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An Enzyme–Plasma Relay: Sculpting the Potential of Casein
Within a drop of milk, casein holds a wealth of nutritional value and bioactive peptide potential. Yet its utilization faces two intertwined challenges: residual antigenicity and the bitterness generated during enzymatic hydrolysis. How can changes at the molecular level help balance taste and functionality? This study begins with alkaline protease hydrolysis, followed by cold plasma treatment, in a process of “molecular sculpting.” Acting as molecular scissors, the protease first cleaves casein chains; reactive species generated by cold plasma then further modify the hydrolysates, altering peptide structures and amino acid composition. This enzyme–plasma relay further reduces residual IgE-binding activity, decreases bitterness measured by an electronic tongue, and shows potential to improve in vitro antioxidant properties. The cover captures this sequence within a single drop of milk, where loosely coiled molecular chains, a site of enzymatic cleavage, and the glow of plasma illustrate the transformation of casein and its peptides. By linking molecular cleavage and modification to changes in antigenic reactivity, bitterness, and antioxidant properties, this work offers a new approach to developing milk protein hydrolysates with a more favorable combination of qualities.
Food Innovation and Advances 5(3): 406−418 doi: 10.48130/fia-0026-0034
