Styrene is present in many industrial and domestic effluents, as a widely-used starting material for synthetic polymers. Over the last few decades, a large number of styrene-degrading microorganisms have been isolated. The majority of reports indicate that the predominant catabolic pathway for styrene degradation is through the oxidation of vinyl side chain catalyzed by styrene monooxygenase (SMO). It is a two-component monooxygenase encoded by styA and styB, consisting of an oxygenase (StyA) and a NADH-flavin oxidoreductase (StyB).
In WU’s study, a novel styrene monooxygenase (SMO) was isolated from Pseudomonas sp. LQ26, a styrene degrader from activated sludge. Sequence alignment demonstrated that it was the most distant member of all SMOs originating from the genus of Pseudomonas.
The substrate spectrum of this enzyme extended beyond typical SMO substrates to 1-allylbenzene analogues, previously reported as non-substrates for the SMO from Pseudomonas fluorescens ST.
WU’s results demonstrate for the first time the asymmetric epoxidation of both conjugated and unconjugated alkenes catalyzed by SMO and suggest that a much broader substrate spectrum is expected for SMOs.
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