Involvement of acyl coenzyme A oxidase isozymes in biotransformation of methyl ricinoleate into gamma-decalactone by Yarrowia lipolytica
Wache, Y. | Laroche, C. | Bergmark, K. | Moller-Andersen, C. | Aguedo, M. | Le Dall, M.T. | Wang, H. | Nicaud, J.M. | Belin, J.M.
We reported previously on the function of acyl coenzyme A (acyl-CoA) oxidase isozymes in the yeast Yarrowia lipolytica by investigating strains disrupted in one or several acyl-CoA oxidase-encoding genes (POX1 through POX5) (H. Wang et al., J. Bacteriol. 181:5140-5148, 1999). Here, these mutants were studied for lactone production. Monodisrupted strains produced similar levels of lactone as the wild-type strain (50 mg/liter) except for deltapox3, which produced 220 mg of gamma-decalactone per liter after 24 h. The deltapox2 deltapox3 double-disrupted strain, although slightly affected in growth, produced about 150 mg of lactone per liter, indicating that Aox2p was not essential for the biotransformation. The deltapox2 deltapox3 deltapox5 triple-disrupted strain produced and consumed lactone very slowly. On the contrary, the deltapox2 deltapox3 deltapox4 deltapox5 multidisrupted strain did not grow or biotransform methyl ricinoleate into gamma-decalactone, demonstrating that Aox4p is essential for the biotransformation.
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