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首页> 外文期刊>RSC Advances >Self-assembled 2,4-dichlorophenol hydroxylase-inorganic hybrid nanoflowers with enhanced activity and stability
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Self-assembled 2,4-dichlorophenol hydroxylase-inorganic hybrid nanoflowers with enhanced activity and stability

机译：自组装的2,4-二氯苯酚羟化酶 - 无机杂交纳米哨具有增强的活性和稳定性

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摘要

2,4-Dichlorophenol hydroxylase (2,4-DCP hydroxylase) is a key enzyme in the degradation of 2,4-dichlorophenoxyacetic acid in the hydroxylation step in many bacteria. Our previous study demonstrated that a cold-adapted 2,4-DCP hydroxylase (tfdB-JLU) exhibits broad substrate specificity for chlorophenols, biphenyl derivatives and their homologues. However, the stability of this enzyme is not satisfactory in practical use. There have been no reports of immobilizing a cold-adapted enzyme to improve its activity and stability so far. This study for the first time reports a facile approach for the synthesis of hybrid nanoflowers (hNFs) formed from cold-adapted 2,4-dichlorophenol hydroxylase (tfdB-JLU) and Cu-3(PO4)(2)3H(2)O. The influence of experimental factors, such as the pH of the solution mixture and the enzyme and Cu2+ concentrations, on the activity of the prepared tfdB-JLU-hNFs is investigated. The morphologies of the tfdB-JLU-hNFs are further analyzed by SEM and TEM. Compared to the free enzyme, the tfdB-JLU-hNFs exhibit up to 162.46 +/- 1.53% enhanced 2,4-dichlorophenol degradation activity when encapsulated at different enzyme concentrations. The tfdB-JLU-hNFs exhibit excellent durability with 58.34% residual activity after six successive cycles, and up to 90.58% residual activity after 20 days of storage. These results demonstrate that this multistage and hierarchical flower-like structure can effectively increase enzyme activity and stability with respect to those of the free enzyme. The satisfactory removal rate of 2,4-dichlorophenol catalyzed by tfdB-JLU-hNFs suggests that this immobilized enzyme exhibits great potential for application in bioremediation.
机译：2,4-二氯苯酚羟化酶（2,4-DCP羟化酶）是许多细菌中羟基化步骤中2,4-二氯苯酸乙酸的偏重中的关键酶。我们以前的研究表明，冷调用的2,4-DCP羟化酶（TFDB-JLU）对氯酚，联苯衍生物及其同源物具有宽的底物特异性。然而，这种酶的稳定性在实际用途方面不令人满意。目前没有报道未提高冷适应酶以改善其活动和稳定性。本研究首次报告了合成由冷适应的2,4-二氯苯酚羟化酶（TFDB-JLU）和Cu-3（PO4）（2）3H（2）o形成的杂化纳米辊（HNFS）的容易方法。 。研究了实验因子的影响，例如溶液混合物的pH和酶和Cu2 +浓度，对制备的TFDB-JLU-HNFS的活性进行研究。通过SEM和TEM进一步分析TFDB-JLU-HNFS的形态。与游离酶相比，当以不同的酶浓度包封时，TFDB-JLU-HNFS显着高达162.46 +/- 1.53％增强的2,4-二氯苯酚降解活性。 TFDB-JLU-HNFS在六个连续循环后具有优异的耐久性，含有58.34％的残余活性，储存20天后的残余活性高达90.58％。这些结果表明，这种多级和等级的花状结构可以有效地增加与游离酶的酶活性和稳定性。 TFDB-JLU-HNFS催化的2,4-二氯苯酚的令人满意的去除率表明，这种固定化酶在生物化中表现出巨大的应用潜力。

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  • 来源
    《RSC Advances》 |2018年第37期|共6页
  • 作者

    Fang Xuexun; Zhang Chengkai; Qian Xue; Yu Dahai;

  • 作者单位

    Jilin Univ Minist Educ Key Lab Mol Enzymol &

    Engn Coll Life Sci 2699 Qianjin St Changchun 130012 Jilin Peoples R China;

    Jilin Univ Minist Educ Key Lab Mol Enzymol &

    Engn Coll Life Sci 2699 Qianjin St Changchun 130012 Jilin Peoples R China;

    Jilin Univ Minist Educ Key Lab Mol Enzymol &

    Engn Coll Life Sci 2699 Qianjin St Changchun 130012 Jilin Peoples R China;

    Jilin Univ Minist Educ Key Lab Mol Enzymol &

    Engn Coll Life Sci 2699 Qianjin St Changchun 130012 Jilin Peoples R China;

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