The effect of magnetized water on the oxidation reaction of phenol derivatives and aromatic amines by horseradish peroxidase enzyme

The present study aimed to investigate, for the first time, the rate of the oxidation reaction of some derivatives of phenol and aromatic amines, that is, pyrogallol, catechol, resorcinol, ortho‐aminophenol, meta‐aminophenol, para‐aminophenol, ortho‐phenylenediamine, and para‐phenylenediamine, in th...

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Bibliographic Details
Published in:Biotechnology progress 2020-11, Vol.36 (6), p.e3035-n/a
Main Authors: Emamdadi, Narjes, Gholizadeh, Mostafa, Housaindokht, Mohammad Reza
Format: Article
Language:English
Subjects:
Amines
Aminophenol
Bonding strength
Catechol
Derivatives
Enzymes
Fluorescence
Fluorescence spectroscopy
Horseradish peroxidase
HRP enzyme
Hydrogen
Hydrogen bonding
Hydrogen bonds
Hydrogen peroxide
magnetized solvent
Measurement techniques
Oxidation
oxidation reaction
Peroxidase
Phenols
Phenylenediamine
Protein structure
pure solvent
Pyrogallol
Resorcinol
Secondary structure
Solvents
Substrates
Viscosity measurement
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Summary:The present study aimed to investigate, for the first time, the rate of the oxidation reaction of some derivatives of phenol and aromatic amines, that is, pyrogallol, catechol, resorcinol, ortho‐aminophenol, meta‐aminophenol, para‐aminophenol, ortho‐phenylenediamine, and para‐phenylenediamine, in the presence of hydrogen peroxide in pure and magnetized solvents using horseradish peroxidase enzyme. The reaction was studied in the absence and presence of a magnetized solvent under completely identical conditions. The results showed that magnetized solvent could change the structure of the enzyme and reduce its activity. In addition, it affected the rate of oxidation of the selected derivatives through altering the strength of the hydrogen bonds of the system. The changes in the structure and activity of the enzyme were examined using UV–Vis and fluorescence spectroscopy as well as viscosity measurement technique. Examination of the secondary structure via the far UV‐CD spectrum indicated the increase in the alpha helical structure in the magnetized solvent. When dissolved in a magnetized solvent, hydrogen peroxide as an enzyme substrate reduced the rate of enzymatic reaction and provided lower saturation conditions for the enzyme compared with when it was dissolved in the pure solvent.
ISSN:8756-7938
1520-6033
DOI:10.1002/btpr.3035