Notice of RetractionCloning, Expression, and Characterization of Recombinant Hydroxyquinol-1, 2-Dioxygenase from Pseudomonas sp. strain HS-D38

2011 5th International Conference on Bioinformatics and Biomedical Engineering Pub Date : 2011-05-10 DOI:10.1109/ICBBE.2011.5781591

Xueting Yang, Yongze Yuan, Jian Liu, Chieri Kimoto, Li Xiong, H. Geng, Deli Liu, Xianfang Wen, Hailing Xi, Yongliang Zheng

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Abstract

Hydroxyquinol 1, 2-Dioxygenase is a key enzyme for p-nitrophenol (PNP) catabolism in bacterium. In this paper, we cloned a pnpC gene encoding hydroxyquinol-1, 2-dioxygenase from Pseudomonas sp. strain HS-D38 that could degrade PNP efficiently. The open reading frame of the pnpC contained 873 nucleotides and the deduced molecular mass of gene product (PnpC) was 33 kDa The recombinant enzyme was highly expressed in E. coli BL21(DE3) as a histidine-tag fusion protein and purified to homogeneity by Ni-NAT affinity chromatography. The specific activity of the purified protein reached at 9.3 U/mg. The maximum activity of the recombinant enzyme towards catechol was exhibited at 45 V and pH5.0. The enzyme activity could be stimulated by 0.2 mM of Fe3+, Fe2+, Cu2+, Zn2+, Mn2+, and Co2+. The above results provided useful information for PnpC application in biodegradation of PNP pollutants.

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假单胞菌HS-D38重组羟基喹啉- 1,2 -双加氧酶的克隆、表达和鉴定

羟基喹啉1,2 -双加氧酶是细菌对硝基酚(PNP)分解代谢的关键酶。本文从假单胞菌HS-D38菌株中克隆了一个能有效降解PNP的羟基喹啉- 1,2 -双加氧酶基因。重组酶在大肠杆菌BL21(DE3)中以组氨酸标签融合蛋白的形式高表达，并通过Ni-NAT亲和层析纯化。纯化后的蛋白比活性达到9.3 U/mg。重组酶在45 V和pH5.0条件下对儿茶酚的活性最大。0.2 mM的Fe3+、Fe2+、Cu2+、Zn2+、Mn2+和Co2+均能刺激酶活性。上述结果为PnpC在PNP污染物生物降解中的应用提供了有益的信息。

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2011 5th International Conference on Bioinformatics and Biomedical Engineering

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