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辣根过氧化物酶固定于普乐利特® A109 上及其对蒽醌染料的生物降解和解毒潜力

Immobilization of horseradish peroxidase onto Purolite® A109 and its anthraquinone dye biodegradation and detoxification potential.

作者信息

Šekuljica Nataša Ž, Jovanović Jelena R, Jakovetić Tanasković Sonja M, Ognjanović Nevena D, Gazikalović Ivana V, Knežević-Jugović Zorica D, Mijin Dušan Ž

机构信息

Innovation Center, Faculty of Technology and Metallurgy, University of Belgrade, Belgrade, Serbia.

Faculty of Technology and Metallurgy, University of Belgrade, Belgrade, Serbia.

出版信息

Biotechnol Prog. 2020 Jul;36(4):e2991. doi: 10.1002/btpr.2991. Epub 2020 Mar 26.

DOI:10.1002/btpr.2991
PMID:32170846
Abstract

Horseradish peroxidase (HRP) is a highly specific enzyme with great potential for use in the decolorization of synthetic dyes. A comprehensive study of HRP immobilization using various techniques such as adsorption and covalent immobilization on the novel carrier Purolite® A109 with a special focus on enzymatic decolorization and toxicity of artificially colored wastewater. The immobilized preparations with an activity of 156.21 ± 1.41 U g and 85.71 ± 1.62 U g after the HRP adsorption and covalent immobilization, respectively, were obtained. Stability and reusability of the immobilized preparations were also evaluated. A noteworthy decolorization level (~90%) with immobilized HRP was achieved. Phytotoxicity testing using Mung bean seeds and acute toxicity assay with Artemia salina has confirmed the applicability of the obtained immobilized preparation in industrial wastewater plants for the treatment of colored wastewater.

摘要

辣根过氧化物酶(HRP)是一种高度特异性的酶,在合成染料脱色方面具有巨大的应用潜力。本研究全面探讨了采用吸附和共价固定等多种技术将HRP固定在新型载体Purolite® A109上,特别关注酶促脱色以及人工染色废水的毒性。分别通过HRP吸附和共价固定获得了固定化制剂,其活性分别为156.21±1.41 U g和85.71±1.62 U g。还评估了固定化制剂的稳定性和可重复使用性。固定化HRP实现了显著的脱色水平(约90%)。使用绿豆种子进行的植物毒性测试和用卤虫进行的急性毒性测定证实了所得固定化制剂在工业废水处理厂处理有色废水方面的适用性。

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