Karger Publishers
Browse
494384_sm1.doc (497 kB)

Supplementary Material for: Identification of A Ring-Hydroxylating Dioxygenases Capable of Anthracene and Benz[a]anthracene Oxidization from Rhodococcus sp. P14

Download (497 kB)
dataset
posted on 2018-12-19, 11:18 authored by Peng T., Luo A., Kan J., Liang L., Huang T., Hu Z.
Nowadays, contamination of soil and marine sediments by polycyclic aromatic hydrocarbons (PAHs) has become a serious problem all over the world. Rhodococcus sp. P14 was isolated from sediments with crude oil contaminate and showed degradation ability on various PAHs. The genome of Rhodococcus sp. P14 was sequenced. A gene cluster encoding a ring-hydroxylating dioxygenase Baa related to PAH degradation was identified by bioinformatics. The expression level of gene baaA was increased when P14 was cultured with anthracene, pyrene, phenanthrene, or benz[a]­anthracene as the single carbon source. The recombinant protein Baa was overexpressed in E. coli BL21 (DE3). Further investigations on the recombinant protein Baa in E. coli demonstrated that it was able to oxidize anthracene and benz [a]anthracene, resulting in 9,10-dihydroxyanthracene and 7, 12-dihydroxybenz[a]anthracene as metabolites, respectively. These results indicate that Baa plays an important role in PAH degradation in Rhodococcus sp. P14 and Baa has potential application in the bioremediation of PAHs in the contaminated environment.

History

Usage metrics

    Journal of Molecular Microbiology and Biotechnology

    Categories

    Licence

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC