鲢鱼鱼糜凝胶在高温（≥100℃）下的特性：品质变化、水分分布和蛋白质模式,International Journal of Food Science & Technology

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鲢鱼鱼糜凝胶在高温（≥100℃）下的特性：品质变化、水分分布和蛋白质模式
International Journal of Food Science & Technology ( IF 2.6 ) Pub Date : 2022-04-26 , DOI: 10.1111/ijfs.15799
Qixing Jiang _{1,

2} , Wenmin Wu ₁ , Jingwen Han ₁ , Hau Yin Chung ₂ , Pei Gao ₁ , Dawei Yu ₁ , Peipei Yu ₁ , Yanshun Xu ₁ , Wenshui Xia ₁

Affiliation

研究了高温处理（100-125°C）对鲢鱼鱼糜凝胶性能的影响。结果表明，随着加热温度的升高和加热时间的延长，鱼糜凝胶的凝胶强度和持水量（WHC）显着下降（P < 0.05），且温度越高，下降趋势越大。疏水作用和二硫键显着减少，而离子键显着增加（P < 0.05)，β-折叠增加而β-转角和卷曲明显减少，证实了高温处理引起的蛋白质二级结构的变化。肌球蛋白重链（MHC）和肌动蛋白条带逐渐变窄，SDS-PAGE产生大于250 kDa的新条带，表明蛋白质发生聚集和交联反应。然而，50-75 kDa 的条带强度增加和三氯乙酸 (TCA) 可溶性肽的增加表明蛋白质降解。PT ₂₂减少和PT ₂₃增加表明固定水在凝胶基质中转化为游离水。综上所述，高温加热引起蛋白质二级结构的变化以及化学力和水的转化，导致蛋白质变性、聚集、交联和降解，形成松散不规则的凝胶网络。

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Characteristics of silver carp surimi gel under high temperature (≥100 °C): quality changes, water distribution and protein pattern

The effects of high-temperature treatments (100–125 °C) on the properties of silver carp surimi gel were studied. The results showed that the gel strength and water holding capacity (WHC) of surimi gel decreased significantly (P < 0.05), with the increase of heating temperature and the prolongation of heating time, and the higher the temperature, the greater the decrease trend. Hydrophobic interaction and disulphide bonds decreased significantly, while ionic bonds increased significantly (P < 0.05), as well as β-sheet increased while β-turn and coil decreased significantly, which confirmed the changes of protein secondary structure caused by high-temperature treatments. Myosin heavy chain (MHC) and actin bands gradually narrowed, and the production of new bands larger than 250 kDa by SDS-PAGE showed the aggregation and cross-linking reaction of proteins. However, the increased band intensity of 50–75 kDa and the increase of trichloroacetic acid (TCA) soluble peptides showed the degradation of proteins. The decrease of PT₂₂ and the increase of PT₂₃ indicated the conversion of immobilised water to free water in the gel matrix. In conclusion, high-temperature heating caused the changes of protein secondary structure as well as chemical forces and water conversion, resulting in protein denaturation, aggregation, cross-linking and degradation, forming a loosen and irregular gel network.

更新日期：2022-04-26

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