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Membrane Water Treatment
  Volume 11, Number 3, May 2020 , pages 195-200

Immobilization of oxidative enzymes onto Cu-activated zeolite to catalyze 4-chlorophenol decomposition
Muhamad Najmi Bin Zol, Muhammad Firdaus Bin Shuhaim1, Jimin Yu1c, Yejee Lim, Jae Wan Choe, Sungjun Bae1 and Han S. Kim

    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 metal-histidine binding between the enzyme and Cu-zeolite.
Key Words
    biocatalyst; 4-chlorophenol; enzyme immobilization; Cu-zeolite; coal fly ash
Muhamad Najmi Bin Zol, Muhammad Firdaus Bin Shuhaim, Jimin Yu, Yejee Lim,
Jae Wan Choe, Sungjun Bae and Han S. Kim: Civil and Environmental Engineering, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, Korea
Jae Wan Choe: Civil Engineering, Gwangju University, 277 Hyodeok-ro, Nam-gu, Gwanju, Korea, Korea

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