Enzymatic conversion of dehydrodivanillin to vanillin by an anaerobic recombinant FE7

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Enzymatic degradation of dehydrodivanillin (DDV) was studied using high performance liquid chromatography (HPLC) with an anaerobic DDV-degrading recombinant FE7 under both aerobic and anaerobic conditions. When 200 mg of FE7 cells were mixed with 40 μg DDV in 1 ml phosphate buffer (0.01 M, pH 7.0) and 10 mM mercaptoethanol and incubated at 37°C for 24 h under an O 2-free CO 2 atmosphere, about 20 μg of DDV was decomposed. Only 12 μg DDV could be degraded when the same reaction was done under aerobic conditions, suggesting that the reaction occurs more easily under anaerobic than aerobic conditions. Enzymatic degradation of DDV was performed using a cell-free extract as a crude enzyme solution under aerobic conditions in a similar way. A reaction product detected and analysed by thin layer, high performance liquid and gas chromatographies and mass spectrometry was found to be vanillin from enzymatic reaction mixture. This enzymatic activity was not detected in either the culture supernatant or the heat-inactivated control. These results suggest that there may be an intracellular enzyme system which is involved in the conversion of DDV to vanillin. This is the first report to study the enzymatic degradation of DDV by anaerobes.