甲酸和3-氯苯甲酸1,2-双加氧酶等复杂结构酶的前瞻性工具。
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