Engineering of Transmembrane Alkane Monooxygenases to Improve a Key Reaction Step in the Synthesis of Polymer Precursor Tulipalin A

Andrea Nigl, Veronica Delsoglio, Marina Grgić, Lenny Malihan-Yap, Kamela Myrtollari, Jelena Spasic, Margit Winkler, Gustav Oberdorfer, Andreas Taden, Iva Anić, Robert Kourist

Research output: Working paperPreprint

Abstract

The α-methylene-γ-butyrolactone tulipalin A, naturally found in tulips can polymerize via addition at the vinyl group or via ring-opening polymerization, making it a highly promising monomer for biobased polymers. As tulipalin A biosynthesis in plants remains elusive, we propose a pathway for its synthesis starting from the metabolic intermediate isoprenol. For this, terminal hydroxylation of the α-methylene substrate isoprenyl acetate is a decisive step. While a panel of fungal unspecific peroxygenases showed a preference for the undesired epoxidation of the exo-olefin group, bacterial alkane monooxygenases were specific for terminal hydroxylation. A combination of protein engineering based on de novo structure prediction of the membrane enzymes with cell engineering allowed to increase the specific activity by 6-fold to 1.83 U gcdw -1, unlocking this reaction for the fermentative production of tulipalin A from renewable resources
Original languageEnglish
PublisherbioRxiv
DOIs
Publication statusPublished - 8 Jul 2024

Fields of Expertise

  • Human- & Biotechnology

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