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Herein, we discuss changes in the emulsifying properties of myofibrillar protein (MP) because of protein denaturation and aggregation from quick-frozen pork patties with multiple fat levels and freeze–thaw (F–T) cycles. Protein denaturation and aggregation were confirmed by the significantly increased surface hydrophobicity, turbidity, and particle size, as well as the significantly decreased solubility and absolute zeta potential, of MPs with increases in fat levels and F–T cycles (p &lt; 0.05). After multiple F–T cycles, the emulsifying activity and emulsion stability indices of all samples were significantly reduced (p &lt; 0.05). The emulsion droplets of MP increased in size, and their distributions were dense and irregular. The results demonstrated that protein denaturation and aggregation due to multiple F–T cycles and fat levels changed the distribution of surface chemical groups and particle sizes of protein, thus affecting the emulsifying properties.

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Mechanisms of Change in Emulsifying Capacity Induced by Protein Denaturation and Aggregation in Quick-Frozen Pork Patties with Different Fat Levels and Freeze–Thaw Cycles