Abstract
In this study, the effect of protein oxidation on the thermal gelation of chicken breast myofibrillar proteins (MPs) was investigated. MP samples treated with different degrees of oxidation were heated (1.5 °C/min) to different end-point temperatures to simulate the thermal gelation process. The results showed that the water-holding capacity (WHC) significantly decreased with increasing temperature, and higher oxidation degree resulted in worse WHC of heat-induced gel. Compared with high degrees of oxidation, low degrees of MP oxidation reduced the migration of immobile water, inhibited its release as free water, enhanced WHC and favored the formation of β-sheet and β-turn structures. Therefore, low oxidation promoted the formation of β-sheet and β-turn structures to form a better gel microstructure with less formation of free water on the thermal gelation and therefore increased the WHC. High oxidation was just the opposite, and high temperature aggravated this negative effect.
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