TY - JOUR
T1 - Novel oleate hydratases and potential biotechnological applications
AU - Hagedoorn, Peter Leon
AU - Hollmann, Frank
AU - Hanefeld, Ulf
PY - 2021
Y1 - 2021
N2 - 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.
AB - 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.
KW - 10-hydroxystearic acid
KW - Biocatalysis
KW - Oleate hydratase
KW - Protein engineering
UR - http://www.scopus.com/inward/record.url?scp=85111732971&partnerID=8YFLogxK
U2 - 10.1007/s00253-021-11465-x
DO - 10.1007/s00253-021-11465-x
M3 - Review article
AN - SCOPUS:85111732971
SN - 0175-7598
VL - 105
SP - 6159
EP - 6172
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
IS - 16-17
ER -