研究报告

油酸对鲅鱼肌浆蛋白结构和理化特性的影响

  • 王友军 ,
  • 周李美佳 ,
  • 赵阳美瑾 ,
  • 敖成翔 ,
  • 刘静宜 ,
  • 赵慧 ,
  • 卢航
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  • 1(大连海洋大学 食品科学与工程学院,辽宁 大连,116023)
    2(辽宁省水产品加工及综合利用重点实验室,辽宁 大连,116023)
    3(海洋食品精深加工关键技术省部共建协同创新中心,大连工业大学,辽宁 大连,116023)
第一作者:硕士研究生(卢航副教授为通信作者,E-mail:luhang@dlou.edu.cn)

收稿日期: 2023-06-15

  修回日期: 2023-06-30

  网络出版日期: 2024-08-02

基金资助

辽宁省科技厅项目(2019-ZD-0727);辽宁省教育厅产业技术研究院项目(DL201906)

Effect of oleic acid on structural and physicochemical properties of sarcoplasmic proteins in Scomberomorus niphonius

  • WANG Youjun ,
  • ZHOU Limeijia ,
  • ZHAO Yangmeijin ,
  • AO Chengxiang ,
  • LIU Jingyi ,
  • ZHAO Hui ,
  • LU Hang
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  • 1(College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, China)
    2(Liaoning Provincial Key Laboratory of Aquatic Products Processing and Comprehensive Utilization, Dalian 116023, China)
    3(Collaborative Innovation Center for Key Technologies of Marine Food Finishing and Deep Processing, Dalian Polytechnic University, Dalian 116034, China)

Received date: 2023-06-15

  Revised date: 2023-06-30

  Online published: 2024-08-02

摘要

为研究油酸(oleic acid,OA)对鲅鱼肌浆蛋白(sarcoplasmic proteins,SP)的诱导作用,采用不同浓度(0~40 mmol/L)的OA处理鲅鱼肌浆蛋白,分析对SP结构和理化特性的影响。结果表明,与对照组相比,随着OA浓度的升高,SP中羰基含量随之显著上升(P<0.05),总巯基含量随之显著下降(P<0.05);表面疏水性和傅里叶红外光谱研究发现,OA可以引起SP的疏水基团暴露和去折叠;十二烷基硫酸钠-聚丙烯酰胺凝胶电泳结果反映出OA造成SP聚合物的形成,并通过内源荧光光谱分析发现OA引起SP二硫键交联;最终导致SP溶解度减小、浊度随之增大,说明OA影响SP结构并导致鲅鱼SP的聚集。

本文引用格式

王友军 , 周李美佳 , 赵阳美瑾 , 敖成翔 , 刘静宜 , 赵慧 , 卢航 . 油酸对鲅鱼肌浆蛋白结构和理化特性的影响[J]. 食品与发酵工业, 2024 , 50(13) : 239 -246 . DOI: 10.13995/j.cnki.11-1802/ts.036486

Abstract

To investigate the sarcoplasmic protein (SP) induced by oleic acid (OA), different concentrations (0-40 mmol/L) of OA were used to treat sarcoplasmic proteins of Scomberomorus niphonius and the structural and physicochemical properties of SP after induction were analyzed.Results showed that compared with the control group, the protein carbonyl group increased significantly, and the total sulfhydryl content decreased significantly (P<0.05) with the increase of OA concentration.It was shown that OA could cause the unfolding of SP and exposure of hydrophobic groups with Fourier-transform infrared spectroscopy and surface hydrophobicity.Sodium dodecyl sulfate-polyacrylamide gel electrophoresis results reflected that OA caused the formation of SP polymers.Furthermore, OA could lead to cross-linking of SP disulfide bonds with endogenous fluorescence spectroscopy and surface hydrophobicity analysis.In addition, with the increase of OA concentration, the SP solubility showed a trend of decreasing and increasing turbidity (P<0.05), indicating that OA could trigger changes in the SP structure and the aggregation of SP.

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