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Optimization of methanol biosynthesis from methane using Methylosinus trichosporium OB3b

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Abstract

Methylosinus trichosporium OB3b oxidized methane to methanol in the presence of a high concentration of Cu2+. Further oxidation of methanol to formaldehyde was prevented by adding 200 mm NaCl which acted as a methanol dehydrogenase H inhibitor. The bacterium, 0.6 mg dry cell ml−1, in methane/air (1:4, v/v) at 25 °C in 12.9 mm phosphate buffer (pH 7) containing 20 mm sodium formate and 200 mm NaCl accumulated 7.7 mm methanol over 36 h.

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References

  • Anthony C (1986) Bacterial oxidation of methane and methanol. Adv. Microb. Physiol. 27: 113–210.

    Google Scholar 

  • Burrows KJ, Cornish A, Scott D, Higgins IJ (1984) Substrate specificities of the soluble and particulate methane monooxygenases of Methylosinus trichosporium OB3b. J. Gen. Microbiol. 130: 3327–3333.

    Google Scholar 

  • Carver MA, Humphrey KM, Patchett RA, Jones CW (1984) The effect of EDTA and related chelating agents on the oxidation of methanol by the methylotrophic bacterium, Methylophilus methylotrophus. Eur. J. Biochem. 138: 611–615.

    Google Scholar 

  • Cox JM, Day DJ, Anthony C (1992) The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria. Biochim. Biophys. Acta 1119: 97–106.

    Google Scholar 

  • Fox BG, Froland WA, Jollie DR, Lipscomb JD (1990) Methane monooxygenase from Methylosinus trichosporium OB3b. Meth. Enzymol. 188: 191–202.

    Google Scholar 

  • Frank JJr, van Krimpen SH, Verwiel PE, Jongejan JA, Mulder AC, Duine JA (1989) On the mechanism of inhibition of methanol dehydrogenase by cyclopropane-derived inhibitors. Eur. J. Biochem. 184: 187–195.

    Google Scholar 

  • Furuto T, Takeguchi M, Okura I (1999) Semicontinuous methanol biosynthesis by Methylosinus trichosporium OB3b. J. Mol. Catal. 144: 257–261.

    Google Scholar 

  • Murrell JC, McDonald IR, Gilbert B (2000) Regulation of expression of methane monooxygenases by copper ions. Trends Microbiol. 8: 221–225.

    Google Scholar 

  • Nielsen AK, Gerdes K, Murrell JC (1997) Copper-dependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium. Mol. Microbiol. 25: 399–409.

    Google Scholar 

  • Shimoda M, Okura I (1991) Selective inhibition of methanol dehydrogenase from Methylosinus trichosporium (OB3b) by cyclopropanol. J. Mol. Catal. 64: L23–L25.

    Google Scholar 

  • Takeguchi M, Okura I (2000) Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b. Catal. Surv. Jpn. 4: 51–13.

    Google Scholar 

  • Takeguchi M, Furuto T, Sugimori D, Okura I (1997) Optimization of methanol biosynthesis by Methylosinus trichosporium OB3b: an approach to improve methanol accumulation. Appl. Biochem. Biotechnol. 68: 143–152.

    Google Scholar 

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Lee, S.G., Goo, J.H., Kim, H.G. et al. Optimization of methanol biosynthesis from methane using Methylosinus trichosporium OB3b. Biotechnology Letters 26, 947–950 (2004). https://doi.org/10.1023/B:bile.0000025908.19252.63

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  • DOI: https://doi.org/10.1023/B:bile.0000025908.19252.63

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