Protein Digestion Dynamics in Infant Nutrition
Summary
Protein digestion in early life is a finely tuned process that underpins growth, development and immune maturation. Human milk proteins, predominantly caseins and whey, undergo sequential gastric and intestinal hydrolysis, with casein micelles forming coagulates under acidic, pepsin-rich conditions and whey proteins remaining largely soluble. The kinetics of coagulation influence gastric emptying rates, peptide release profiles and subsequent uptake of amino acids. Processing variables—such as mineral balance, thermal treatments and glycation during formula manufacture—can alter protein structure, unfolding and aggregation, thereby modulating enzyme accessibility and digestive efficiency. Recent advances in dynamic in vitro models and animal studies have elucidated the interplay between curd rheology, proteolytic kinetics and peptide bioavailability. A detailed understanding of these mechanisms informs the design of infant formulas that better replicate human milk digestion, optimise nutrient delivery and promote tolerance and gut health across diverse clinical and socio-economic contexts.
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Protein Digestion Dynamics in Infant Nutrition publication trend
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Technical terms
Casein micelle: Colloidal assemblies of casein proteins and calcium phosphate that coagulate under gastric conditions.
Gastric coagulation: The acid- and pepsin-driven aggregation of milk proteins into curds, affecting emptying rate.
Maillard reaction: Non-enzymatic glycation between reducing sugars and amino groups during heat processing.
Protein unfolding: Structural loosening of tertiary and quaternary protein conformations that enhances enzyme binding.
Proteolysis: Enzymatic cleavage of peptide bonds, producing smaller peptides and free amino acids.
References
- Milk protein coagulation under gastric conditions: A review. International Dairy Journal (2021).
- Influence of micellar calcium phosphate on in vitro gastric coagulation and digestion of milk proteins in infant formula model systems. International Dairy Journal (2020).
- Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release. Food & Function (2020).
- Kinetics of pepsin-induced hydrolysis and the coagulation of milk proteins. Journal of Dairy Science (2022).
- Heat-induced unfolding facilitates plant protein digestibility during in vitro static infant digestion. Food Chemistry (2021).
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