食品科学 ›› 2021, Vol. 42 ›› Issue (1): 101-107.doi: 10.7506/spkx1002-6630-20191213-152

• 基础研究 • 上一篇    下一篇

热处理温度及时间对镜鲤鱼肌原纤维蛋白热聚集行为的影响

畅鹏,谢艳英,王浩,夏秀芳   

  1. (东北农业大学食品学院,黑龙江 哈尔滨 150030)
  • 发布日期:2021-01-18
  • 基金资助:
    黑龙江省百千万工程科技重大专项(2019ZX07B03)

Effects of Heat Treatment Temperature and Time on Thermal Aggregation Behavior of Myofibrillar Proteins from Mirror Carp (Cyprinus carpio)

CHANG Peng, XIE Yanying, WANG Hao, XIA Xiufang   

  1. (School of Food Science, Northeast Agricultural University, Harbin 150030, China)
  • Published:2021-01-18

摘要: 通过测定蛋白溶解度、浊度、表面疏水性、巯基含量、破碎力等指标并结合傅里叶变换红外光谱分析,探究热处理温度(30~90 ℃)和保温时间(0~60 min)对镜鲤鱼肌原纤维蛋白热聚集行为的影响。结果表明,镜鲤鱼肌原纤维蛋白热诱导聚集具有高度的温度依赖性。30 ℃处理条件下,蛋白变性程度较小,活性巯基含量增加,总巯基含量不变,二硫键未形成,此时蛋白聚集主要依靠表面疏水相互作用。随着温度的升高,蛋白具有高的表面疏水性、β-折叠结构含量、浊度、破碎力和低的巯基含量、α-螺旋结构含量、溶解度。这表明热处理温度的升高导致蛋白具有较高的热诱导聚集性。在0~15 min保温处理过程中,蛋白各指标水平变化显著(P<0.05),并在30 min后基本保持稳定。另外,在70 ℃、30 min时蛋白热诱导凝胶强度最大(1.07 N)。综上,热处理条件对蛋白热聚集行为具有显著影响,控制热处理条件可以调节蛋白热聚集行为。

关键词: 热处理条件;镜鲤鱼;肌原纤维蛋白质;热聚集行为?

Abstract: Effects of heat treatment temperature (30–90 ℃) and time (0–60 min) on the thermal aggregation behavior of myofibrillar proteins (MPs) from mirror carp (Cyprinus carpio) were studied by measuring changes in protein solubility, turbidity, surface hydrophobicity, sulfhydryl content, Fourier transform infrared spectrum and the rupture force of heat-induced MP gels. The results showed that the heat-induced aggregation of MPs strongly depended on temperature. After heat treatment at 30 ℃, the degree of protein denaturation became smaller, and the active sulfhydryl content increased, while the total sulfhydryl content remained unchanged without the formation of any disulfide bonds. In this case, protein aggregation mainly depended on the surface hydrophobic interaction. As heating temperature increased, surface hydrophobicity, β-sheet content, turbidity and the rupture force of heat-induced gels increased, and sulfhydryl content, α-helix content, and solubility decreased. These results corroborated that the increase of temperature could lead to high aggregation ability of proteins. All the tested indexes changed significantly (P < 0.05) during heat treatment from 0 to 15 min and remained stable from 30 min onward. In addition, the highest heat-induced gel strength (1.07 N) was obtained upon heat treatment at 70 ℃ for 30 min. Collectively, the above results suggest that protein thermal aggregation behavior is significantly affected by heat treatment conditions, and it can be regulated by controlling heat treatment condition.

Key words: heat treatment conditions; mirror carp; myofibrillar proteins; thermal aggregation behavior

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