THE HEAT INACTIVATION OF ANTISTAPHYLOCOCCUS BACTERIOPHAGE

Abstract

The heat inactivation of Staphylococcus bacteriophage suspended in broth of pH 7.6 at 51-62[degree] C. proceeded strictly in accordance with the equation for a monomolecular reaction. The data present no evidence that lysates consist of particles possessing varying degrees of resistance to heat; and, further, they can not be interpreted as suggesting the living nature of bacteriophage. While it is true that many unicellular organisms follow a logarithmic order of death, inactivation of certain enzymes is similarly an exponential process. The critical thermal increment over the temp. range studied was 101,000, i.e., of the same order of magnitude as those values determined for the spontaneous destruction of enzymes, the heat denaturation of egg-white, and for the course of death among some bacterial populations. This extremely high critical thermal increment characterizes protein denaturation reactions and it would suggest that the chief reaction involved in heat inactivation of bacteriophage is a protein denaturation.