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.
Original language | English |
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Pages (from-to) | 268-275 |
Number of pages | 8 |
Journal | Bioresource technology |
Volume | 259 |
DOIs | |
Publication status | Published - 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