食品科学 ›› 2018, Vol. 39 ›› Issue (21): 59-65.doi: 10.7506/spkx1002-6630-201821009

• 食品工程 • 上一篇    下一篇

高强度超声处理对鹅胸肉肌动球蛋白特性的影响

张 坤1,2,邹 烨1,*,王道营1,*,张新笑1,陈 琳1,诸永志1,徐为民1,3   

  1. 1.江苏省农业科学院农产品加工研究所,江苏 南京 210014;2.南京财经大学食品科学与工程学院,江苏 南京 210046;3.江苏省肉类生产与加工质量安全控制协同创新中心,江苏 南京 210095
  • 出版日期:2018-11-15 发布日期:2018-11-21
  • 基金资助:
    国家自然科学基金面上项目(31571863);现代农业产业技术体系建设专项(CARS-41);江苏省自然科学基金青年基金项目(BK20180300);江苏省苏北科技专项(SZ-XZ2017008);江苏省农业科技自主创新资金项目(CX(15)1008);江苏省高校优势学科建设工程资助项目

Effect of High-Intensity Ultrasound on the Characteristics of Goose Breast Muscle Actomyosin

ZHANG Kun1,2, ZOU Ye1,*, WANG Daoying1,*, ZHANG Xinxiao1, CHEN Lin1, ZHU Yongzhi1, XU Weimin1,3   

  1. 1. Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China; 2. College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210046, China; 3. Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing 210095, China
  • Online:2018-11-15 Published:2018-11-21

摘要: 为了解超声处理对鹅胸肉肌动球蛋白特性的影响,采用高强度超声波(超声频率20 kHz、超声功率800 W、超声总时间42 min、工作时间2 s、停歇时间3 s)对鹅胸肉进行处理,测定鹅胸肉于4 ℃放置不同时间(0、6、12、24、36、48 h)下对照组(未经超声处理)和超声组中肌动球蛋白的紫外吸收光谱、荧光光谱、傅里叶变换红外光谱、圆二色光谱,以及肌动球蛋白的ATPase活力、粒径、Zeta电位、静态流变性、组织蛋白酶活力和超微结构等指标。结果显示:与对照组相比,超声组肌动球蛋白构象发生改变,ATPase活力、蛋白粒径以及静态流变性均明显降低,Zeta电位明显升高,组织蛋白酶B、D、L、H活力均明显升高,蛋白表面微观结构发生明显变化,由完整且有序排列的肌动球蛋白结构变为破碎、无序的蛋白颗粒。因此,超声处理可改变肌动球蛋白的构象,促进肌动球蛋白解离,使肌动球蛋白由大分子聚合物解离为小分子蛋白,本研究为超声嫩化鹅胸肉提供了理论依据。

关键词: 肌动球蛋白, 蛋白二级结构, 酶活力, 蛋白构象

Abstract: This study was performed to investigate changes in the characteristics of goose breast muscle actomyosin treated with high-intensity ultrasound (frequency 20 kHz, power 800 W, total time 42 min, on-time 2 s and off-time 3 s) during freezing storage. Untreated sample was used as a control. The effect of ultrasonic treatment and different storage time (0, 6, 12, 24, 36 and 48 h) at 4 ℃ on goose breast muscle actomyosin was determined by ultraviolet spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy, circular dichroism spectroscopy, ATPase activity, zeta potential, particle size, viscosity, cathepsin activity and scanning electron microscopy. The results showed that ultrasound treatment changed the conformation and significantly reduced the ATPase activity, particle size and viscosity, and significantly increased the zeta potential and cathepsin B, D, L and H activities of actomyosin compared with the control group. Moreover, the surface microstructure significantly changed after ultrasound treatment, transforming the actomyosin structure from complete and ordered arrangement into broken and disordered protein particles. The above findings suggested that ultrasonic treatment could change actomyosin conformation and aid in the dissociation of actomyosin into small molecule proteins, which can provide the theoretical basis for applying ultrasonic treatment to improve goose breast muscle tenderness and quality.

Key words: actomyosin, protein secondary structure, enzyme activity, protein conformation

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