Category
Basic
Description
Per- and polyfluoroalkyl substances (PFAS) are persistent environmental contaminants, motivating the exploration of peroxidases as potential bioremediation catalysts. This study spectroscopically characterized three peroxidases, with a focus on Pumpkin Skin Peroxidase (PKS). Initial characterization assessed PKS equilibrium binding with various ligands to determine dissociation constants (Kd) for each ligand-enzyme interaction. To characterize PKS catalytic activity, guaiacol oxidation was monitored, with parallel KF trials modelled by Michaelis-Menten kinetics, revealing fluoride-induced increases in Km and Vmax, consistent with an inhibitory effect on substrate binding and catalytic turnover. These findings provide insight into the function of PKS and its potential for environmentally relevant PFAS degradation.
Characterizing Novel Peroxidase Activity Through Enzyme Kinetics and Equilibrium Binding
Basic
Per- and polyfluoroalkyl substances (PFAS) are persistent environmental contaminants, motivating the exploration of peroxidases as potential bioremediation catalysts. This study spectroscopically characterized three peroxidases, with a focus on Pumpkin Skin Peroxidase (PKS). Initial characterization assessed PKS equilibrium binding with various ligands to determine dissociation constants (Kd) for each ligand-enzyme interaction. To characterize PKS catalytic activity, guaiacol oxidation was monitored, with parallel KF trials modelled by Michaelis-Menten kinetics, revealing fluoride-induced increases in Km and Vmax, consistent with an inhibitory effect on substrate binding and catalytic turnover. These findings provide insight into the function of PKS and its potential for environmentally relevant PFAS degradation.
