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- W2953644563 endingPage "e6971" @default.
- W2953644563 startingPage "e6971" @default.
- W2953644563 abstract "Medium chain esters produced from fruits and flowering plants have a number of commercial applications including use as flavour and fragrance ingredients, biofuels, and in pharmaceutical formulations. These esters are typically made via the activity of an alcohol acyl transferase (AAT) enzyme which catalyses the condensation of an alcohol and an acyl-CoA. Developing a microbial platform for medium chain ester production using AAT activity presents several obstacles, including the low product specificity of these enzymes for the desired ester and/or low endogenous substrate availability. In this study, we engineered Escherichia coli for the production of butyl octanoate from endogenously produced octanoyl-CoA. This was achieved through rational protein engineering of an AAT enzyme from Actinidia chinensis for improved octanoyl-CoA substrate specificity and metabolic engineering of E. coli fatty acid metabolism for increased endogenous octanoyl-CoA availability. This resulted in accumulation of 3.3 + 0.1 mg/L butyl octanoate as the sole product from E. coli after 48 h. This study represents a preliminary examination of the feasibility of developing E. coli platforms for the synthesis single medium chain esters from endogenous fatty acids." @default.
- W2953644563 created "2019-07-12" @default.
- W2953644563 creator A5017939794 @default.
- W2953644563 creator A5031776148 @default.
- W2953644563 creator A5063837071 @default.
- W2953644563 date "2019-07-01" @default.
- W2953644563 modified "2023-10-16" @default.
- W2953644563 title "Engineering<i>Escherichia coli</i>for the production of butyl octanoate from endogenous octanoyl-CoA" @default.
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