Catabolic Pathway of Gamma-caprolactone in the Biocontrol Agent Rhodococcus erythropolis

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Barbey, Corinne | Crépin, Alexandre | Cirou, Amélie | Budin-Verneuil, Aurélie | Orange, Nicole | Feuilloley, Marc | Faure, Denis | Dessaux, Yves | Burini, Jean-François | Latour, Xavier

Edité par CCSD ; American Chemical Society -

International audience. Gamma-caprolactone (GCL) is well-known as a food flavor and has been recently described as a biostimulant molecule promoting the growth of bacteria with biocontrol activity against soft-rot pathogens. Among these biocontrol agents, Rhodococcus erythropolis, characterized by a remarkable metabolic versatility, assimilates various gamma-butyrolactone molecules with a branched-aliphatic chain, such as GCL. The assimilative pathway of GCL in R. erythropolis was investigated by two-dimensional gel electrophoresis coupled to matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) analysis. This analysis suggests the involvement of the lactonase QsdA in ring-opening, a feature confirmed by heterologous expression in Escherichia colt. According to proteome analysis, the open-chain form of GCL was degraded by beta- and omega-oxidation coupled to the Krebs cycle and beta-ketoadipate pathway. Ubiquity of qsdA gene among environmental R. elythropolis isolates was verified by PCR. In addition to a previous N-acyl homoserine lactone catabolic function, QsdA may therefore be involved in an intermediate degradative step of cyclic recalcitrant molecules or in synthesis of flavoring lactones.

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