Home > Articles > Published articles > Trimethyl-e-caprolactone synthesis with a novel immobilized glucose dehydrogenase and an immobilized thermostable cyclohexanone monooxygenase |
Additional title: | Synthesis of trimethyl-ε-caprolactone with a novel immobilized Glucose dehydrogenase and an immobilized thermostable Cyclohexanone monooxygenase |
Date: | 2019 |
Abstract: | 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. |
Grants: | European Commission 635734 Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-1462 |
Rights: | Tots els drets reservats. |
Language: | Anglès |
Document: | Article ; recerca ; Versió sotmesa a revisió |
Subject: | Trimethyl-ε-caprolactone ; Baeyer-Villiger monooxygenase ; Cofactor regeneration ; Re-cycling ; Immobilized enzymes ; Biocatalyst yield |
Published in: | Applied catalysis. A, General, Vol. 585 (September 2019) , art. 117187, ISSN 0926-860X |
Preprint 32 p, 923.8 KB |