Identification of metabolites from benzo[a]pyreme oxidation by ligninolytic enzymes of polyporus sp. S133

• Main Authors: Hadibarata, T., Kristanti, R. A.
• Format: Article
• Published: Elsevier 2012
• Subjects: TA Engineering (General). Civil engineering (General)
• Online Access: http://eprints.utm.my/id/eprint/47069/; https://www.sciencedirect.com/science/article/pii/S0301479712003623?via%3Dihub

The biodegradation of benzo[. a]pyrene (B. aP) by using Polyporus sp. S133, a white-rot fungus isolated from oil-contaminated soil was investigated. Approximately 73% of the initial concentration of B. aP was degraded within 30 d of incubation. The isolation and characterization of 3 metabolites by thin layer chromatography, column chromatography, and UV-vis spectrophotometry in combination with gas chromatography-mass spectrometry, indicated that Polyporus sp. S133 transformed B. aP to B. aP-1,6-quinone. This quinone was further degraded in 2 ways. First, B. aP-1,6-quinone was decarboxylated and oxidized to form coumarin, which was then hydroxylated to hydroxycoumarin, and finally to hydroxyphenyl acetic acid by addition of an epoxide group. Second, Polyporus sp. S133 converted B. aP-1,6-quinone into a major product, 1-hydroxy-2-naphthoic acid. During degradation, free extracellular laccase was detected with reduced activity of lignin peroxidase, manganese-dependent peroxidase and 2,3-dioxygenase, suggesting that laccase and 1,2-dioxygenase might play an important role in the transformation of PAHs compounds.