How Heat Changes Milk Protein Digestion! #sciencefather #researchawards #MilkScience #ProteinDigestion



Milk is a powerhouse of nutrients, with proteins like casein and whey playing a key role in its health benefits. However, these proteins are sensitive to heat. When milk is processed using heat treatments such as pasteurization or sterilization, its protein structure is altered. Understanding how heat affects these proteins helps us better comprehend their digestion and nutritional outcomes.


Heating milk causes a process called protein denaturation. This means the proteins unfold from their natural shape, exposing hidden amino acid chains. For example, whey proteins like β-lactoglobulin and α-lactalbumin are especially sensitive to heat. Denaturation can make them more accessible to digestive enzymes, which might improve how the body breaks them down during digestion.


Studies have shown that heat-treated milk proteins may digest at different rates compared to raw milk proteins. In some cases, heating slows down gastric digestion due to the formation of larger protein aggregates. This can delay the release of nutrients in the stomach but may allow for more controlled absorption in the intestine, which could benefit sustained energy release.


Despite changes in digestion speed, the bioavailability of amino acids—the building blocks of protein—remains mostly unaffected. This means the body still absorbs the same amount of essential nutrients, even if heat alters the digestion timeline. This is good news for consumers relying on heat-processed dairy products for their protein intake.


Heat treatment of milk is crucial for food safety, but it also modifies the way our body digests milk proteins. While it can affect the speed of digestion, it doesn’t reduce the nutritional value of the amino acids provided. Whether in raw or heat-treated form, milk remains a highly valuable dietary protein source. As science progresses, we continue to refine heat treatments to optimize both safety and nutrition.


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