Enzymatic Synthesis of Trimethyl-ϵ-caprolactone : Process Intensification and Demonstration on a 100 L Scale
| Autor: | Jordi Solé, Martin Schürmann, Jan Brummund, Gregorio Álvaro, Gloria Caminal, Marina Guillén |
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| Přispěvatelé: | European Commission, Caminal, Glòria [0000-0001-9646-6099], Caminal, Glòria |
| Rok vydání: | 2021 |
| Předmět: |
Materials science
Baeyer−Villiger monooxygenase (BVMO) Preindustrial scale Scale (ratio) Branched lactone synthesis Biocatalyst yield 010405 organic chemistry Organic Chemistry Baeyer-Villiger monooxygenase Enzymatic synthesis 010402 general chemistry 01 natural sciences 0104 chemical sciences chemistry.chemical_compound Pilot plant chemistry Chemical engineering Scientific method Space time yield Physical and Theoretical Chemistry Scaling Caprolactone Applied biocatalysis |
| Zdroj: | Recercat. Dipósit de la Recerca de Catalunya instname Digital.CSIC. Repositorio Institucional del CSIC Recercat: Dipósit de la Recerca de Catalunya Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) Dipòsit Digital de Documents de la UAB Universitat Autònoma de Barcelona |
| Popis: | Optimization and scaling up of the Baeyer-Villiger oxidation of 3,3,5-trimethyl-cyclohexanone to trimethyl-ϵ-caprolactones (CHLs) were studied to demonstrate this technology on a 100 L pilot plant scale. The reaction was catalyzed by a cyclohexanone monooxygenase from Thermocrispum municipale that utilizes the costly redox cofactor nicotinamide adenine dinucleotide phosphate (reduced form), which was regenerated by a glucose dehydrogenase (GDH). As a first stage, different cyclohexanone monooxygenase formulations were tested: cell-free extract, whole cells, fermentation broth, and sonicated fermentation broth. Using broth resulted in the highest yield (63%) and required the least biocatalyst preparation effort. Two commercial glucose dehydrogenases (GDH-105 and GDH-01) were evaluated, resulting in similar performances. Substrate dosing rates and biocatalyst loadings were optimized. On a 30 mL scale, the best conditions were found when 30 mM h-1 dosing rate, 10% (v/v) cyclohexanone monooxygenase broth, and 0.05% (v/v) of glucose dehydrogenase (GDH-01) liquid enzyme formulation were applied. These same conditions (with oxygen instead of air) were applied on a 1 L scale with 92% conversion, achieving a specific activity of 13.3 U gcell wet weight (cww) -1, a space time yield of 3.4 gCHL L-1 h-1, and a biocatalyst yield of 0.83 gCHL gcww -1. A final 100 L demonstration was performed in a pilot plant facility. After 9 h, the reaction reached 85% conversion, 12.8 U gcww -1, a space time yield of 2.7 g L-1 h-1, and a biocatalyst yield of 0.60 gCHL gcww -1. The extraction of product resulted in 2.58 kg of isolated final product. The overall isolated CHL yield was 76% (distal lactone 47% and proximal lactone 53%). © 2019 American Chemical Society. The research in this work has received funding from the European Union project ROBOX (grant agreement no. 635734) under EU’s Horizon 2020 Programme Research and Innovation actions H2020-LEIT BIO-2014-1. This document reflects only the authors’ view and the agency is not responsible for any use that may be made of the information it contains. The Department of Chemical, Biological and Environmental Engineering of Universitat Autònoma de Barcelona constitutes the Biochemical Engineering Unit of the Reference Network in Biotechnology and the research group 2017 SGR 1462, Generalitat de Catalunya. The authors thank COST Action CM 1303: Systems Biocatalysis for financial support and Marie Delgove et al. from the University of Maastricht for providing analytical standards. J.S. also acknowledges UAB for funding his Ph.D. grant. |
| Databáze: | OpenAIRE |
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