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Biocatalytic Routes to Lactone Monomers for Polymer Production

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)1997-2008
Number of pages12
JournalBiochemistry
Volume57
Issue number13
Early online date13 Mar 2018
DOIs
DateAccepted/In press - 13 Mar 2018
DateE-pub ahead of print - 13 Mar 2018
DatePublished (current) - 3 Apr 2018

Abstract

Monoterpenoids offer potential as bio-derived monomer feedstocks for high performance renewable polymers. We describe a biocatalytic route to lactone monomers menthide and dihydrocarvide employing Baeyer-Villiger monooxygenases (BVMOs) from Pseudomonas sp. HI-70 (CPDMO) and Rhodococcus sp. Phi1 (CHMOPhi1) as an alternative to organic synthesis. The regio-selectivity of dihydrocarvide isomer formation was controlled by site-directed mutagenesis of three key active site residues in CHMOPhi1. A combination of crystal structure determination, molecular dynamics simulations and mechanistic modeling using density functional theory (DFT) on a range of models provides insight into the origins of discrimination of wild type (WT) and a variant CHMOPhi1 for producing different regio-isomers of the lactone product. Ring-opening polymerizations of the resultant lactones using mild metal-organic catalysts demonstrate their utility in polymer production. This semi-synthetic approach utilizing a biocatalytic step, non-petroleum feedstocks and mild polymerization catalysts, allows access to known and also to previously unreported and potentially novel lactone monomers and polymers.

    Research areas

  • Baeyer-Villiger monooxygenases (BVMOs), biocatalysis, crystallography, molecular dynamics simulations, DFT mechanistic study, biopolymers, ring-opening polymerization

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS at https://pubs.acs.org/doi/10.1021/acs.biochem.8b00169 . Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 2.44 MB, PDF document

  • Supporting information PDF

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS at https://pubs.acs.org/doi/10.1021/acs.biochem.8b00169 . Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 3.63 MB, PDF document

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