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中国精品科技期刊2020
冯佳雯,郑云芳,张芳,等. 超声处理对鲈鱼肌原纤维蛋白结构和功能特性的影响[J]. 食品工业科技,2022,43(17):95−103. doi: 10.13386/j.issn1002-0306.2021120027.
引用本文: 冯佳雯,郑云芳,张芳,等. 超声处理对鲈鱼肌原纤维蛋白结构和功能特性的影响[J]. 食品工业科技,2022,43(17):95−103. doi: 10.13386/j.issn1002-0306.2021120027.
FENG Jiawen, ZHENG Yunfang, ZHANG Fang, et al. Effect of Ultrasonic Treatment on the Structure and Functional Properties of Myofibrillar Protein in Sea Bass[J]. Science and Technology of Food Industry, 2022, 43(17): 95−103. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021120027.
Citation: FENG Jiawen, ZHENG Yunfang, ZHANG Fang, et al. Effect of Ultrasonic Treatment on the Structure and Functional Properties of Myofibrillar Protein in Sea Bass[J]. Science and Technology of Food Industry, 2022, 43(17): 95−103. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021120027.

超声处理对鲈鱼肌原纤维蛋白结构和功能特性的影响

Effect of Ultrasonic Treatment on the Structure and Functional Properties of Myofibrillar Protein in Sea Bass

  • 摘要: 本文以鲈鱼(Lateolabrax maculatus)肌原纤维蛋白为原料,研究了不同超声功率(0~540 W)和时间(0~12 min)对鲈鱼肌原纤维蛋白结构及功能特性的影响。结果显示,随着超声功率和时间的增加,肌原纤维蛋白的巯基含量总体减少,紫外吸光度增大,其α-螺旋含量减少,β-折叠、β-转角和无规卷曲的含量增加。180~450 W的超声处理使肌原纤维蛋白的粒径和浊度减小,溶解度提高。超声处理改善了肌原纤维蛋白的流变特性,提高了热诱导凝胶过程的G’和G”。主成分和聚类分析表明不同超声功率和时间对肌原纤维蛋白的理化性质有较大的影响。结果表明,超声处理会使鲈鱼肌原纤维蛋白的结构发生改变,从而影响流变特性,有利于提供更好的功能特性。

     

    Abstract: In this paper, sea bass (Lateolabrax maculatus) were uesd as raw material to study the effect of ultrasound on the structure and functional properties of myofibrillar proteins in sea bass by the different ultrasonic power in the range of 0~540 W and time at 0~12 min. The results showed that, with the extension of the ultrasonic time and power, the sulfhydryl content of myofibrillar protein decreased, while the UV absorbance increased, and the α-helix content had a tendency to transform into β-sheets, β-turns and random coils. Ultrasound at 180~450 W, particle size and turbidity of myofibrillar protein were reduced, the solubility was improved. Ultrasonic treatment improved the rheological properties of myofibrillar and increased the G' and G" in the thermally induced gel process. Principal component and cluster analysis showed that different ultrasonic power and time had a greater impact on the physical and chemical properties of myofibrillar protein. These findings suggested that ultrasound altered the structure of myofibrillar proteins in sea bass, which affected rheological properties and contributed to better functional performance.

     

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