Lee, Seok H. Lee, Sun H. Ryu, Song J. Kang, Christina S. Suma, Yanasinee Kim, Han S. 2024-01-20T12:01:01Z 2024-01-20T12:01:01Z 2021-09-05 2013-08 0960-8524 https://pubs.kist.re.kr/handle/201004/127825 The enzymatic decomposition of 4-chlorophenol metabolites using an immobilized biocatalyst was investigated in this study. Catechol 1,2-dioxygenase for ortho ring cleavage obtained via cloning of the corresponding gene cphA-I from Arthrobacter chlorophenolicus A6 was overexpressed and purified. It was found that the cphA-I enzyme could catalyze the degradation of catechol, 4-chlorocatechol, and 3-methylcatechol. The expressed enzyme was immobilized onto a natural enzyme support, fulvic acid-activated montmorillonite. The immobilization yield was as high as 63%, and the immobilized enzyme maintained high substrate utilization activity, with only a 15-24% reduction in the specific activity. Kinetic analysis demonstrated marginal differences in nu(max) and K-M values for the free and immobilized enzymes, indicating that inactivation of the immobilized enzyme was minimal. The immobilized enzyme exhibited notably increased stability against changes in the surrounding environment (temperature, pH, and ionic strength). Our results provide useful information for the effective enzymatic biochemical treatment of hazardous organic compounds. (C) 2013 Elsevier Ltd. All rights reserved. English ELSEVIER SCI LTD HORSERADISH-PEROXIDASE CATECHOL 1,2-DIOXYGENASE P-CHLOROPHENOL 4-CHLOROPHENOL DEGRADATION PHENOL PURIFICATION REMOVAL MONTMORILLONITE BIODEGRADATION Effective biochemical decomposition of chlorinated aromatic hydrocarbons with a biocatalyst immobilized on a natural enzyme support Article 10.1016/j.biortech.2013.01.159 1 BIORESOURCE TECHNOLOGY, v.141, pp.89 - 96 BIORESOURCE TECHNOLOGY 141 89 96 scie scopus 000321315200016 2-s2.0-84878898391 Agricultural Engineering Biotechnology & Applied Microbiology Energy & Fuels Agriculture Biotechnology & Applied Microbiology Energy & Fuels Article; Proceedings Paper HORSERADISH-PEROXIDASE CATECHOL 1,2-DIOXYGENASE P-CHLOROPHENOL 4-CHLOROPHENOL DEGRADATION PHENOL PURIFICATION REMOVAL MONTMORILLONITE BIODEGRADATION Cloning Catechol dioxygenase Enzyme immobilization Natural enzyme support Chlorinated aromatic hydrocarbon