Effective biochemical decomposition of chlorinated aromatic hydrocarbons with a biocatalyst immobilized on a natural enzyme support

Title
Effective biochemical decomposition of chlorinated aromatic hydrocarbons with a biocatalyst immobilized on a natural enzyme support
Authors
이석헌Sun H. LeeSong J. RyuChristina S. KangYanasinee Suma김한승
Keywords
Cloning; Catechol dioxygenase; Enzyme immobilization; Natural enzyme support; Chlorinated aromatic hydrocarbon
Issue Date
2013-08
Publisher
Bioresource technology
Citation
VOL 141, 89-96
Abstract
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 νmax and KM 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.
URI
http://pubs.kist.re.kr/handle/201004/46619
ISSN
09608524
Appears in Collections:
KIST Publication > Article
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