食品科学 ›› 2020, Vol. 41 ›› Issue (4): 67-73.doi: 10.7506/spkx1002-6630-20190306-076

• 食品化学 • 上一篇    下一篇

工业改性对大豆蛋白结构及大豆蛋白-肌原纤维蛋白复合凝胶的影响

贾子璇,冉安琪,刘季善,李杨,王中江,江连洲   

  1. (1.东北农业大学食品学院,黑龙江 哈尔滨 150030;2.山东万得福实业集团有限公司,山东 东营 257000)
  • 出版日期:2020-02-25 发布日期:2020-03-02
  • 基金资助:
    山东省泰山产业领军人才工程高效生态农业创新类项目(LJNY201607); 中国博士后科学基金面上资助项目(2018M641798);黑龙江省自然科学基金项目(C2018024)

Effect of Industrial Modifications on Soybean Protein Structure and the Texture and Microstructure of Soybean Protein-Myofibrillar Protein Hybrid Gels

JIA Zixuan, RAN Anqi, LIU Jishan, LI Yang, WANG Zhongjiang, JIANG Lianzhou   

  1. (1. College of Food Science, Northeast Agricultural University, Harbin 150030, China;2. Shandong Wandefu?Industrial Group, Dongying 257000, China)
  • Online:2020-02-25 Published:2020-03-02

摘要: 采用工业热改性、工业碱改性、工业糖基化改性、工业氧化改性4 种方法对大豆分离蛋白(soybean protein isolate,SPI)进行改性处理,研究其对SPI结构的影响,进而探讨改性蛋白与肌原纤维蛋白(myofibrillar protein,MP)制成的复合凝胶的质构特性及凝胶特性。结果表明:4 种工业改性对SPI亚基组成并未造成显著影响,但是均减少了SPI的α-螺旋和无规卷曲结构相对含量,并增加了β-折叠与β-转角结构相对含量;工业热改性、工业碱改性、工业糖基化改性处理显著增加了SPI的二硫键含量并降低了SPI的游离巯基含量,而工业氧化改性显著降低了SPI的二硫键含量(P<0.05),且4 种工业改性处理均改变了SPI的二硫键构型;4 种工业改性蛋白的酪氨酸残基均趋向于“暴露式”,工业热改性、工业碱改性、工业糖基化改性处理使色氨酸残基趋向于“暴露”态,而工业氧化改性导致氧化蛋白聚集使色氨酸残基被包埋。SPI-MP复合凝胶的质构特性结果表明,工业热改性、工业碱改性、工业糖基化改性3 种改性SPI与MP形成的复合凝胶硬度、弹性等质构特性均显著优于对照SPI(P<0.05),而工业氧化改性SPI形成的混合凝胶除黏结性外各项质构特性均差于对照SPI。观察SPI-MP复合凝胶扫描电镜图可知,工业热改性、工业碱改性、工业糖基化改性SPI形成的复合凝胶更加致密均匀,工业氧化改性SPI与MP形成的复合凝胶粗糙多孔。

关键词: 工业改性大豆分离蛋白, 肌原纤维蛋白, 结构特性, 凝胶性

Abstract: In this study, four industrial modification methods including heat treatment, alkali treatment, glycosylation and oxidation were applied to modify soybean protein isolate (SPI) to investigate their effects on the structure of SPI. The texture and microstructure of the hybrid gels of the modified soybean protein and myofibrillar protein (MP) were further investigated. The results showed that the four industrial modifications did not have a significant effect on the subunit composition of SPI, but they reduced the contents of α-helix and random coil structures and increased the contents of β-sheet and β-turn. Industrial oxidation significantly reduced the disulfide bond content of SPI, while the other treatments significantly increased the disulfide bond content and reduced the free sulfhydryl group content of SPI (P < 0.05); all four treatments changed the disulfide bond configuration of SPI. Tyrosine residues of SPI modified by each method tended to be exposed outside, and tryptophan residues were buried inside after oxidation but were exposed outside after the other modifications. The texture characteristics of SPI-MP hybrid gel showed that the hardness, elasticity, adhesion, and chewiness of the hybrid gels with heat, alkali and glycosylation modification were significantly better than those of the control SPI (P < 0.05). All texture characteristics except cohesiveness of the hybrid gel with oxidized SPI were poorer than those of the control SPI. Under scanning electron microscopy, it was seen that the oxidized SPI-MP hybrid gel was rough and porous, while the hybrid gels with the other industrial modifications were more dense and uniform.

Key words: industrial modified soybean protein isolate, myofibrillar protein, structural properties, gel properties

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