Correlation of Conformational Changes and Protein Degradation with Loss of Lysozyme Activity Due to Chlorine Dioxide...

Chlorine dioxide (ClO₂) is a potent oxidizing agent used for the treatment of drinking water and decontamination of facilities and equipment. The purpose of this research is to elucidate the manner in which ClO₂ destroys proteins by studying the effects of ClO₂ on lysozyme. The degree of enzyme activity lost can be correlated to the treatment time and levels of the ClO₂ used. Lysozyme activity was drastically reduced to 45.3% of original enzyme activity when exposed to 4.3 mM ClO₂ in the sample after 3 h. Almost all activities were lost in 3 h after exposure to higher ClO₂ concentrations of up to 16.8 and 21.9 mM. Changes in protein conformation and amount as a result of ClO₂ treatment were determined using the Raman spectroscopy and gel electrophoresis. Raman shifts and the alteration of spectral features observed in the ClO₂-treated lysozyme samples are associated with loss of the α-helix secondary structure, tertiary structure, and disulfide bond. Progressive degradation of the denatured lysozyme by increasing levels of chlorine dioxide was also observed in gel electrophoresis. Hence, ClO₂ can effectively cause protein denaturation and degradation resulting in loss of enzyme activity.