Web of Science: 12 cites, Scopus: 0 cites, Google Scholar: cites,
An immobilized and highly stabilized self-sufficientmonooxygenase as biocatalyst for oxidative biotransformations
Valencia, Daniela (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Guillén Montalbán, Marina (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Fürst, Maximilian JLJ (Rijksuniversiteit Groningen. Molecular Enzymology Group)
López Santín, Josep (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Álvaro Campos, Gregorio (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)

Data: 2018
Resum: Background: the requirement for expensive cofactors that must be efficiently recycled is one of the major factors hindering the wide implementation of industrial biocatalytic oxidation processes. In this research, a sustainable approach based on immobilized self-sufficient Baeyer-Villiger monooxygenases is discussed. - Results: a bifunctional biocatalyst composed of an NADPH-dependent cyclohexanone monooxygenase (CHMO) fused to an NADP+-accepting phosphite dehydrogenase (PTDH) catalyzes ϵ-caprolactone synthesis from cyclohexanone, using phosphite as a cheap sacrificial substrate for cofactor regeneration. Several immobilized derivatives of the fused enzyme have been prepared with high immobilization yield (97%); the one obtained by affinity adsorption on Co-IDA (Co: cobalt chelated; IDA: iminodiacetic acid) support has shown to be highly stable affording average yields of 80% after 18 reaction cycles. - Conclusions -the immobilized self-sufficient monooxygenase has demonstrated to be able to perform Baeyer-Villiger oxidation with efficient cofactor recovery and biocatalyst recycling. The proposed biocatalytic process offers access to valuable molecules with high atom economy and limited waste generation.
Ajuts: European Commission 635734
Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-452
Nota: Authors also thank COST Action CM 1303-Systems Biocatalysis for financial support and the Servei d'Anàlisi Química of UAB for their assistance on mass spectrometry analyses. Daniela Valencia acknowledges UAB for funding her PhD grant.
Drets: Tots els drets reservats.
Llengua: Anglès
Document: Article ; recerca ; Versió sotmesa a revisió
Matèria: Cyclohexanone monooxygenase (CHMO) ; Phosphite dehydrogenase (PTDH) ; Multi-enzymatic reactions ; Biocatalyst immobilization ; Biocatalyst reutilization ; Cofactor recycling
Publicat a: Journal of chemical technology and biotechnology, Vol, 93, issue 4 (April 2018) , p. 985-993, ISSN 1097-4660

DOI: 10.1002/jctb.5450


Preprint
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Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Enginyeries > Grup de Recerca en Compostatge (GICOM)
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2018-10-01, darrera modificació el 2021-09-05



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