Web of Science: 3 cites, Scopus: 5 cites, Google Scholar: cites
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
Drets: Tots els drets reservats.
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

32 p, 923.8 KB

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 Registre creat el 2019-11-06, darrera modificació el 2022-02-01

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