Journal
BIOPROCESS AND BIOSYSTEMS ENGINEERING
Volume 44, Issue 8, Pages 1699-1710Publisher
SPRINGER
DOI: 10.1007/s00449-021-02553-3
Keywords
Mesoporous carbon; Protein nanoconfinement; Cytochrome c; Formate dehydrogenase hydrogen peroxide; Carbon dioxide
Funding
- MINICINN, Spain [CTQ2013-48280-C3-3-R, CTQ2016-76231-C2-2-R]
- European Research Council [PHOROSOL 684161]
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This study immobilized two biocatalysts on a series of mesoporous carbons with controlled pore sizes, finding that the catalytic activity of nanoconfined proteins was correlated with the pore size distribution of the carbon materials used as supports. The study also evaluated a biocatalyst's production of formic acid upon immobilization, finding higher yields compared to free solution conditions.
This study reports the immobilization of two biocatalysts (e.g., cytochrome c-Cyt c-and the non-metalloenzyme formate dehydrogenase from Candida boidinii-cbFDH) on a series of mesoporous carbons with controlled pore sizes. The catalytic activity of the nanoconfined proteins was correlated with the pore size distribution of the carbon materials used as supports. The electrochemical behaviour of nanoconfined Cyt c showed direct electron transfer electroactivity in pore sizes matching tightly the protein dimension. The pseudo-peroxidase activity towards H2O2 reduction was enhanced at pH 4.0, due to the protein conformational changes. For cbFDH, the reduction of CO2 towards formic acid was evaluated for the nanoconfined protein, in the presence of nicotinamide adenine dinucleotide (NADH). The carbons displayed different cbFDH uptake capacity, governed by the dimensions of the main mesopore cavities and their accessibility through narrow pore necks. The catalytic activity of nanoconfined cbFDH was largely improved, compared to its performance in free solution. Regardless of the carbon support used, the production of formic acid was higher upon immobilization with lower nominal cbFDH:NADH ratios.
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