Back to Search
Start Over
Novel oleate hydratases and potential biotechnological applications
- Source :
- Applied Microbiology and Biotechnology
- Publication Year :
- 2021
- Publisher :
- Springer Science and Business Media LLC, 2021.
-
Abstract
- 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.
- Subjects :
- Double bond
Applied Microbiology and Biotechnology
Catalysis
Cofactor
chemistry.chemical_compound
Catalytic Domain
Hydro-Lyases
chemistry.chemical_classification
biology
10-hydroxystearic acid
Substrate (chemistry)
Active site
General Medicine
Protein engineering
Mini-Review
Oleate hydratase
Directed evolution
Combinatorial chemistry
Oleic acid
chemistry
Fatty Acids, Unsaturated
Biocatalysis
biology.protein
Oleic Acid
Biotechnology
Subjects
Details
- ISSN :
- 14320614 and 01757598
- Volume :
- 105
- Database :
- OpenAIRE
- Journal :
- Applied Microbiology and Biotechnology
- Accession number :
- edsair.doi.dedup.....23c27e1ab02b639d32aa5e7b9473c945