%0 Journal Article %A Oelschlägel, Michel %A Zimmerling, Juliane %A Schlömann, Michael %A Tischler, Dirk %T Styrene oxide isomerase of Sphingopyxis sp. Kp5.2 %D 2014 %J Microbiology, %V 160 %N 11 %P 2481-2491 %@ 1465-2080 %R https://doi.org/10.1099/mic.0.080259-0 %I Microbiology Society, %X Styrene oxide isomerase (SOI) catalyses the isomerization of styrene oxide to phenylacetaldehyde. The enzyme is involved in the aerobic styrene catabolism via side-chain oxidation and allows the biotechnological production of flavours. Here, we reported the isolation of new styrene-degrading bacteria that allowed us to identify novel SOIs. Out of an initial pool of 87 strains potentially utilizing styrene as the sole carbon source, just 14 were found to possess SOI activity. Selected strains were classified phylogenetically based on 16S rRNA genes, screened for SOI genes and styrene-catabolic gene clusters, as well as assayed for SOI production and activity. Genome sequencing allowed bioinformatic analysis of several SOI gene clusters. The isolate Sphingopyxis sp. Kp5.2 was most interesting in that regard because to our knowledge this is the first time it was shown that a member of the family Sphingomonadaceae utilized styrene as the sole carbon source by side-chain oxidation. The corresponding SOI showed a considerable activity of 3.1 U (mg protein)–1. Most importantly, a higher resistance toward product inhibition in comparison with other SOIs was determined. A phylogenetic analysis of SOIs allowed classification of these biocatalysts from various bacteria and showed the exceptional position of SOI from strain Kp5.2. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.080259-0