Regioselective biooxidation of (+)-valencene by recombinant E. coli expressing CYP109B1 from Bacillus subtilis in a two-liquid-phase system

Additional file 1:

12% SDS-PAGE of protein expression in recombinant E. coli and purified CYP109B1, putidaredoxin reductase (PdR) and putidaredoxin (Pdx). The picture provided shows protein expression as follows: Uninduced E. coli whole-cells (line 1); induced CYP109B1-, PdR- and Pdx-co-expressing strain (line 2); induced PdR- and Pdx-co-expressing strain (line 3); soluble protein fraction of CYP109B1 overexpression strain (line 4); purified CYP109B1 (line 5); purified PdR (line 6); purified Pdx (line 7); PageRuler™ Unstained Protein Ladder (line M). The molecular weights were estimated with 45.0 kDa for CYP109B1, 43.5 kDa for PdR and 11.6 kDa for Pdx.

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Additional file 2:

Mass spectra of oxidation products derived from (+)-valencene conversion. The mass spectra provided correspond to the GC-chromatogram shown in Figure 2. Each spectrum is numbered according to the peak number given in Figure 2. The numbers represent spectra of cis-nootkatol (peak 2), trans-nootkatol (peak 3), (+)-nootkatone (peak 4) and overoxidation products (peaks 5, 6 and 7). Mass spectra of 2, 3 and 4 were compared to those of authentic reference compounds that were either commercially available or have been synthesized chemically in our lab.

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