Abstract
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.
Highlights
Hydratases or hydrolyases (EC 4.2.1) are enzymes that catalyse the addition of water to C=C double bonds
All these reviews offer a comprehensive overview of the published literature and important biotechnological potential of fatty acid hydratases, these articles are superseded by new recent developments as new enzymes and structures have changed our understanding of the mechanism and opened new directions for biotechnological applications
Enzymes for which only conversions and data on cell extracts or whole cells were reported have been excluded. a An attempt was made to use a consistent short name to designate the different enzymes, which is not always identical to the short name used in the literature, b L. acidophilus Ohy1 has a strong preference for linoleic acid over oleic acid, c preparation of oleic acid stock: 4 mM in 4% (v/v) ethanol, homogenised at 10000 rpm for 10 s
Summary
Hydratases or hydrolyases (EC 4.2.1) are enzymes that catalyse the addition of water to C=C double bonds. Löwe and Gröger published a mini-review on the applications of fatty acid hydratases in organic synthesis, highlighting the possibility to produce industrially relevant chemical building blocks from renewable resources (Löwe and Gröger 2020). All these reviews offer a comprehensive overview of the published literature and important biotechnological potential of fatty acid hydratases, these articles are superseded by new recent developments as new enzymes and structures have changed our understanding of the mechanism and opened new directions for biotechnological applications. That oleate hydratases have a wider substrate scope, overlapping with other fatty acid hydratases
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