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一种利用固定化 CueO 漆酶样多铜氧化酶在聚 3-羟基丁酸酯上对废水染料进行脱色的酶系统。

An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase-like multicopper oxidase on poly-3-hydroxybutyrate.

机构信息

Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, Avda. Universidad s/n, 03202, Elche, Spain.

Biotechnology Research Group, Textile Research Institute (AITEX), Plaza Emilio Sala 1, 03801, Alcoy, Spain.

出版信息

Microb Biotechnol. 2018 Sep;11(5):881-892. doi: 10.1111/1751-7915.13287. Epub 2018 Jun 12.

DOI:10.1111/1751-7915.13287
PMID:29896867
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6116751/
Abstract

The presence of synthetic dyes in wastewaters generated by the textile industry constitutes a serious environmental and health problem that urges the scientific community on an appropriate action. As a proof-of-concept, we have developed a novel approach to design enzymatic bioreactors with the ability to decolorize dye solutions through the immobilization of the bacterial CueO laccase-like multicopper oxidase from Escherichia coli on polyhydroxybutyrate (PHB) beads by making use of the BioF affinity tag. The decolorization efficiency of the system was characterized by a series of parameters, namely maximum enzyme adsorption capacity, pH profile, kinetic constants, substrate range, temperature and bioreactor recycling. Depending on the tested dye, immobilization increased the catalytic activity of CueO by up to 40-fold with respect to the soluble enzyme, reaching decolorization efficiencies of 45-90%. Our results indicate that oxidase bioreactors based on polyhydroxyalkanoates are a promising alternative for the treatment of coloured industrial wastewaters.

摘要

纺织工业废水中合成染料的存在构成了严重的环境和健康问题,促使科学界采取适当的行动。作为概念验证,我们开发了一种新方法,通过利用 BioF 亲和标签将大肠杆菌的 CueO 漆酶样多铜氧化酶固定在聚羟基丁酸酯 (PHB) 珠上,设计能够通过固定化酶使染料溶液脱色的酶生物反应器。通过一系列参数(即最大酶吸附容量、pH 值曲线、动力学常数、底物范围、温度和生物反应器循环)对系统的脱色效率进行了表征。根据测试的染料,固定化使 CueO 的催化活性相对于可溶性酶提高了 40 倍,达到了 45-90%的脱色效率。我们的结果表明,基于聚羟基链烷酸酯的氧化酶生物反应器是处理有色工业废水的一种很有前途的替代方法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/bdc1244a07a1/MBT2-11-881-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/49d02346badb/MBT2-11-881-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/42a1936e5ffa/MBT2-11-881-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/9493a84f4e9e/MBT2-11-881-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/75eac8cd7782/MBT2-11-881-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/befc5ef70ae4/MBT2-11-881-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/bdc1244a07a1/MBT2-11-881-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/49d02346badb/MBT2-11-881-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/42a1936e5ffa/MBT2-11-881-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/9493a84f4e9e/MBT2-11-881-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/75eac8cd7782/MBT2-11-881-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/befc5ef70ae4/MBT2-11-881-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bc9/6116751/bdc1244a07a1/MBT2-11-881-g006.jpg

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