首页> 外文期刊>Biochemical Engineering Journal >Simultaneous purification and immobilization of laccase on magnetic zeolitic imidazolate frameworks: Recyclable biocatalysts with enhanced stability for dye decolorization
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Simultaneous purification and immobilization of laccase on magnetic zeolitic imidazolate frameworks: Recyclable biocatalysts with enhanced stability for dye decolorization

机译:在磁共沸石咪唑酯骨架上同时纯化和固定漆:可回收生物催化剂,具有增强的染料脱色稳定性

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摘要

Laccases are versatile oxidases showing strong ability to eliminate hazardous pollutants from wastewater. Magnetic zeolitic imidazolate framework-8 (Fe304@ZIF-8) nanoparticles were synthesized by a facile method and used for single-step purification and immobilization of recombinant laccase from Escherichia coli culture supernatant. An activity recovery of 75.7% was achieved for the immobilized biocatalyst. The storage and thermal stability of laccase was remarkably enhanced after immobilization. The immobilized laccase exhibited optimum temperature at 80°C. It retained about 46.0% of initial activity after 6 h incubation at 80°C, while the free laccase was totally inactivated by this treatment. In addition, the immobilized enzyme maintained 87.1% activity after 10 days of storage at 30°C. Finally, excellent reusability was also observed for the immobilized laccase, which was able to completely decolorize indigo carmine after 5 consecutive cycles. Therefore, the immobilization of laccase on Fe304@ZIF-8 nanoparticles offers a facile and cost-effective way for environmental application of bacterial laccase.
机译:漆酶是通用氧化酶,显示出消除废水的有害污染物的强能力。磁共沸石咪唑酯框架-8(FE304 @ ZIF-8)纳米颗粒通过容易方法合成,并用于从大肠杆菌培养上清液中的重组漆酶的单步纯化和固定化。对于固定的生物催化剂,实现了75.7%的活动回收率。固定后,漆酶的储存和热稳定性显着提高。固定化漆酶在80℃下表现出最佳温度。在80℃温育后,它保留约46.0%的初始活性,而通过该处理完全灭活免漆酶。此外,在30℃下储存10天后,固定化酶在10天后保持87.1%。最后,对于固定的漆酶也观察到优异的可重用性,其能够在连续5个循环后完全脱色靛蓝胭脂红。因此,FE304 @ ZIF-8纳米颗粒的漆酶固定化为细菌漆酶的环境应用提供了一种容易和成本效益的方式。

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