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Studies on the production of (S)-(+)-solketal (2,2-dimethyl-1,3-dioxolane-4-methanol) by enantioselective oxidation of racemic solketal with Comamonas testosteroni

  • Biotechnology
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Abstract

All strains of Comamonas testosteroni investigated here, produced quinohaemoprotein ethanol dehydrogenase (QH-EDH) when grown on ethanol or butanol, but one strain of C. acidovorans and of C. terrigena did not. Hybridization experiments showed that the gene for QH-EDH is absent in the latter two strains. Induction and properties of the QH-EDHs seem to be similar: all C. testosteroni strains produced the enzyme in its apo-form [without pyrroloquinoline quinone (PQQ)] and the levels were higher at growth at low temperature; preference for the R-enentiomer and similar selectivity was shown in the oxidation of solketal (2,2-dimethyl-1,3-dioxolane-4-methanol) by cells (supplemented with PQQ); the fragment of the qhedh gene gave high hybridization with the DNA of the C. testosteroni strains. Experiments with C. testosteroni LMD 26.36 revealed that the organism is well suited for production of (S)-solketal: it shows an adequate enantioselectivity (E value of 49) for the oxidation of racemic solketal; the conversion rate of (R)-solketal is only 3.5 times lower than that of ethanol; the optimal pH for conversion (7.6) is in a region where solketal has sufficient chemical stability; separation of the remaining (S)-solketal from the acid formed is simple; induction of QH-EDH, the sole enzyme responsible for the oxidation of (R)-solketal, occurs during growth on ethanol or butanol so that the presence of solketal (inhibitory for growth) is not required; production of active cells and the conversion step can be integrated into one process, provided that PQQ and solketal addition occur at the appropriate moment; the conversion seems environmentally feasible. However, since high concentrations of solketal inhibit respiration via QH-EDH, further investigations on the mechanism of inhibition and the stability of the enzyme might be rewarding as it could lead to application of higher substrate concentrations with consequently lower down-stream processing costs.

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Author notes

  1. E. J. T. M. Leenen

    Present address: Department of Food Science, Food and Bioprocess Engineering Group, Agricultural University Wageningen, P.O. Box 8129, 6700 EV, Wageningen, The Netherlands

Authors and Affiliations

  1. Department of Microbiology and Enzymology, Delft University of Technology, Julianalaan 67, 2628 BC, Delft, The Netherlands

    A. Geerlof, J. Stoorvogel, J. A. Jongejan & J. A. Duine

  2. Bioorganic Chemistry Section, DSM Research, P.O. Box 18, 6160 MD, Geleen, The Netherlands

    E. J. T. M. Leenen, T. J. G. M. van Dooren & W. J. J. van den Tweel

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  1. A. Geerlof
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  2. J. Stoorvogel
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  3. J. A. Jongejan
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  4. E. J. T. M. Leenen
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  5. T. J. G. M. van Dooren
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  6. W. J. J. van den Tweel
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  7. J. A. Duine
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Geerlof, A., Stoorvogel, J., Jongejan, J.A. et al. Studies on the production of (S)-(+)-solketal (2,2-dimethyl-1,3-dioxolane-4-methanol) by enantioselective oxidation of racemic solketal with Comamonas testosteroni . Appl Microbiol Biotechnol 42, 8–15 (1994). https://doi.org/10.1007/BF00170216

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  • DOI: https://doi.org/10.1007/BF00170216

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