Abstract

Heat‐treatment is one of the most commonly used processes in food preparation technology. An understanding of the thermodynamics of protein stability and of conformational changes of proteins, acquired through the measurement of the denaturation temperature, is therefore of particular importance. This paper attempts to shed light on the interpretation of recent calorimetric data on the thennal denaturation of bovine β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin by showing that thermodynamic parameters of heat‐induced unfolding, measured by differential scanning calonmetry, are closely related to the prevailing chemical conditions such as pH, concentration of ions, protein purity, and protein concentration.