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

化学 鲢鱼 变性(裂变材料) 三氯乙酸 肌球蛋白 蛋白质聚集 降级(电信) 挑剔 离子强度 蛋白质二级结构 胶束 色谱法 生物物理学 生物化学 核化学 有机化学 电信 渔业 水溶液 计算机科学 生物
作者
Qixing Jiang,Wei Wu,Jie Han,Hau Yin Chung,Pei Gao,Dawei Yu,Peipei Yu,Yanshun Xu,Wenshui Xia
出处
期刊:International Journal of Food Science and Technology [Wiley]
卷期号:57 (7): 4613-4627 被引量:7
标识
DOI:10.1111/ijfs.15799
摘要

Abstract 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 PT 22 and the increase of PT 23 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.
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