Desulfurization of alkylated forms of both dibenzothiophene and benzothiophene by a single bacterial strain

Abstract Thirty-five bacterial strains capable of converting dibenzothiophene into 2-hydroxybiphenyl were isolated. Among them Rhodococcus erythropolis KA2-5-1 was chosen for further characterization because of its ability to retain high desulfurization activity stably. PCR cloning and DNA sequencin...

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Bibliographic Details
Published in:FEMS microbiology letters 2000-06, Vol.187 (2), p.123-126
Main Authors: Kobayashi, Morio, Onaka, Toshimitsu, Ishii, Yoshitaka, Konishi, Jin, Takaki, Mikihiro, Okada, Hideki, Ohta, Yoshinori, Koizumi, Kenichi, Suzuki, Masanori
Format: Article
Language:English
Subjects:
Alkyl benzothiophene
Alkyl dibenzothiophene
Alkylation
Benzothiophene
Biodegradation, Environmental
Biological and medical sciences
Biotechnology
Cloning
Deoxyribonucleic acid
Desulfurization
Desulfurizing
Dibenzothiophene
DNA
DNA sequencing
Energy
Fundamental and applied biological sciences. Psychology
Gas Chromatography-Mass Spectrometry
Industrial applications and implications. Economical aspects
Microbiology
Monooxygenase
NADH
Nicotinamide adenine dinucleotide
Oxidoreductase
Rhodococcus
Rhodococcus - genetics
Rhodococcus - growth & development
Rhodococcus - isolation & purification
Rhodococcus - metabolism
Soil Microbiology
Sulfur
Thiophenes - metabolism
Use of microorganisms or biopolymers in fossil fuel recovery
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Summary:Abstract Thirty-five bacterial strains capable of converting dibenzothiophene into 2-hydroxybiphenyl were isolated. Among them Rhodococcus erythropolis KA2-5-1 was chosen for further characterization because of its ability to retain high desulfurization activity stably. PCR cloning and DNA sequencing of a KA2-5-1 genomic DNA fragment showed that it was practically identical with dszABC genes from Rhodococcus sp. IGTS8, a representative carbon–sulfur-bond-targeted dibenzothiophene-degrading bacterium. KA2-5-1 desulfurized a variety of alkyl dibenzothiophenes through the specific cleavage of their C–S bonds. In addition, unexpectedly, KA2-5-1 also attacked alkyl benzothiophenes in a C–S-bond-targeted fashion. The purified monooxygenase, encoded by dszC of KA2-5-1, converted benzothiophene and dibenzothiophene into benzothiophene sulfone and dibenzothiophene sulfone, respectively, with the aid of an NADH-dependent oxidoreductase. This result raises the possibility that the same enzymatic step may be involved in desulfurization of alkylated forms of both dibenzothiophene and benzothiophene in KA2-5-1 cells.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2000.tb09147.x