Förster Resonance Energy Transfer Study of the Improved Biocatalytic Conversion of CO2 to Formaldehyde by Coimmobilization of Enzymes in Siliceous Mesostructured Cellular Foams
Journal article, 2018

By combining two enzymes, formate dehydrogenase (FateDH) and formaldehyde dehydrogenase (FaldDH), it is possible to drive the thermodynamically unfavorable conversion of CO2to formaldehyde. For this purpose, the enzymes were coimmobilized in siliceous mesostructured cellular foams (MCFs). A high degree of adsorption of both enzymes was achieved by coimmobilizing the enzymes sequentially, i.e., first FateDH and then FaldDH. The highest conversion rate was obtained with an enzyme mass ratio of 1:15 (FateDH/FaldDH). Using MCF functionalized with mercaptopropyl groups (MCF-MP), the activity increased ∼4 times compared to the enzymes free in solution. To probe the distance between the two enzymes, they were separately labeled with either Cy3 or Cy5 dyes and studied with Förster resonance energy transfer (FRET). An increased energy transfer was observed when the enzymes were coimmobilized in MCF-MP, suggesting that the two enzymes are in close proximity, resulting in higher conversion of CO2to formaldehyde.

Author

Pegah Sadat Nabavi Zadeh

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Physical Chemistry

Milene Zezzi Do Valle Gomes

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Applied Surface Chemistry

Björn Åkerman

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry

Anders Palmqvist

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry

ACS Catalysis

2155-5435 (eISSN)

Vol. 8 8 7251-7260

Subject Categories

Biochemistry and Molecular Biology

Analytical Chemistry

Structural Biology

DOI

10.1021/acscatal.8b01806

More information

Latest update

8/20/2018