CONFORMATIONAL CHANGES OF LYSOZYME DURING PHOTODYNAMIC IN ACTIVATION*

Abstract

Abstract— Egg white lysozyme was inactivated by photodynamic treatment in sodium phosphate buffer at pH8 using methylene blue, eosin Y and FMN as sensitizers. Measurements sensitive to changes in protein conformation, in particular, tryptophyl fluorescence and protease digestibility, were made during the course of inactivation. The rate of change of lysozyme tertiary structure as measured in these ways correlated closely with the rate of loss of enzyme activity during photodynamic treatment. Further, forms of lysozyme which were enzymatically active, but which were more sensitive to high temperature than native enzyme were produced by photodynamic treatment. It is concluded that the photodynamic inactivation of lysozyme under the conditions used results largely from the photooxidation of amino acid residues essential for the maintenance of the catalytically active conformation of the enzyme.