Improved biocatalytic cascade conversion of CO2 to methanol by enzymes Co-immobilized in tailored siliceous mesostructured cellular foams
Journal article, 2021

CO2 can be enzymatically reduced to methanol in a cascade reaction involving three enzymes: formate-, formaldehyde- and alcohol dehydrogenase (FateDH, FaldDH, ADH). We report an improvement in the yield of this reaction by co-immobilizing the three dehydrogenases in siliceous mesostructured cellular foams (MCF). This material consists of large mesopores suitable for the co-immobilization of these comparatively large enzymes. To improve the interaction between the enzymes and support, the host silica material was functionalized with mercaptopropyl groups (MCF-MP). The enzymes were fluorescently labelled to independently monitor their uptake and spatial distribution into the particle. The three dehydrogenases were co-immobilized using two sequential methods. In the first one, the enzymes were immobilized according to the reaction order (FateDH -> FaldDH -> ADH) and secondly in order of increasing enzyme size (FateDH -> ADH -> FaldDH). Two protein loadings were also tested: 50 and 150 mg(enzymes) g(support)(-1). We could observe a 4.5-fold higher methanol yield in comparison to enzymes free in solution when the enzymes were immobilized in order of size and with a loading of 50 mg(enzymes) g(support)(-1). The results of this work show that by using MCF-MP, a simple method of immobilization can be applied to significantly increase the activity of the enzymes for the cascade reaction.


Milene Zezzi Do Valle Gomes

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry

Gerard Masdeu Gámez

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry

Patrick Eiring

University of Würzburg

Alexander Kuhlemann

University of Würzburg

Markus Sauer

University of Würzburg

Björn Åkerman

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry

Anders Palmqvist

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry

Catalysis Science and Technology

2044-4753 (ISSN) 2044-4761 (eISSN)

Vol. 11 21 6952-6959

Subject Categories

Analytical Chemistry

Biocatalysis and Enzyme Technology

Organic Chemistry



More information

Latest update

4/5/2022 5