Based on proteomics probing into the deterioration mechanism of pork batter gel caused by different cooking temperatures.

Compared to the control group Z0, the number of hydrogen bonds showed a trend of decrease firstly, then, increased as the increase of cooking temperature point.

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Compared with the control group Z0, the content of actin (43 kDa) showed an increasing trend at Z2 and Z3, which might be due to the aggregation of small molecular weight protein molecules of pork batter gel or the degradation of large molecular weight protein molecules to increase the content of aggregates at 43 kDa; however, the band at 43 kDa showed a weakening trend at Z4, which might be due to excessive aggregation of actin molecules to form larger aggregates or further degradation of the formed aggregates, thus, resulting in a decrease of the content of 43 kDa.

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Compare to Z3, the number of aggregates with weight greater than 220 kDa decreased at Z4, the reason for this phenomenon might be that, under this heating condition 121 °C (30 min), the formed aggregates undergo further degradation, thus, resulting in a decreasing trend of aggregates content.

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