Protein adsorption can also occur as a direct result of heating a mixture. Protein adsorption in milk processing is often used as a model for this type of adsorption in other situations. Milk is composed mainly of water, with less than 20% of suspended solids or dissolved proteins. Proteins make up only 3.6% of milk in total, and only 26% of the components that are not water. These proteins are all responsible for fouling that occurs during pasteurization.
As milk is heated during pasteurization many of the proteins in the milk are denatured. Pasteurization temperatures can reach 161 °F (71.7 °C). This temperature is high enough to denature the proteins below, lowering the nutritional value of the milk and causing fouling. Milk is heated to these high temperatures for a short time (15–20 seconds) to reduce the amount of denaturization. However fouling from denatured proteins is still a significant problem.  
Denaturation exposes hydrophobic amino acid residues in the protein, which had been previously protected by the protein. The exposed hydrophobic amino acids decrease the entropy of the water surrounding them, making it favorable for surface adsorption. Some of the β-lactoglobulin (β-lg) will adsorb directly onto the surface of a heat exchanger or container. Other denatured β-lg molecules adsorb to casein micelles, which are also present in the milk. As more and more β-lg proteins bind to the casein micelle it forms an aggregate, which will then diffuse to the heat exchanger and/or surface of the container.