Denaturation Kinetics and Aggregation Mechanism of the Sarcoplasmic and Myofibril Proteins from Grass Carp During Microwave Processing

Optimizing the physicochemical properties of microwave-cooked meat needs a better understanding of the mechanisms responsible for protein changes. This paper explored the causes of aggregation of the denatured fish protein in ready-to-eat food by determining the changes in sarcoplasmic and myofibril proteins, which includes the effects of different microwave power levels (300, 600, and 900 W) and heating times (0-60 s) on the aggregation kinetics and physiochemical properties. The determination of aggregation kinetics that accurately describes microwave cooking characteristics is crucial for the optimization of operating parameters, performance improvement of the cooked food system, and product quality. The aggregation rate and turbidity of proteins increased with increasing microwave power and time. A negative correlation was observed between the protein solubility and microwave power and time. Protein aggregation induced by microwave showed a reliable and reproducible characterization of particle size distributions. At longer microwave heating time or higher microwave power, these protein particles formed larger aggregates.