Lysozyme is an enzyme that hydrolyzes the polysaccharides that form the cell walls of eubacteria found in human tears, nasal discharge, and breast milk. Industrially, hen egg-white lysozyme extracted from egg-white is used in the food industry to improve shelf life of food products and in the pharmaceutical industry as a cold medicine ingredient. Heat denatures, causes conformational change, and increases the hydrophobicity of lysozyme, resulting in precipitation.
Understanding the specific structures involved in the heat denaturation process is important for supporting stability and steric structure formation.
We used dynamic light scattering to evaluate the heat denaturation process, including the effects of temperature on particle diamter and relative light scattering intensity.
