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Modulation of the catalytic activity of free and immobilized peroxidase by extremely low frequency electromagnetic fields: dependence on frequency
Author(s) -
Portaccio M.,
De Luca P.,
Durante D.,
Grano V.,
Rossi S.,
Bencivenga U.,
Lepore M.,
Mita D.G.
Publication year - 2005
Publication title -
bioelectromagnetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.435
H-Index - 81
eISSN - 1521-186X
pISSN - 0197-8462
DOI - 10.1002/bem.20059
Subject(s) - point of delivery , peroxidase , covalent bond , chemistry , horseradish peroxidase , catalysis , membrane , enzyme , bioelectromagnetics , gelatin , immobilized enzyme , enzyme assay , biophysics , magnetic field , biochemistry , organic chemistry , physics , biology , quantum mechanics , agronomy
Abstract A study of the influence of electromagnetic fields (EMF) of various frequencies, from 50 up to 400 Hz, on the catalytic activity of soluble and insoluble horseradish peroxidase (POD) was carried out. To simulate the conditions in which the enzyme operates in vivo, the POD was immobilized by entrapment on a gelatin membrane or by covalent attachment on a nylon graft membrane. The rate of inactivation of the soluble POD was found to exhibit positive and negative interactions with the 1 mT applied magnetic field, with an optimum positive effect at 130 Hz. The immobilized PODs, on the contrary, do not exhibit negative interactions, but show a maximum positive interaction at 150 Hz when entrapped and at 170 Hz when covalently attached. At 50 Hz and at frequencies higher than 250 Hz no effects were observed with insoluble POD. The optimum frequency of positive interaction between the EMF and the catalytic activity of the insoluble enzymes is shifted with respect to that of the soluble enzymes towards higher frequencies, the size of the shifts being dependent on the intensity of the physical forces involved in the immobilization process. Bioelectromagnetics 26:145–152, 2005. © 2005 Wiley‐Liss, Inc.