食品科学 ›› 2020, Vol. 41 ›› Issue (17): 9-16.doi: 10.7506/spkx1002-6630-20190824-254

• 基础研究 • 上一篇    下一篇

烷过氧自由基氧化对草鱼肌原纤维蛋白热聚集行为的影响

李学鹏,刘慈坤,王金厢,周明言,蔺博燕,李文协,朱文慧,励建荣,林洪   

  1. (1.中国海洋大学食品科学与工程学院,山东 青岛 266003;2.渤海大学食品科学与工程学院,生鲜农产品贮藏加工及安全控制技术国家地方联合工程研究中心,国家鱼糜及鱼糜制品加工技术研发分中心,辽宁 锦州 121013)
  • 出版日期:2020-09-15 发布日期:2020-09-16
  • 基金资助:
    国家自然科学基金面上项目(31771999;31571868);中国博士后基金项目(2015M582143)

Effect of Alkylperoxyl Radical Oxidation on Heat-Induced Aggregation Behavior of Myofibrillar Protein from Grass Carp (Ctenopharyngodon idellus)

LI Xuepeng, LIU Cikun, WANG Jinxiang, ZHOU Mingyan, LIN Boyan, LI Wenxie, ZHU Wenhui, LI Jianrong, LIN Hong   

  1. (1. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China;2. National & Local Joint Engineering Research Center of Storage Processing and Safety Control Technology for Fresh Agricultural Products, National R & D Branch Centre for Surimi and Surimi Products Processing, College of Food Science and Engineering, Bohai University, Jinzhou 121013, China)
  • Online:2020-09-15 Published:2020-09-16

摘要: 采用不同浓度2,2’-偶氮(2-脒基丙烷)二盐酸盐(2,2’-azobis(2-amidinopropane)dihydrochloride,AAPH)溶液有氧热分解产生的烷过氧自由基体系对草鱼肌原纤维蛋白进行模拟氧化,通过测定草鱼及原纤维蛋白热稳定性、表面疏水性、Zeta电位、浊度、平均粒径并进行内源荧光光谱分析以及原子力显微镜观察,研究不同氧化程度肌原纤维蛋白溶液在加热过程中热聚集行为的差异。结果显示,较低浓度(不高于1.0 mmol/L)AAPH氧化处理有助于增强草鱼肌原纤维蛋白的热稳定性,而高浓度(5.0 mmol/L)AAPH氧化则降低其热稳定性。随着加热温度的升高,对照组和各氧化处理组样品蛋白溶液的表面疏水性指数、Zeta电位绝对值、浊度呈先升高后降低趋势。内源荧光强度随加热温度的升高逐渐降低并出现红移,且氧化程度越大,红移现象越明显。对照组和0.2 mmol/L AAPH氧化组样品热聚集体的平均粒径随着加热温度的升高逐渐增大,1.0 mmol/L和5.0 mmol/L AAPH氧化组样品则呈先增大后减小趋势。原子力显微镜观察结果显示,热聚集体颗粒大小均随着加热温度的升高而增大,未氧化样品聚集体颗粒相对较小且分布均匀,氧化组样品颗粒大小不一、分布不均匀,且氧化程度越高聚集体颗粒越大、数量越少。结果表明,烷过氧自由基氧化显著影响草鱼肌原纤维蛋白的热聚集规律,且能改变热聚集体形貌特征。

关键词: 草鱼;肌原纤维蛋白;烷过氧自由基;蛋白质氧化;热聚集

Abstract: Alkylperoxyl radicals derived from the thermal decomposition of 2,2’-azobis(2-amidinopropane)dihydrochloride (AAPH) at different concentrations were used to oxidize myofibrillar protein from grass carp (Ctenopharyngodon idellus), the thermal stability, surface hydrophobicity, zeta potential, turbidity and average particle size of grass carp myofibrillar protein were determined, and the endogenous fluorescence spectrum and atomic force microscope observation were carried out, and the effect of oxidative modification by alkylperoxyl radicals on its heat-induced aggregation behavior was investigated. The results showed that oxidative modification with low concentration (≤ 1.0 mmol/L) of AAPH enhanced the thermal stability of myofibrillar protein, while the opposite effect was observed with high concentration of AAPH (5.0 mmol/L). With the increase in heating temperature, the surface hydrophobicity, zeta potetial, and turbidity of myofibrillar protein in the control and AAPH-treated groups increased first and then decreased. The intrinsic fluorescence intensity declined with increasing temperature, and a red shift of the fluorescence peak was observed, which was more obvious at higher degree of oxidization. The mean particle size of thermal aggregates increased gradually with increasing temperature in the control and 0.2 mmol/L AAPH-treated groups, while it increased first and then decreased in the 1.0 mmol/L and 5.0 mmol/L AAPH-treated groups. The results of atomic force microscopy (AFM) demonstrated that the particle size of thermal aggregates increased with increasing temperature, and the particle size of the control group was relatively smaller and evenly distributed, while the particle size of the oxidized groups was varying and unevenly distributed. Higher degree of oxidization resulted in bigger particle size and smaller number of particles. This study indicated that alkylperoxyl radical could significantly affect the heat-induced denaturation and aggregation of myofibrillar protein from grass carp, and change the morphological characteristics of thermal aggregates.

Key words: grass carp; myofibrillar protein; alkylperoxyl radical; protein oxidation; heat-induced aggregation

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