Skip to main content
PMC home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1979 Jul;38(1):135–142. doi: 10.1128/aem.38.1.135-142.1979

Microbial Oxidation of Gaseous Hydrocarbons: Production of Methyl Ketones from Their Corresponding Secondary Alcohols by Methane- and Methanol-Grown Microbes

Ching T Hou 1, Ramesh Patel 1, Allen I Laskin 1, Nancy Barnabe 1, Irene Marczak 1
PMCID: PMC243447  PMID: 39503

Abstract

Cultures of methane- or methanol-utilizing microbes, including obligate (both types I and II) and facultative methylotrophic bacteria, obligate methanol utilizers, and methanol-grown yeasts were isolated from lake water of Warinanco Park, Linden, N.J., and lake and soil samples of Bayway Refinery, Linden, N.J. Resting-cell suspensions of these, and of other known C1-utilizing microbes, oxidized secondary alcohols to their corresponding methyl ketones. The product methyl ketones accumulated extracellularly. Succinate-grown cells of facultative methylotrophs did not oxidize secondary alcohols. Among the secondary alcohols, 2-butanol was oxidized at the highest rate. The optimal conditions for in vivo methyl ketone formation were compared among five different types of C1-utilizing microbes. Some enzymatic degradation of 2-butanone was observed. The product, 2-butanone, did not inhibit the oxidation of 2-butanol. The rate of the 2-butanone production was linear for the first 4 h of incubation for all five cultures tested. A yeast culture had the highest production rate. The optimum temperature for the production of 2-butanone was 35°C for all the bacteria tested. The yeast culture had a higher temperature optimum (40°C), and there was a reasonably high 2-butanone production rate even at 45°C. Metal-chelating agents inhibit the production of 2-butanone, suggesting the involvement of metal(s) in the oxidation of secondary alcohols. Secondary alcohol dehydrogenase activity was found in the cell-free soluble extract of sonically disrupted cells. The cell-free system requires a cofactor, specifically nicotinamide adenine dinucleotide, for its activity. This is the first report of a nicotinamide adenine dinucleotide-dependent, secondary alcohol-specific enzyme.

Full text

PDF
135

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anthony C., Zatman L. J. The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27. Biochem J. 1967 Sep;104(3):953–959. doi: 10.1042/bj1040953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bellion E., Wu G. T. Alcohol dehydrogenases from a facultative methylotrophic bacterium. J Bacteriol. 1978 Jul;135(1):251–258. doi: 10.1128/jb.135.1.251-258.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Colby J., Stirling D. I., Dalton H. The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds. Biochem J. 1977 Aug 1;165(2):395–402. doi: 10.1042/bj1650395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Foster J. W., Davis R. H. A methane-dependent coccus, with notes on classification and nomenclature of obligate, methane-utilizing bacteria. J Bacteriol. 1966 May;91(5):1924–1931. doi: 10.1128/jb.91.5.1924-1931.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hou C. T., Patel R. N., Laskin A. I., Barnabe N., Marczak I. Identification and purification of a nicotinamide adenine dinucleotide-dependent secondary alcohol dehydrogenase from C1-utilizing microbes. FEBS Lett. 1979 May 1;101(1):179–183. doi: 10.1016/0014-5793(79)81321-6. [DOI] [PubMed] [Google Scholar]
  6. LEADBETTER E. R., FOSTER J. W. Bacterial oxidation of gaseous alkanes. Arch Mikrobiol. 1960;35:92–104. doi: 10.1007/BF00425597. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. LUKINS H. B., FOSTER J. W. METHYL KETONE METABOLISM IN HYDROCARBON-UTILIZING MYCOBACTERIA. J Bacteriol. 1963 May;85:1074–1087. doi: 10.1128/jb.85.5.1074-1087.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Mehta R. J. Pyridine nucleotide-linked oxidation of methanol in methanol-assimilating yeasts. J Bacteriol. 1975 Dec;124(3):1165–1167. doi: 10.1128/jb.124.3.1165-1167.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Niehaus W. G., Jr, Frielle T., Kingsley E. A., Jr Purification and characterization of a secondary alcohol dehydrogenase from a pseudomonad. J Bacteriol. 1978 Apr;134(1):177–183. doi: 10.1128/jb.134.1.177-183.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Patel R. N., Felix A. Microbial oxidation of methane and methanol: crystallization and properties of methanol dehydrogenase from Methylosinus sporium. J Bacteriol. 1976 Oct;128(1):413–424. doi: 10.1128/jb.128.1.413-424.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Patel R. N., Hou C. T., Felix A. Microbial oxidation of methane and methanol: crystallization of methanol dehydrogenase and properties of holo- and apomethanol dehydrogenase from Methylomonas methanica. J Bacteriol. 1978 Feb;133(2):641–649. doi: 10.1128/jb.133.2.641-649.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Whittenbury R., Phillips K. C., Wilkinson J. F. Enrichment, isolation and some properties of methane-utilizing bacteria. J Gen Microbiol. 1970 May;61(2):205–218. doi: 10.1099/00221287-61-2-205. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES