Role of beta-oxidation enzymes in gamma-decalactone production by the yeast Yarrowia lipolytica. - École Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation ENSBANA Accéder directement au contenu
Article Dans Une Revue Applied and Environmental Microbiology Année : 2001

Role of beta-oxidation enzymes in gamma-decalactone production by the yeast Yarrowia lipolytica.

Résumé

Some microorganisms can transform methyl ricinoleate into gamma-decalactone, a valuable aroma compound, but yields of the bioconversion are low due to (i) incomplete conversion of ricinoleate (C(18)) to the C(10) precursor of gamma-decalactone, (ii) accumulation of other lactones (3-hydroxy-gamma-decalactone and 2- and 3-decen-4-olide), and (iii) gamma-decalactone reconsumption. We evaluated acyl coenzyme A (acyl-CoA) oxidase activity (encoded by the POX1 through POX5 genes) in Yarrowia lipolytica in lactone accumulation and gamma-decalactone reconsumption in POX mutants. Mutants with no acyl-CoA oxidase activity could not reconsume gamma-decalactone, and mutants with a disruption of pox3, which encodes the short-chain acyl-CoA oxidase, reconsumed it more slowly. 3-Hydroxy-gamma-decalactone accumulation during transformation of methyl ricinoleate suggests that, in wild-type strains, beta-oxidation is controlled by 3-hydroxyacyl-CoA dehydrogenase. In mutants with low acyl-CoA oxidase activity, however, the acyl-CoA oxidase controls the beta-oxidation flux. We also identified mutant strains that produced 26 times more gamma-decalactone than the wild-type parents.

Dates et versions

hal-00368231 , version 1 (15-03-2009)

Identifiants

Citer

Yves Waché, M. Aguedo, A. Choquet, I. L. Gatfield, J. M. Nicaud, et al.. Role of beta-oxidation enzymes in gamma-decalactone production by the yeast Yarrowia lipolytica.. Applied and Environmental Microbiology, 2001, 67 (12), pp.5700-4. ⟨10.1128/AEM.67.12.5700-5704.2001⟩. ⟨hal-00368231⟩
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