Protein aggregation is a pivotal phenomenon that occurs during the processing and preservation of animal-based foods, directly influencing their nutritional value, functionality, and consumer appeal. Thermal treatments such as cooking, pasteurization, and sterilization are essential for food safety but often disrupt protein structure, leading to unfolding, exposure of hydrophobic regions, and aggregation through hydrophobic and disulfide interactions. Similarly, freeze processing—widely employed to extend shelf life—subjects proteins to ice crystal damage, cryoconcentration, and repeated phase transitions, which destabilize native conformations and promote aggregation. These structural modifications affect food quality on multiple levels: they alter texture, juiciness, and water-holding capacity; reduce solubility and digestibility; and influence sensory acceptance. Importantly, the extent and nature of aggregation vary with protein type, processing intensity, and storage conditions, making meat, fish, milk, and egg proteins particularly susceptible. Recent advances, including microencapsulation, cryoprotectants, and alternative processing technologies such as high-pressure or ultrasound, offer strategies to mitigate detrimental aggregation while harnessing beneficial structural changes for desired texture formation. Understanding the molecular basis and practical consequences of protein aggregation is crucial for developing optimized processing methods that preserve quality, enhance nutritional retention, and meet consumer expectations, consolidates current knowledge on aggregation mechanisms, consequences, and control strategies, with emphasis on animal-derived food systems.
