4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite. (July 2018)

• Record Type: Journal Article
• Authors: Kwean, Oh Sung; Cho, Su Yeon; Yang, Jun Won; Cho, Wooyoun; Park, Sungyoon; Lim, Yejee; Shin, Min Chul; Kim, Han-Suk; Park, Joonhong; Kim, Han S.
• Is Part Of: Bioresource technology. Volume 259(2018)
• Page Start: 268
• Page End: 275
• Publication Date: 2018-07
• Subjects: Biodegradation facilitator -- 4-Chlorophenol -- Recombinant technology -- Oxygenase -- Immobilization; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2018.03.066
• Languages: English
• ISSNs: 0960-8524

Abstract

Graphical abstract: Highlights: Enzymatic biodegradation facilitator was developed. Recombinant 4-CP mono- and di-oxygenases were immobilized together. Immobilization improved enzyme stability and handling efficiency. 4-CP is converted to hydroxyquinol and then ring-fissioned by the facilitator. Abstract: 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.