Trimethyl-e-caprolactone synthesis with a novel immobilized glucose dehydrogenase and an immobilized thermostable cyclohexanone monooxygenase
Solé Ferré, Jordi (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Brummund, Jan (InnoSyn B.V.)
Caminal i Saperas, Glòria 
(Institut de Química Avançada de Catalunya)
Schürman, Martin (InnoSyn B.V.)
Álvaro, Gregorio 
(Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Guillén, Marina 
(Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Títol variant: |
Synthesis of trimethyl-ε-caprolactone with a novel immobilized Glucose dehydrogenase and an immobilized thermostable Cyclohexanone monooxygenase |
Data: |
2019 |
Resum: |
An often associated drawback with Baeyer-Villiger monooxygenases, is its poor operational stability. Furthermore, these biocatalysts frequently suffer from substrate/product inhibition. In this work, a thermostable cyclohexanone monooxygenase (TmCHMO) was immobilized and used in the synthesis of trimethyl-ε-caprolactone (CHL). As a cofactor regeneration enzyme, a novel and highly active glucose dehydrogenase (GDH-01) was used immobilized for the first time. MANA-agarose was the carrier chosen since it presented an immobilization yield of 76. 3 ± 0. 7% and a retained activity of 62. 6 ± 2. 3%, the highest metrics among the supports tested. Both immobilized enzymes were studied either separately or together in six reaction cycles (30 mL; [substrate] =132. 5 mM). A biocatalyst yield of 37. 3 g g−1 of TmCHMO and 474. 2 g g−1 of GDH-01 were obtained. These values represent a 3. 6-fold and 1. 9-fold increase respectively, compared with a model reaction where both enzymes were used in its soluble form. |
Ajuts: |
European Commission 635734 Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-1462
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Drets: |
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Llengua: |
Anglès |
Document: |
Article ; recerca ; Versió sotmesa a revisió |
Matèria: |
Trimethyl-ε-caprolactone ;
Baeyer-Villiger monooxygenase ;
Cofactor regeneration ;
Re-cycling ;
Immobilized enzymes ;
Biocatalyst yield |
Publicat a: |
Applied catalysis. A, General, Vol. 585 (September 2019) , art. 117187, ISSN 0926-860X |
DOI: 10.1016/j.apcata.2019.117187
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Registre creat el 2019-11-06, darrera modificació el 2024-11-17