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Applied and Environmental Microbiology, June 2002, p. 2754-2762, Vol. 68, No. 6
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.6.2754-2762.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Biodegradation of Methyl tert-Butyl Ether and Other Fuel Oxygenates by a New Strain, Mycobacterium austroafricanum IFP 2012

Alan François, Hugues Mathis, Davy Godefroy, Pascal Piveteau, Françoise Fayolle,* and Frédéric Monot

Institut Français du Pétrole, Département de Microbiologie, 92852 Rueil-Malmaison Cedex, France

Received 26 December 2001/ Accepted 13 March 2002

A strain that efficiently degraded methyl tert-butyl ether (MTBE) was obtained by initial selection on the recalcitrant compound tert-butyl alcohol (TBA). This strain, a gram-positive methylotrophic bacterium identified as Mycobacterium austroafricanum IFP 2012, was also able to degrade tert-amyl methyl ether and tert-amyl alcohol. Ethyl tert-butyl ether was weakly degraded. tert-Butyl formate and 2-hydroxy isobutyrate (HIBA), two intermediates in the MTBE catabolism pathway, were detected during growth on MTBE. A positive effect of Co2+ during growth of M. austroafricanum IFP 2012 on HIBA was demonstrated. The specific rate of MTBE degradation was 0.6 mmol/h/g (dry weight) of cells, and the biomass yield on MTBE was 0.44 g (dry weight) per g of MTBE. MTBE, TBA, and HIBA degradation activities were induced by MTBE and TBA, and TBA was a good inducer. Involvement of at least one monooxygenase during degradation of MTBE and TBA was shown by (i) the requirement for oxygen, (ii) the production of propylene epoxide from propylene by MTBE- or TBA- grown cells, and (iii) the inhibition of MTBE or TBA degradation and of propylene epoxide production by acetylene. No cytochrome P-450 was detected in MTBE- or TBA-grown cells. Similar protein profiles were obtained after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of crude extracts from MTBE- and TBA-grown cells. Among the polypeptides induced by these substrates, two polypeptides (66 and 27 kDa) exhibited strong similarities with known oxidoreductases.

* Corresponding author. Mailing address: Institut Français du Pétrole, Département de Microbiologie, 1 & 4 avenue de Bois-Préau, 92852 Rueil-Malmaison Cedex, France. Phone: (33) 1-47-52-68-64. Fax: (33) 1-47-52-70-01. E-mail: francoise.fayolle{at}ifp.fr.

Applied and Environmental Microbiology, June 2002, p. 2754-2762, Vol. 68, No. 6
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.6.2754-2762.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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