Biodegradation of methyl tert-Butyl ether and other fuel oxygenates by a new strain, Mycobacterium austroafricanum IFP 2012

Francois, A; Mathis, H; Godefroy, D; Piveteau, P; Fayolle, F; Monot, F

HERO ID

52680

Reference Type

Journal Article

Year

2002

Language

English

PMID

12039730

HERO ID 52680
In Press No
Year 2002
Title Biodegradation of methyl tert-Butyl ether and other fuel oxygenates by a new strain, Mycobacterium austroafricanum IFP 2012
Authors Francois, A; Mathis, H; Godefroy, D; Piveteau, P; Fayolle, F; Monot, F
Journal Applied and Environmental Microbiology
Volume 68
Issue 6
Page Numbers 2754-2762
Abstract 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.
Doi 10.1128/AEM.68.6.2754-2762.2002
Pmid 12039730
Wosid WOS:000176030100018
Url http://aem.asm.org/cgi/doi/10.1128/AEM.68.6.2754-2762.2002
Is Certified Translation No
Dupe Override No
Comments ECRIB. c in Francois is "þ"; Mycobacterium austroafricanum and tert are italicized.
Is Public Yes
Language Text English
Is Qa No