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

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Abstract

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.

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Acknowledgements

The authors wish to thank ICA Tri Nova, LLC, Newnan, for providing the precursor materials for the preparation of the chlorine dioxide gas.

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  1. Department of Chemistry, Middle Tennessee State University, Murfreesboro, TN, 37132, USA

    Beng Guat Ooi & Sharon Alyssa Branning

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  1. Beng Guat Ooi
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  2. Sharon Alyssa Branning
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Correspondence to Beng Guat Ooi.

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Ooi, B.G., Branning, S.A. Correlation of Conformational Changes and Protein Degradation with Loss of Lysozyme Activity Due to Chlorine Dioxide Treatment. Appl Biochem Biotechnol 182, 782–791 (2017). https://doi.org/10.1007/s12010-016-2361-8

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  • DOI: https://doi.org/10.1007/s12010-016-2361-8

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