Transglutaminase (TGase)-crosslinked Cyperus esculentus protein and whey protein complexes as Pickering stabilizers...

We developed an enzymatic hetero-crosslinking strategy to create protein-based Pickering stabilizers that enhance ice-cream meltdown resistance and structural stability. Transglutaminase induced covalent coupling between Cyperus esculentus protein (CEP) and whey protein isolate (WPI), establishing a composition-structure-function framework. Under an optimized window (40 °C, 2 h, pH 6.5), crosslinking promoted an α-helix-to-β-sheet transition and increased surface hydrophobicity. A functional optimum at 30% CEP yielded a continuous, compact scaffold with fast interfacial adsorption. In coconut-oil Pickering emulsions, it improved freeze-thaw stability by forming a resilient interfacial film that withstood ice-crystal disruption. In model ice cream, it lowered the ice-crystallization peak temperature, reduced air-cell size by ∼50%, and increased overrun, producing the longest first-drip time and slowest melting rate. These results clarify how protein engineering governs interfacial mechanics and network connectivity across multiphase frozen matrices. Electronic-nose analysis indicated altered volatile fingerprints and aroma-release patterns, offering a scalable, clean-label approach for frozen dessert formulation.