食品科学 ›› 2020, Vol. 41 ›› Issue (12): 46-53.doi: 10.7506/spkx1002-6630-20190521-239

• 食品化学 • 上一篇    下一篇

等电点沉淀提取蛋白和漂洗鱼糜蛋白的高温胶凝特性

石柳,章蔚,周俊鹏,汪兰,李新,丁安子,熊光权,杨宏   

  1. (1.湖北省农业科学院农产品加工与核农技术研究所,湖北省农业科技创新中心农产品加工研究分中心,湖北 武汉 430064;2.湖北工业大学生物工程与食品学院,湖北 武汉 430068;3.华中农业大学食品科技学院,湖北 武汉 430070)
  • 出版日期:2020-06-25 发布日期:2020-06-22
  • 基金资助:
    湖北省科技创新专项重大项目(2017ABA141);湖北省农业科学院青年科学基金项目(2017NKYJJ10)

Effects of High Temperature Treatments on the Gel Properties of Fish Proteins Extracted Using Isoelectric Solubilization Precipitation versus Rinsing Method

SHI Liu, ZHANG Wei, ZHOU Junpeng, WANG Lan, LI Xin, DING Anzi, XIONG Guangquan, YANG Hong   

  1. (1. Institute for Farm Products Processing and Nuclear-Agricultural Technology, Hubei Academy of Agricultural Science, Farm Products Processing Research Sub-center of Hubei Innovation Center of Agriculture Science and Technology, Wuhan 430064, China; 2. School of Food and Biological Engineering, Hubei University of Technology, Wuhan 430068, China; 3. School of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China)
  • Online:2020-06-25 Published:2020-06-22

摘要: 研究不同加热温度(100、110、120 ℃)和时间(15、30、60 min)对等电点沉淀法(isoelectric solubilization precipitation,ISP)提取蛋白与漂洗鱼糜蛋白高温胶凝特性的影响,以白鲢为原料,分别测定凝胶强度、持水性、色泽、化学作用力、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳。结果表明,ISP蛋白凝胶的破断力低于漂洗蛋白凝胶,凹陷深度高于漂洗蛋白凝胶。漂洗蛋白凝胶和ISP蛋白凝胶获得最高凝胶强度的热处理温度分别为110 ℃和100 ℃。随着加热时间的延长,凝胶的破断力和凹陷深度降低。ISP蛋白凝胶的持水性不受热处理条件的影响,而漂洗蛋白凝胶的持水性随加热时间的延长而降低,ISP蛋白凝胶的持水性低于漂洗蛋白凝胶。漂洗蛋白凝胶的亮度值(L*)和白度值(W)高于ISP蛋白凝胶,随着加热时间的延长,漂洗蛋白凝胶的L*值和W值呈下降趋势,而ISP蛋白凝胶的L*值和W值呈上升趋势。高温处理过程中,ISP蛋白凝胶和漂洗蛋白凝胶的离子键和氢键含量呈先上升后下降趋势,而疏水相互作用和总巯基含量整体呈下降趋势;漂洗蛋白凝胶和ISP蛋白凝胶的肌球蛋白重链条带消失,肌动蛋白和原肌球蛋白等蛋白条带强度逐渐下降。

关键词: 等电点沉淀, 漂洗鱼糜蛋白, 高温, 胶凝特性

Abstract: The effects of heat treatment temperature (100, 110, and 120 ℃) and duration (15, 30, and 60 min) on the gel properties of proteins extracted from silver carp muscle using isoelectric solubilization precipitation (ISP) and those recovered from surimi wash water including gel strength, water-holding capacity, color, chemical interactions and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) pattern were analyzed and compared. The results showed that that ISP protein gels had weaker breaking force and higher deformation degree than did washed protein gels. The highest gel strength for washed protein gels and ISP protein gels were found under thermal treatments at 110 and 100 ℃, respectively. With increasing treatment time, breaking force and deformation degree decreased for the two protein gels. The water-holding capacity of ISP protein gels was not significantly affected by the treatments, while that of washed protein gels was decreased with increasing heating time. The water-holding capacity, L* value and whiteness of washed protein gels were higher than those of ISP protein gels. With the increase in treatment duration, L* value and whiteness of washed protein gels significantly decreased, while those of ISP protein gels showed an opposite trend. The concentrations of ionic and hydrogen bonds increased first and decreased later, while the concentration of hydrophobic interaction and total sulfydryl group showed a decline trend during the thermal treatment process. With raising temperature and time, the myosin heavy chain (MHC) bands disappeared and the band intensities of actin and myosin light chain gradually decreased in the SDS-PAGE patterns for both protein gels.

Key words: isoelectric solubilization precipitation, surimi gel, high temperature, gel properties

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