Lysozyme is an enzyme that prevents bacterial infections by attacking peptidoglycan, a component of certain bacterial cell walls. Peptidoglycan is composed of the repeating amino sugars N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM), which are crosslinked by peptide bridges. Lysozyme hydrolyzes the bond between NAG and NAM, increasing the bacteria's permeability and causing the bacteria to burst. It is widely distributed in plants and animals. The majority of the lysozyme used in research is purified from hen egg whites. In a thermal unfolding measurement in Prometheus, in which it is assured that the protein does not aggregate (e.g. by choosing an appropriate unfolding buffer), not only the transition temperature T_m, but also the transition enthalpy DH_m  can be determined.

thermal unfolding | conformational stability | colloidal stability | thermodynamics | T_m | T_on | T_agg | DH_m | PR-P-0010