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中国精品科技期刊2020
李京九,宋明菲,牛越,等. 超高压处理过程中卤鸭腿肌原纤维蛋白结构变化[J]. 食品工业科技,2025,46(2):1−8. doi: 10.13386/j.issn1002-0306.2024030285.
引用本文: 李京九,宋明菲,牛越,等. 超高压处理过程中卤鸭腿肌原纤维蛋白结构变化[J]. 食品工业科技,2025,46(2):1−8. doi: 10.13386/j.issn1002-0306.2024030285.
LI Jingjiu, SONG Mingfei, NIU Yue, et al. Structural Changes of Myofibrillar Proteins in Marinated Duck Drumsticks during High Pressure Processing Treatment[J]. Science and Technology of Food Industry, 2025, 46(2): 1−8. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024030285.
Citation: LI Jingjiu, SONG Mingfei, NIU Yue, et al. Structural Changes of Myofibrillar Proteins in Marinated Duck Drumsticks during High Pressure Processing Treatment[J]. Science and Technology of Food Industry, 2025, 46(2): 1−8. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024030285.

超高压处理过程中卤鸭腿肌原纤维蛋白结构变化

Structural Changes of Myofibrillar Proteins in Marinated Duck Drumsticks during High Pressure Processing Treatment

  • 摘要: 为探究超高压处理对卤鸭腿嫩度的改善机制,本研究通过测定表面疏水性、巯基含量、化学作用力、二级结构、微观结构等指标,分析了超高压处理(400 MPa,15 min)过程中肌原纤维蛋白结构的变化规律。结果表明,肌原纤维蛋白表面疏水性先上升后下降,在处理12 min时达到最大值51.03。总巯基含量在处理15 min后下降了40.6%,而游离巯基含量上升了42.7%,二硫键显著(P<0.05)增加了189.2%。色氨酸和酪氨酸基团暴露。以上变化表明蛋白三级结构发生改变。超高压处理15 min后,肌原纤维蛋白α-螺旋含量从20.63%减少到13.45%,无规则卷曲含量从23.93%增加到28.67%,说明蛋白二级结构重排。SDS-PAGE电泳和扫描电镜结果分别显示,超高压处理后的肌原纤维蛋白发生解聚,颗粒尺寸明显减小且分布更加均匀。综上所述,在超高压处理过程中,鸭腿肌原纤维蛋白的三级结构、二级结构和微观结构均发生了明显变化,这有利于提高鸭肉嫩度。该研究为超高压技术在肉制品嫩度改善的应用提供了理论基础。

     

    Abstract: To investigate the improvement mechanism of ultra-high pressure treatment on the tenderness of marinated duck drumsticks, this study analyzed the pattern of structural changes of myofibrillar proteins during high pressure processing (400 MPa, 15 min) by determining the surface hydrophobicity, sulfhydryl content, chemical force, secondary structure and microstructure. The results showed that the hydrophobicity of myofibrillar proteins initially increased and then decreased, reaching a maximum of 51.03 after 12 minutes of treatment. The total thiol content decreased by 40.6% after 15 minutes of treatment, while the free thiol content increased by 42.7%, and disulfide bonds significantly (P<0.05) increased by 189.2%. Tryptophan and tyrosine residues were exposed, indicating changes in protein tertiary structure. After 15 min of HPP treatment, the α-helix content of myofibrillar protein decreased from 20.63% to 13.45%, and the content of irregular coils increased from 23.93% to 28.67%, suggesting rearrangement of the protein secondary structure. SDS-PAGE electrophoresis and scanning electron microscopy results demonstrated protein depolymerization of high pressure processing treatment, significant reduction in particle size, and more uniform distribution. In conclusion, during high-pressure processing, significant changes occur in the tertiary structure, secondary structure, and microstructure of duck leg myofibrillar proteins, contributing to the improvement of duck meat tenderness. This study would provide a theoretical basis for the application of high-pressure technology in improving meat tenderness and provides insight into the underlying mechanisms.

     

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