Effect of confinement of horse heart cytochrome c and formate dehydrogenase from Candida boidinii on mesoporous carbons on their catalytic activity

• 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. 

Ämnesord

TEKNIK OCH TEKNOLOGIER  -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)

ENGINEERING AND TECHNOLOGY  -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)

NATURVETENSKAP  -- Kemi -- Analytisk kemi (hsv//swe)

NATURAL SCIENCES  -- Chemical Sciences -- Analytical Chemistry (hsv//eng)

NATURVETENSKAP  -- Kemi -- Materialkemi (hsv//swe)

NATURAL SCIENCES  -- Chemical Sciences -- Materials Chemistry (hsv//eng)

Nyckelord

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

Publikations- och innehållstyp

ref (ämneskategori)

art (ämneskategori)