Effect of confinement of horse heart cytochrome c and formate dehydrogenase from Candida boidinii on mesoporous carbons on their catalytic activityShow others and affiliations
2021 (English)In: Bioprocess and biosystems engineering (Print), ISSN 1615-7591, E-ISSN 1615-7605, Vol. 44, no 8, p. 1699-1710Article in journal (Refereed) Published
Abstract [en]
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.
Place, publisher, year, edition, pages
Springer Science and Business Media Deutschland GmbH , 2021. Vol. 44, no 8, p. 1699-1710
Keywords [en]
Carbon dioxide, Cytochrome c, Formate dehydrogenase hydrogen peroxide, Mesoporous carbon, Protein nanoconfinement, Candida, Carbon, Electron transport properties, Formic acid, Hydrogen peroxide, Pore size, Proteins, Reduction, Yeast, Direct electron transfer, Electro-activity, Electrochemical behaviour, Formate dehydrogenase, Nicotinamide adenine dinucleotides, Peroxidase activities, Protein conformational changes, Catalyst activity, heart enzyme, reduced nicotinamide adenine dinucleotide, nicotinamide adenine dinucleotide, biocatalyst, Candida boidinii, chronoamperometry, conformational transition, controlled study, cyclic voltammetry, electrochemical analysis, electron transport, enzyme activity, enzyme immobilization, horse, nonhuman, pH, pore size distribution, porosity, protein conformation, reduction (chemistry), surface area, synthesis, ultraviolet visible spectrophotometry, adsorption, animal, budding yeast, chemistry, electrochemistry, electrode, enzymology, kinetics, metabolism, statistical model, time factor, Animals, Cytochromes c, Electrodes, Formate Dehydrogenases, Formates, Horses, Hydrogen-Ion Concentration, Linear Models, NAD, Saccharomycetales, Time Factors
National Category
Biocatalysis and Enzyme Technology Analytical Chemistry Materials Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-308505DOI: 10.1007/s00449-021-02553-3ISI: 000636405300001PubMedID: 33813652Scopus ID: 2-s2.0-85103630956OAI: oai:DiVA.org:kth-308505DiVA, id: diva2:1637449
Note
QC 20220214
2022-02-142022-02-142024-03-18Bibliographically approved