Summary
Recent advances in the development of both experimental and computational protein engineering tools have enabled a number of further successes in the development of biocatalysts ready for large-scale applications.The production of monomers from cheap, readily available components (e.g. terpenoids) for sustainable biopolymer synthesis is a growing area of interest. Biomaterials composed of lactone monomers have been used to produce polyurethanes.The present research proposal is focused on the deep understanding of catalysis by newly identified BVMO enzymes, realized through detailed structural and functional analysis of enzyme mechanisms and substrate/coenzyme recognition. This project will involve multidisciplinary training, with clear objectives in the technical areas of synthetic biology, proteomics, structural biology and biophysical chemistry. This project will allow me to work on structure/function relationship of proteins and to extend my knowledge in metabolic pathway engineering especially in understanding of monooxygenases.The objective will be to identify new Baeyer Villiger monooxygenases biocatalysts that have the appropriate biocatalytic and stability characteristics to enable lactone monomer synthesis. The methods would generate novel structural and biocatalytic data to provide a comprehensive toolkit of flavin-dependent BayerVilliger monooxygenases that are suitable for exploitation in lactone monomer synthesis. These new biocatalysts will be used to construct new strains of E. coli that are capable of producing the target lactone monomers in high yield. The immediate outcomes will be new structural information (native and variant forms of the enzymes); new biocatalytic parameters (reactivity profiles with target substrates; stereoselectivity; conversion; stability; coenzyme specificities) and new lactone producing strains generated from existing monoterpene producing E. coli strains.
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More information & hyperlinks
| Web resources: | https://cordis.europa.eu/project/id/834816 |
| Start date: | 15-07-2019 |
| End date: | 09-10-2021 |
| Total budget - Public funding: | 224 933,76 Euro - 224 933,00 Euro |
Cordis data
Original description
Recent advances in the development of both experimental and computational protein engineering tools have enabled a number of further successes in the development of biocatalysts ready for large-scale applications.The production of monomers from cheap, readily available components (e.g. terpenoids) for sustainable biopolymer synthesis is a growing area of interest. Biomaterials composed of lactone monomers have been used to produce polyurethanes.The present research proposal is focused on the deep understanding of catalysis by newly identified BVMO enzymes, realized through detailed structural and functional analysis of enzyme mechanisms and substrate/coenzyme recognition. This project will involve multidisciplinary training, with clear objectives in the technical areas of synthetic biology, proteomics, structural biology and biophysical chemistry. This project will allow me to work on structure/function relationship of proteins and to extend my knowledge in metabolic pathway engineering especially in understanding of monooxygenases.The objective will be to identify new Baeyer Villiger monooxygenases biocatalysts that have the appropriate biocatalytic and stability characteristics to enable lactone monomer synthesis. The methods would generate novel structural and biocatalytic data to provide a comprehensive toolkit of flavin-dependent BayerVilliger monooxygenases that are suitable for exploitation in lactone monomer synthesis. These new biocatalysts will be used to construct new strains of E. coli that are capable of producing the target lactone monomers in high yield. The immediate outcomes will be new structural information (native and variant forms of the enzymes); new biocatalytic parameters (reactivity profiles with target substrates; stereoselectivity; conversion; stability; coenzyme specificities) and new lactone producing strains generated from existing monoterpene producing E. coli strains.Status
TERMINATEDCall topic
MSCA-IF-2018Update Date
28-04-2024
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