Bioprocess and biosystems engineering, 2021-08, Vol.44 (8), p.1699-1710
2021
Details
- Autor(en) / Beteiligte
- Titel
- Effect of confinement of horse heart cytochrome c and formate dehydrogenase from Candida boidinii on mesoporous carbons on their catalytic activity
- Ist Teil von
- Bioprocess and biosystems engineering, 2021-08, Vol.44 (8), p.1699-1710
- Ort / Verlag
- Berlin/Heidelberg: Springer Berlin Heidelberg
- Erscheinungsjahr
- 2021
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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 H 2 O 2 reduction was enhanced at pH 4.0, due to the protein conformational changes. For cbFDH, the reduction of CO 2 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1615-7591, 1615-7605eISSN: 1615-7605DOI: 10.1007/s00449-021-02553-3Titel-ID: cdi_swepub_primary_oai_DiVA_org_kth_308505
- Format
- –
- Schlagworte
- Adenine, Adsorption, animal, Animals, biocatalyst, Biocatalysts, Biotechnology, budding yeast, Candida, Candida boidinii, Carbon, Carbon - chemistry, Carbon dioxide, Carbon Dioxide - chemistry, Catalysis, Catalyst activity, Catalytic activity, Chemical Sciences, Chemistry, Chemistry and Materials Science, chronoamperometry, conformational transition, controlled study, cyclic voltammetry, Cytochrome, Cytochrome c, Cytochromes, Cytochromes c, Cytochromes c - metabolism, Dehydrogenase, Dehydrogenases, Direct electron transfer, Electro-activity, Electroactivity, Electrochemical analysis, Electrochemical behaviour, Electrochemistry, electrode, Electrodes, Electron transfer, Electron Transport, Electron transport properties, Environmental Engineering, Environmental Engineering/Biotechnology, Environmental Sciences, enzyme activity, enzyme immobilization, enzymology, Food Science, Formate dehydrogenase, Formate dehydrogenase hydrogen peroxide, Formate Dehydrogenases, Formate Dehydrogenases - chemistry, Formates, Formates - chemistry, Formic acid, heart enzyme, horse, Horses, Hydrogen peroxide, Hydrogen Peroxide - chemistry, Hydrogen-Ion Concentration, Immobilization, Industrial and Production Engineering, Industrial Chemistry/Chemical Engineering, Kinetics, Linear Models, Material chemistry, Mesoporous carbon, metabolism, NAD, NAD - metabolism, NADH, Nicotinamide, Nicotinamide adenine dinucleotide, Nicotinamide adenine dinucleotides, nonhuman, Peroxidase, Peroxidase activities, Pore size, Pore size distribution, Porosity, protein conformation, Protein conformational changes, Protein nanoconfinement, Proteins, reduced nicotinamide adenine dinucleotide, Reduction, reduction (chemistry), Research Paper, Saccharomycetales, Saccharomycetales - enzymology, Size distribution, statistical model, surface area, synthesis, time factor, Time Factors, ultraviolet visible spectrophotometry, Yeast