Please use this identifier to cite or link to this item: http://dx.doi.org/10.18419/opus-530
Authors: Dobslaw, Daniel
Engesser, Karl-Heinrich
Title: Degradation of toluene by ortho cleavage enzymes in Burkholderia fungorum FLU100
Issue Date: 2014
metadata.ubs.publikation.typ: Zeitschriftenartikel
metadata.ubs.publikation.source: Microbial biotechnology (2014). URL http://dx.doi.org./10.1111/1751-7915.12147
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-95385
http://elib.uni-stuttgart.de/handle/11682/547
http://dx.doi.org/10.18419/opus-530
Abstract: Burkholderia fungorum FLU100 simultaneously oxidized any mixture of toluene, benzene and monohalogen benzenes to (3-substituted) catechols with a selectivity of nearly 100%. Further metabolism occurred via enzymes of ortho cleavage pathways with complete mineralization. During the transformation of 3-methylcatechol, 4-carboxymethyl-2-methylbut-2-en-4-olide (2-methyl-2-enelactone, 2-ML) accumulated transiently, being further mineralized only after a lag phase of 2 h in case of cells pre-grown on benzene or mono-halogen benzenes. No lag phase, however, occurred after growth on toluene. Cultures inhibited by chloramphenicol after growth on benzene or mono-halogen benzenes were unable to metabolize 2-ML supplied externally, even after prolonged incubation. A control culture grown with toluene did not show any lag phase and used 2-ML as a substrate. This means that 2-ML is an intermediate of toluene degradation and converted by specific enzymes. The conversion of 4-methylcatechol as a very minor by-product of toluene degradation in strain FLU100 resulted in the accumulation of 4-carboxymethyl-4-methylbut-2-en-4-olide (4-methyl-2-enelactone, 4-ML) as a dead-end product, excluding its nature as a possible intermediate. Thus, 3-methylcyclohexa-3,5-diene-1,2-diol, 3-methylcatechol, 2-methyl muconate and 2-ML were identified as central intermediates of productive ortho cleavage pathways for toluene metabolism in B. fungorum FLU100.
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