食品科学 ›› 2020, Vol. 41 ›› Issue (14): 15-22.doi: 10.7506/spkx1002-6630-20190620-232

• 食品化学 • 上一篇    下一篇

海鲈鱼糜加工及凝胶形成过程中蛋白质的变化机理

刘芳芳,林婉玲,李来好,吴燕燕,杨少玲,黄 卉,杨贤庆,林 织   

  1. (1.中国水产科学研究院南海水产研究所,国家水产品加工技术研发中心,农业农村部水产品加工重点实验室,广东 广州 510300;2.上海海洋大学食品学院,上海 201306;3.广东顺欣海洋渔业集团有限公司,广东 阳江 529800)
  • 发布日期:2020-07-29
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2016YFD0400201-6);中央级公益性科研院所基本科研业务费专项(2019TS16); 现代农业产业技术体系建设专项(CARS-47);“扬帆计划”引进创新创业团队专项(2015YT02H109)

Mechanism Underlying Protein Changes during Processing and Gelation of Sea Bass Surimi

LIU Fangfang, LIN Wanling, LI Laihao, WU Yanyan, YANG Shaoling, HUANG Hui, YANG Xianqing, LIN Zhi   

  1. (1. Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National Research and Development Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China; 2. College of Food Sciences & Technology, Shanghai Ocean University, Shanghai 201306, China; 3. Guangdong Shun Xin Ocean Fishery Group Co. Ltd., Yangjiang 529800, China)
  • Published:2020-07-29

摘要: 以pH值、水分含量、蛋白质间化学作用力、三氯乙酸(trichloroacetic acid solution,TCA)-可溶性肽、蛋白质溶解度、蛋白质二级结构以及超微结构等物理化学变化为指标,研究蛋白质在鱼糜加工及凝胶形成过程中的变化机理。结果表明:在海鲈鱼糜加工过程中,漂洗可调节鱼糜pH值使其接近中性,斩拌和低温加热使pH值降低,40 ℃和90 ℃加热对鱼糜含水量无显著影响。漂洗可有效抑制蛋白质降解,使TCA-可溶性肽下降83%;斩拌对TCA-可溶性肽、溶解度和巯基无显著影响(P>0.05);40 ℃加热,由于组织蛋白酶的作用,TCA-可溶性肽增大68%。离子键和氢键在整个过程中呈持续下降趋势,加热后显著减少(P<0.05);疏水相互作用和二硫键呈上升趋势,均在90 ℃加热后含量最大;非二硫共价键在40 ℃加热时最大。漂洗后β-折叠结构含量下降13%,β-转角结构含量上升39%,无规卷曲和α-螺旋变化不显著(P>0.05);斩拌对β-折叠、β-转角、无规卷曲和α-螺旋均影响显著;40 ℃加热,α-螺旋解旋,β-折叠含量上升8%;90 ℃加热,β-转角含量上升36%(P<0.05),无规卷曲含量变化不显著。经相关性分析,蛋白质间化学键与α-螺旋和β-转角显著相关,与β-折叠和无规卷曲无明显相关性。本研究旨在为鱼糜凝胶形成机理的研究提供进一步参考。

关键词: 鱼糜凝胶;加工过程;理化性质;二级结构

Abstract: The physicochemical changes such as pH, moisture content, and chemical interaction among proteins, trichloroacetic acid solution (TCA)-soluble peptide, protein solubility, protein secondary structures and ultra- structure were measured to study the mechanism underlying protein changes during the processing and gelation of surimi from sea bass. The results showed that during the processing of surimi, pH was adjusted to approximately 7 by rising, and was reduced by chopping and heating at low temperature. Heating at 40 and 90 ℃ had no significant effect on the moisture content of surimi. Rinsing effectively inhibited protein degradation, and reduced TCA-soluble peptide by 83%. Chopping had no significant effect on TCA-soluble peptide content, protein solubility or sulfhydryl group content (P > 0.05). Heating at 40 ℃increased TCA-soluble peptide content by 68% due to the action of cathepsin. Ion bonds and hydrogen bonds continued to decrease during the whole process, and decreased significantly upon heating (P < 0.05). Hydrophobic interaction and disulfide bonds showed an upward trend, reaching the highest value upon heating at 90 ℃. Upon heating at 40 ℃, the maximum level of non-disulfide covalent bond was reached. The content of β-fold structure decreased by 13% after rinsing, the content of β-turn structure increased by 39%, while the contents of random coil and α-helix did not significant changed (P > 0.05). Chopping did not significantly affect the contents of β-fold, β-turn, random coil or α-helix. Upon heating at 40 ℃, the α-helix content decreased and the β-fold content increased by 8%. Upon heating at 90 ℃, the β-turn content increased by 36% (P < 0.05), the random coil content did not significantly changed. Correlation analysis showed that the chemical bonds between protein molecules were significantly correlated with the contents of α-helix and β-turn, but not with the contents of β-sheet and random coil. This study provides useful information for further study of the mechanism underlying the formation of surimi gel.

Key words: surimi gel; processing; physicochemical properties; secondary structure

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