Heat-Induced Structural Evolution of Coconut Globulin and Its Techno-Functional Properties

Abstract

The heat-induced aggregation behavior of coconut globulin at pH 2.0 and 85 °C was investigated over a continuous heating period of 0–24 h, with a focus on the temporal evolution of protein structure and corresponding changes in techno-functional performance. The aggregation process exhibited three distinct stages: initial unfolding and dissociation (0–6 h), formation of β-sheet-enriched structures (6–12 h), and subsequent over-aggregation (12–24 h). Surface hydrophobicity reached its maximum at 20 h, foaming capacity peaked at 12 h, and emulsifying activity achieved its optimal value at 10 h. These time-dependent functional variations were closely correlated with progressive conformational rearrangement, peptide chain degradation, and interfacial structural changes. The results establish a time-resolved structure–function correlation for coconut globulin under acidic heating conditions, offering practical guidance for the processing of coconut protein as a plant-based functional ingredient.