Science blog posts

An IgM-lipoprotein complex clusters fat globules together in cold raw milk, accelerating creaming well beyond what density alone would predict.

Refrigerating milk causes one of its four major casein proteins to leave its normal structure entirely, a reversible effect documented since 1977.

In some cows’ milk, simply cooling it after milking is enough to trigger rancidity, no bacteria or physical damage required.

Freezing raw milk causes real structural damage from ice crystals, and how you freeze and thaw it changes how much. Here is what the research documents.

Refrigeration favors a specific category of bacteria whose enzymes often survive pasteurization and even UHT heat completely intact.

Unfortified milk contains too little vitamin D to matter nutritionally, and fortification, not pasteurization, supplies almost all of what is on the label.

The milk fat globule membrane’s own proteins respond to heat unevenly: some resist modification, one shows stabilization, and processing can add proteins in.

Between alkaline phosphatase and lactoperoxidase sits GGT, a milk enzyme whose heat sensitivity distinguishes specific pasteurization intensities.

HPP denatures a different set of whey proteins than heat, preserves human milk miRNA far better, but isn’t automatically gentler overall.

Milk’s main native protein-cutting enzyme survives standard pasteurization largely intact and even retains activity after UHT, unlike most milk enzymes.

Unlike most milk components, oligosaccharides show up consistently unaffected by standard pasteurization across more than a decade of independent research.

A controlled comparative study found furosine, the marker for heat-induced protein damage, rises far less under pasteurization than under UHT or sterilization.