Improved pinene production in a recombinant yeast by fusion linker optimization and chaperon coexpression

Pinene is an active natural monoterpene from plants and has important applications in flavorings, fragrances,and pesticides. Especially, pinene dimers are regarded as renewable fuels with high density. However, the microbial production was limited by low activity synthase. In this study, synthase improved fusion linker optimization chaperon coexpression. To construct pathway Saccharomyces cerevisiae, YPL062W gene deleted to increase MVA precursor acetyl-CoA. Truncated 3-hydroxyl-3-methylglutaryl-CoA reductase (tHMG1), isopentenyl-diphosphate isomerase (IDI1), farnesyl diphosphate mutant (ERG20F96W−N127W) were then integrated improve GPP pool. tPt1 expressed constructed engineered yeast, titer of reached 0.166 mg/L. direct pinene, ERG20ww fused different linkers orders accessibility GPP. 9.94 mg/L these proteins order a flexible (G)8. After that, several chaperons coexpressed Sil1p 10.2 yield 1.63 mg/L·OD600. The results presented here provide novel information on protein production.