Open AccessIntense Pulsed Electric Fields Denature Urease Protein
Author(s) -
Gen Urabe,
Toshiaki Katagiri,
S. Katsuki
Publication year - 2020
Publication title -
bioelectricity
Language(s) - English
Resource type - Journals
eISSN - 2576-3113
pISSN - 2576-3105
DOI - 10.1089/bioe.2019.0021
Subject(s) - urease , nanosecond , electric field , lysozyme , chemistry , crystallography , enzyme , albumin , peptide bond , biophysics , peptide , biochemistry , optics , biology , physics , laser , quantum mechanics
Background: This article describes the effects of nanosecond pulsed electric fields (nsPEFs) on the structure and enzyme activity of three types of proteins. Materials and Methods: Intense (up to 300 kV/cm) 5-ns-long electrical pulses were applied for 500 times at 3 Hz to solutions of lysozyme, albumin, and urease. We analyzed covalent bonds (peptide bonds and disulfide bonds) of lysozyme and albumin, and also the tertiary and quaternary structures of urease as well as urease activity. Results: The results indicated deformation of both the quaternary and tertiary structures of urease upon exposure to an electric field with an amplitude of 250 kV/cm or higher, whereas no structural changes were observed in lysozyme or albumin, even at 300 kV/cm. The enzyme activity of urease also decreased at field strengths of 250 kV/cm or higher. Conclusion: Our experiments demonstrated that intense nsPEFs physically affected the conformation and function of some types of proteins. Such intense electric fields often occur in cell membranes when exposed to a moderate pulsed electric field.