食品科学 ›› 2020, Vol. 41 ›› Issue (4): 15-22.doi: 10.7506/spkx1002-6630-20181022-229

• 食品化学 • 上一篇    下一篇

不同种类肉肌浆蛋白的油-水界面性质

杜菲菲,吴长玲,方艾虎,张莉,李震,杨宗韫,周楠,李鹏鹏,李典昭,王鹏   

  1. (南京农业大学 肉品加工与质量控制教育部重点实验室,江苏 南京 210095)
  • 出版日期:2020-02-25 发布日期:2020-03-02
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2018YFD0401203);中央高校基本科研业务费专项(KYZ201652)

Oil-Water Interfacial Properties of Sarcoplasmic Proteins in Meat from Different Animal Species

DU Feifei, WU Changling, FANG Aihu, ZHANG Li, LI Zhen, YANG Zongyun, ZHOU Nan, LI Pengpeng, LI Dianzhao, WANG Peng   

  1. (Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing Agricultural University, Nanjing 210095, China)
  • Online:2020-02-25 Published:2020-03-02

摘要: 为解释肌浆蛋白的蛋白结构(疏水性、分子柔性等)-界面吸附中构象动态变化-体系能量三者的科学联系,进一步挖掘肌浆蛋白的功能性,以猪肉、鱼肉、鸡肉为原料(根据所占胴体的比例及研究价值确定原料肉),通过测定其氨基酸组成、重要理化指标、蛋白质构象、乳化性质以及界面性质,探究不同肉类(畜、禽、鱼)肌浆蛋白的油-水界面性质,以及各指标之间的内在联系。结果表明:鸡肉肌浆蛋白中苯丙氨酸和酪氨酸含量较高,其粒径与表面疏水性也显著高于猪肉与鱼肉肌浆蛋白(P<0.05);在相同时间下,猪肉肌浆蛋白与鸡肉肌浆蛋白的蛋白构象峰值变化速率无显著差异(P>0.05),而鱼肉肌浆蛋白峰值变化速率相比较显著较慢(P<0.05);与猪肉和鸡肉肌浆蛋白相比,鱼肉肌浆蛋白的界面扩散速率显著较快(P<0.05),但鸡肉与猪肉肌浆蛋白之间的扩散速率无显著性差异(P>0.05);猪肉肌浆蛋白乳化活性稍低于鸡肉(P>0.05),但是鱼肉肌浆蛋白乳化活性显著低于猪肉和鸡肉肌浆蛋白(P<0.05),3 种肌浆蛋白中鱼肉肌浆蛋白的乳化稳定性显著最差(P<0.05)。主成分分析表明,从总体上看,猪鸡肉肌浆蛋白的性质较为相近,二者与鱼肉肌浆蛋白有较大差异;肌浆蛋白的乳化活性和乳化稳定性与其表面疏水性、电位和构象变化速率相关性较强,而扩散速率与溶解度具有较强相关性。

关键词: 肌浆蛋白, 氨基酸组成, 蛋白构象, 界面性质, 乳化性质

Abstract: In order to explain the relationship between the structural properties (such as hydrophobicity and molecular flexibility), dynamic conformational changes during interfacial adsorption and system energy of sarcoplasmic proteins, and more broadly, to understand their functions, sarcoplasmic proteins were extracted from pork, fish and chicken meat and evaluated for amino acid composition, some important physicochemical properties, conformation, emulsifying properties and oil-water interfacial properties. The results showed that chicken sarcoplasmic protein had higher contents of phenylalanine and tyrosine as well as significantly higher particle size and surface hydrophobicity than pork and fish sarcoplasmic proteins (P < 0.05). There was no significant difference in the rate of conformational change within the same time period between pork and chicken sarcoplasmic proteins (P > 0.05), but the rate of conformational change was significantly slower in fish sarcoplasmic protein (P < 0.05). Compared with pork and chicken sarcoplasmic proteins, the interfacial diffusion rate of fish sarcoplasmic protein was significantly higher (P < 0.05) but no significant difference was seen between chicken and pork sarcoplasmic protein (P > 0.05). The emulsifying activity of fish sarcoplasmic protein was significantly lower than that of pork and chicken sarcoplasmic protein (P < 0.05), but the emulsifying activity of pork sarcoplasmic protein was only slightly lower than that of chicken sarcoplasmic protein (P > 0.05). The emulsifying stability of fish sarcoplasmic protein was the lowest among the three sarcoplasmic proteins (P < 0.05). Principal component analysis showed that pork and chicken meat sarcoplasmic proteins had similar properties, which were significantly different from those of fish muscle sarcoplasmic protein. The emulsifying activity and emulsion stability of sarcoplasmic proteins were strongly correlated with the surface hydrophobicity, zeta potential and conformational change rate, and the diffusion rate was strongly correlated with the solubility.

Key words: sarcoplasmic protein, amino acid composition, protein conformation, interfacial properties, emulsifying properties

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