What question did this study set out to answer?

To investigate controlled trypsin hydrolysis's ability to reduce α S1-casein and generate bioactive peptides.

Controlled Trypsin Hydrolysis of Bovine Casein for Preferential α S1 -Casein Reduction: Fraction-Specific Kinetics, α S1 -Casein-Related Antigenicity and Candidate Bioactive Peptides

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Randomized trial demonstrates reduced α S1-casein levels in bovine casein, suggesting new infant formula applications.

To investigate controlled trypsin hydrolysis's ability to reduce α S1-casein and generate bioactive peptides.
Controlled trypsin hydrolysis at 38 °C, pH 8.0 for 5 hours.
Peptidomics analysis identified peptides, specifically focusing on binding affinity to α-amylase.
Evaluated radical scavenging activity and enzyme inhibition of the hydrolysate.
Relative residual peak area of α S1-casein decreased significantly, remaining α S2-casein and β-casein levels at 33.15% and 45.01%.
Identified 17 peptides, with HQGLPQEVLNENLLR showing the highest binding affinity to α-amylase (−13.98 kcal/mol).
Achieved 92.10% ABTS radical scavenging activity and 53.44% α-amylase inhibition.

Wang et al. (2026) studied this question.

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