Terpenes are a large class of organic compounds, primarily produced by plants and constitute the main components of essential oils. Functionalization of the terpene carbon backbone using cytochrome P450 enzymes could derive more useful compounds that can be converted to higher value products. In this study, cytochrome P450 enzymes were investigated for oxidizing monoterpene (e.g. limonene, 1,8-cineole), a few oxidized terpenes were produced, including carveol, carvone, limonene 1,2-epoxide, 2-endo-hydroxy-1,8-cineole. Based on those oxidized terpenes, possible biosynthetic pathways were explored toward making biology-derived functionalized terpenes, such as monomer of the polymer.<br/> <br/>On the other hand, terpenes are hydrophobic and volatile compounds that limit the accessibility of P450 enzymes. To optimize the production of oxidized terpenes, we developed an enzyme fusion strategy with linking terpene synthase and P450 enzyme. In an example of producing 2-endo-hydroxy-1,8-cineole, the engineered fusion showed higher efficiency from both in vitro and in vivo production results. Thus, engineering a fusion between terpene synthase and P450 presents a feasible strategy for producing oxidized terpenes, suggesting broad application during the production of terpene-based bioproducts.<br/>

Production of oxidized terpenes using P450 enzymes and their engineered enzyme fusions

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.