食品与发酵工业 >

2021 , Vol. 47 >Issue 24: 179 - 186

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.027285

生产与科研应用

腌制方式对牛肉肌原纤维蛋白特性及水分分布的影响

  • 高子武 ,
  • 吴丹璇 ,
  • 王恒鹏 ,
  • 吴鹏 ,
  • 屠明亮 ,
  • 许志诚 ,
  • 孟祥忍
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  • 1(扬州大学 旅游烹饪学院,江苏 扬州,225127)
    2(江苏省淮扬菜产业化工程中心,江苏 扬州,225127)
硕士研究生(孟祥忍教授为通讯作者,E-mail:xrmeng@yzu.edu.cn)

收稿日期: 2021-03-11

  修回日期: 2021-04-01

  网络出版日期: 2022-01-21

基金资助

江苏省社会科学基金项目(17GLD021);扬州市“绿扬金凤计划”领军人才资助项目;扬州大学研究生科研与实践创新计划资助项目(kycxyl202003)

收起

Effects of curing process on myofibrillar protein characteristics and water distribution of beef

  • GAO Ziwu ,
  • WU Danxuan ,
  • WANG Hengpeng ,
  • WU Peng ,
  • TU Mingliang ,
  • XU Zhicheng ,
  • MENG Xiangren
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  • 1(College of Tourism and Cooking, Yangzhou University, Yangzhou 225127, China)
    2(Huaiyang Cuisine Engineering Center, Yangzhou 225127, China)

Received date: 2021-03-11

  Revised date: 2021-04-01

  Online published: 2022-01-21

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摘要

为探究不同腌制方式下牛肉水分分布及其肌原纤维蛋白特性的变化规律,以未腌制牛肉为空白对照,分别采用静置腌制、真空滚揉腌制及超声波辅助腌制3种方式对牛肉进行腌制处理,测定肌原纤维蛋白的表面疏水性、总巯基、羰基、二级结构、水分分布并进行十二烷基硫酸钠聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)分析。结果表明,超声波辅助腌制牛肉肌原纤维蛋白表面疏水性低于其他2种腌制方式处理组;真空滚揉腌制牛肉肌原纤维蛋白总巯基含量最低,羰基含量最高,蛋白氧化程度最高;相比于对照组,真空滚揉腌制牛肉肌原纤维蛋白中α-螺旋结构含量显著降低(P<0.05),β-折叠结构含量显著增加(P<0.05)。超声波辅助腌制40 min时肌原纤维蛋白β-折叠结构含量最低,仅为15.47%,宏观表现为嫩度更佳;SDS-PAGE凝胶电泳显示,真空滚揉和超声波辅助腌制牛肉肌原纤维蛋白在10~26 kDa处条带呈现加深,43~95 kDa处条带呈现模糊且肌球蛋白重链处有轻微扩散现象,表明蛋白发生降解;低场核磁共振结果显示,真空滚揉腌制和超声波辅助腌制处理的牛肉结合水及不易流动水弛豫峰面积明显高于未腌制及静置腌制牛肉(P<0.05),且随着超声波腌制时间的延长,牛肉自由水弛豫峰面积显著降低(P<0.05),保水性进一步增强。以上指标表明,在腌制过程中,超声波和真空滚揉会促进牛肉肌原纤维蛋白的氧化降解,且超声波辅助腌制更有利于增强牛肉的保水性,从而改善牛肉嫩度。

关键词： 腌制方式; 牛肉; 肌原纤维蛋白; 蛋白特性; 水分分布

本文引用格式

高子武 , 吴丹璇 , 王恒鹏 , 吴鹏 , 屠明亮 , 许志诚 , 孟祥忍 . 腌制方式对牛肉肌原纤维蛋白特性及水分分布的影响[J]. 食品与发酵工业, 2021 , 47(24) : 179 -186 . DOI: 10.13995/j.cnki.11-1802/ts.027285

Abstract

In order to explore water distribution and myofibrillar protein characteristics of beef under different curing process, the beef was cured by static curing, vacuum tumbling curing and ultrasonic-assisted curing, respectively and the surface hydrophobicity, total sulfhydryl, carbonyl, secondary structure and water distribution of myofibrillar protein were determined, and polyacrylamide gel electrophoresis (SDS-PAGE) was used to analyze it. The results showed that the surface hydrophobicity of ultrasound-assisted curing was lower than that of the other two curing process. The contents of the total sulfhydryl group was the lowest and the content of carbonyl group was the highest in vacuum tumbling curing, and the degree of protein oxidation was the highest. Compared with the control group, the content of α-helix structure in myofibrillar protein of vacuum tumbling curing beef decreased significantly (P<0.05), while the content of β-sheet structure increased significantly (P<0.05). After ultrasonic-assisted curing for 40 min, the content of myofibrillar β-sheet structure was only 15.47%, and the macroscopic tenderness was better. SDS-PAGE gel electrophoresis patterns showed that the myofibrillar protein bands of vacuum tumbling and ultrasound-assisted cured beef were clear at 10-26 kDa, while the band at 43-95 kDa was blurred and slightly diffused at myosin heavy chain which indicating protein degradation. The results of low-field nuclear magnetic resonance (LF-NMR) showed that the area of relaxation peak of binding water and non-flowing water of beef cured by vacuum tumbling and ultrasonic wave were significantly higher than those of uncured and static cured beef (P<0.05). With the extension of ultrasonic curing time, the area of free water relaxation peak of beef was significantly decreased (P<0.05), and water retention was further enhanced. Above indexes showed that in the curing process, ultrasonic and vacuum tumbling could promote the oxidative degradation of beef myofibrillar protein, and ultrasonic-assisted curing was more beneficial to improve the water retention and tenderness of beef.

Key words： curing processing; beef; myofibrillar protein; protein characteristics; water distribution

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