食品科学 ›› 2023, Vol. 44 ›› Issue (13): 23-31.doi: 10.7506/spkx1002-6630-20220624-269

• 食品工程 • 上一篇    下一篇

不同超声波功率处理对类PSE鸡肉肌原纤维蛋白结构和乳化稳定性的影响

李可,张俊霞,王欣瑶,王昱,杜曼婷,吴楠,赵颖颖,白艳红   

  1. (郑州轻工业大学食品与生物工程学院,河南省冷链食品质量安全控制重点实验室,食品生产与安全河南省协同创新中心,河南 郑州 450001)
  • 出版日期:2023-07-15 发布日期:2023-08-11
  • 基金资助:
    国家自然科学基金面上项目(32072243);河南省优秀青年科学基金项目(222300420092); 河南省留学人员科研择优资助项目(2022038);河南省高等学校青年骨干教师培养计划项目(2019GGJS128); 河南省大学生创新创业训练计划项目(202210462071)

Effects of Ultrasound Treatment at Different Powers on the Structure and Emulsifying Properties of PSE-Like Chicken Myofibrillar Protein

LI Ke, ZHANG Junxia, WANG Xinyao, WANG Yu, DU Manting, WU Nan, ZHAO Yingying, BAI Yanhong   

  1. (Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Henan Province Collaborative Innovation Center for Food Production and Safety, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China)
  • Online:2023-07-15 Published:2023-08-11

摘要: 以类PSE(pale, soft and exudative,PSE)鸡肉肌原纤维蛋白(myofibrillar protein,MP)为研究对象,研究不同超声波功率(20 kHz,6 min,0、150、300、450 W和600 W)处理对其结构、理化性质和乳化稳定性的影响。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)结果显示不同超声功率处理后MP的组成成分未发生明显改变,然而,超声功率为450 W和600 W时肌球蛋白重链和肌动蛋白的条带强度显著增加。随着超声功率增加至450 W时,MP的α-螺旋相对含量、表面疏水性和溶解度增加,β-折叠相对含量降低(P<0.05)。600 W时MP的α-螺旋相对含量、表面疏水性和溶解度有所下降,但仍显著高于对照组(P<0.05)。随着超声功率的增加,MP的荧光强度增大,MP和MP乳液的平均粒径和Zeta-电位都显著降低(P<0.05);当超声功率为600 W时,MP的乳化活性指数和乳化稳定性指数最高,油-水界面张力最小,Turbiscan稳定性指数最低,表明超声功率为600 W时MP制备的乳液最稳定;冷场发射扫描电子显微镜观察结果也证实此时乳液油滴小而均匀。综上所述,超声波处理可改变类PSE鸡肉MP的结构和理化性质,有效提高其乳化稳定性。

关键词: 类PSE鸡肉;肌原纤维蛋白;超声波;结构特性;乳化特性

Abstract: The effects of ultrasound treatment at different powers (20 kHz for 6 min; 0, 150, 300, 450 and 600 W) on the structure, physicochemical properties and emulsifying properties of pale, soft and exudative-like (PSE-like) chicken meat myofibrillar protein (MP) were investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed no significant changes in the composition of MP after ultrasound treatments; however, the band intensities of myosin heavy chain and actin were significantly increased at ultrasonic power of 450 and 600 W (P < 0.05). The α-helix content, surface hydrophobicity and solubility of MP increased and the β-fold content decreased as the ultrasonic power increased to 450 W. The α-helix content, surface hydrophobicity and solubility of MP decreased at 600 W ultrasonic power, but they were still significantly higher than those of the control group (P < 0.05). With an increase in ultrasound power, the fluorescence intensity of MP increased, and the particle size and zeta potential of MP and MP emulsion decreased significantly (P < 0.05). At ultrasonic power of 600 W, the highest emulsification activity index (EAI) and emulsion stability index (ESI) of MP, and the lowest oil/water interfacial tension and Turbiscan stability index of MP emulsion were obtained, indicating the highest emulsion stability. The cold field emission scanning electron micrograph confirmed that the oil droplets of the emulsion were smaller and more uniform. In summary, ultrasonic treatment can change the structure and physicochemical properties of PSE-like chicken MP, in turn improving the emulsion stability.

Key words: pale, soft and exudative-like chicken; myofibrillar protein; ultrasound; structural properties; emulsifying properties

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