| Structure Identification: |
| Applied and Environmental Microbiology, 2001, 67(12):5700-5704. | | Role of beta-oxidation enzymes in gamma-decalactone production by the yeast Yarrowia lipolytica.[Reference: WebLink] | 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.
METHODS AND RESULTS:
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.
CONCLUSIONS:
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. |
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