4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite

Oh Sung Kwean, Su Yeon Cho, Jun Won Yang, Wooyoun Cho, Sungyoon Park, Yejee Lim, Min Chul Shin, Han Suk Kim, Joonhong Park, Han S. Kim

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


A biodegradation facilitator which catalyzes the initial steps of 4-chlorophenol (4-CP) oxidation was prepared by immobilizing multiple enzymes (monooxygenase, CphC-I and dioxygenase, CphA-I) onto a natural inorganic support. The enzymes were obtained via overexpression and purification after cloning the corresponding genes (cphC-I and cphA-I) from Arthrobacter chlorophenolicus A6. Then, the recombinant CphC-I was immobilized onto fulvic acid-activated montmorillonite. The immobilization yield was 60%, and the high enzyme activity (82.6%) was retained after immobilization. Kinetic analysis indicated that the Michaelis-Menten model parameters for the immobilized CphC-I were similar to those for the free enzyme. The enzyme stability was markedly enhanced after immobilization. The immobilized enzyme exhibited a high level of activity even after repetitive use (84.7%) and powdering (65.8%). 4-CP was sequentially oxidized by a multiple enzyme complex, comprising the immobilized CphC-I and CphA-I, via the hydroquinone pathway: oxidative transformation of 4-CP to hydroxyquinol followed by ring fission of hydroxyquinol.

Original languageEnglish
Pages (from-to)268-275
Number of pages8
JournalBioresource technology
Publication statusPublished - 2018 Jul

Bibliographical note

Funding Information:
This research was supported by the Faculty Research Fund of Konkuk University 2017.

Publisher Copyright:
© 2018 Elsevier Ltd

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Environmental Engineering
  • Renewable Energy, Sustainability and the Environment
  • Waste Management and Disposal


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