Characterization of Styrene Oxide Isomerase, a Key Enzyme of Styrene and Styrene Oxide Metabolism in Corynebacterium sp.

Abstract

Styrene oxide isomerase (SOI) [EC 5.3.99.7], most probably located in the cell wall, was partially purified from Corynebacterium sp. AC-5 cells grown in a styrene gas atmospheres. The enzyme catalyzed the isomerization reaction to give phenylacetaldehyde, but did not catalyze its reverse reaction. The optimum pH of the reaction was around 7.0, and the enzyme was unstable below pH 6.0. The K_m toward styrene oxide was very low (7.7×10^-5 M), indicating its high affinity for styrene oxide. The enzyme showed strict substrate specificity, and epoxide compounds other than styrene oxide did not serve as substrates. (S)-Styrene oxide was preferentially converted by the enzyme, compared with the (R)-isomer. The possible application of SOI as a biocatalyst is also discussed.