Long-time oscillations in correlation of lysozyme solutions and the effects of antagonistic salt in external electric field light scattering

Abstract

Lysozyme is a ubiquitous protein and enzyme that prevents the bacterial infections and maintains the catalytic balance in majority of biological fluids. However, it often causes problems at higher concentrations. In particular, the build up of lysozyme engaged with other protein interactions initiates severe disorders in most mammalian cells, such as the formation of harmful aggregates in the nervous system and the loss of connectivity in rheumatism. To understand such complex behaviors with respective to the catalytic activity of the enzyme, the lysozyme solution and the effect of hydrophobic antagonistic salt (NaBPh4) are explored in-vitro, in their relaxation behaviors. Here, we used, both normal dynamic light scattering and home-built in-situ AC external electric field light scattering. As results, the fast and slow-mode