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Immobilization of oxidative enzymes onto Cu-activated zeolite to catalyze 4-chlorophenol decomposition

  • Received : 2020.01.11
  • Accepted : 2020.01.17
  • Published : 2020.05.25
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Abstract

In this study, a biocatalyst composite was prepared by immobilizing oxidoreductases onto Cu-activated zeolite to facilitate biochemical decomposition of 4-chlorophenol (4-CP). 4-CP monooxygenase (CphC-I) was cloned from a 4-CP degrading bacterium, Pseudarthrobacter chlorophenolicus A6, and then overexpressed and purified. Type X zeolite was synthesized from non-magnetic coal fly ash using acetic acid treatment, and its surfaces were coated with copper ions via impregnation (Cu-zeolite). Then, the recombinant oxidative and reductive enzymes were immobilized onto Cu-zeolite. The enzymes were effectively immobilized onto the Cu-zeolite (79% of immobilization yield). The retained catalytic activity of CphC-I after immobilization was 0.3423 U/g-Cu-zeolite, which was 63.3% of the value of free enzymes. The results of this study suggest that copper can be used as an effective enzyme immobilization binder because it provides favorable metalhistidine binding between the enzyme and Cu-zeolite.

Keywords

Acknowledgement

This work was supported by the Korea Institute of Energy Technology Evaluation and Planning (KETEP) and the Ministry of Trade, Industry and Energy (MOTIE, 20194010201900), and the National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (2019R1A2C1008706).

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