Role of β-Oxidation Enzymes in γ-Decalactone Production by the Yeast Yarrowia lipolytica
作者： Yves Waché , Mario Aguedo , Armelle Choquet , Ian L. Gatfield , Jean-Marc Nicaud
DOI: 10.1128/AEM.67.12.5700-5704.2001
关键词:
摘要: 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 (C(18)) C(10) precursor (ii) accumulation other lactones (3-hydroxy-gamma-decalactone and 2- 3-decen-4-olide), (iii) gamma-decalactone reconsumption. We evaluated acyl coenzyme A (acyl-CoA) oxidase activity (encoded by POX1 through POX5 genes) in Yarrowia lipolytica lactone reconsumption POX mutants. Mutants with no acyl-CoA could not reconsume mutants disruption pox3, which encodes short-chain oxidase, reconsumed it more slowly. 3-Hydroxy-gamma-decalactone during transformation suggests that, wild-type strains, beta-oxidation is controlled 3-hydroxyacyl-CoA dehydrogenase. In activity, however, controls flux. also identified mutant strains that produced 26 times than parents.
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