Novel oleate hydratases and potential biotechnological applications

Peter Leon Hagedoorn*, Frank Hollmann, Ulf Hanefeld

*Corresponding author for this work

Research output: Contribution to journalReview articleScientificpeer-review

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Oleate hydratase catalyses the addition of water to the CC double bond of oleic acid to produce (R)-10-hydroxystearic acid. The enzyme requires an FAD cofactor that functions to optimise the active site structure. A wide range of unsaturated fatty acids can be hydrated at the C10 and in some cases the C13 position. The substrate scope can be expanded using ‘decoy’ small carboxylic acids to convert small chain alkenes to secondary alcohols, albeit at low conversion rates. Systematic protein engineering and directed evolution to widen the substrate scope and increase the conversion rate is possible, supported by new high throughput screening assays that have been developed. Multi-enzyme cascades allow the formation of a wide range of products including keto-fatty acids, secondary alcohols, secondary amines and α,ω-dicarboxylic acids. Key points: • Phylogenetically distinct oleate hydratases may exhibit mechanistic differences. • Protein engineering to improve productivity and substrate scope is possible. • Multi-enzymatic cascades greatly widen the product portfolio.

Original languageEnglish
Pages (from-to)6159-6172
Number of pages14
JournalApplied Microbiology and Biotechnology
Issue number16-17
Publication statusPublished - 2021


  • 10-hydroxystearic acid
  • Biocatalysis
  • Oleate hydratase
  • Protein engineering


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