食品科学 ›› 2025, Vol. 46 ›› Issue (22): 145-156.doi: 10.7506/spkx1002-6630-20250610-069

• 基础研究 • 上一篇    下一篇

不同盐离子对转谷氨酰胺酶交联大豆分离蛋白凝胶特性的提升机制

曾祥权,彭琳琳,赵美婷,李英燕,曹瑞,刘梦萱,刘思嵘,李健   

  1. (1.北京工商大学食品与健康学院,国家市场监督管理总局技术创新中心(动物替代蛋白),北京 100071;2.北京工商大学食品与健康学院,老年营养与健康教育部重点实验室,北京 100048)
  • 发布日期:2025-11-21
  • 基金资助:
    农业科技重大项目

Mechanisms of Action of Different Salt Ions in Improving the Gel Properties of Transglutaminase Cross-Linked Soybean Protein Isolate

ZENG Xiangquan, PENG Linlin, ZHAO Meiting, LI Yingyan, CAO Rui, LIU Mengxuan, LIU Sirong, LI Jian   

  1. (1. Technology Innovation Center of Animal Alternative Protein, State Administration for Market Regulation, School of Food and Health, Beijing Technology and Business University, Beijing 100071, China; 2. Key Laboratory of Geriatric Nutrition and Health, Ministry of Education, School of Food and Health, Beijing Technology and Business University, Beijing 100048, China)
  • Published:2025-11-21

摘要: 本研究系统探究了不同盐离子对转谷氨酰胺酶(transglutaminase,TG)交联的大豆分离蛋白(soybean isolate protein,SPI)凝胶形成的影响及其作用机制。结果表明,0.1 mol/L Na+、K+和Mg2+处理可诱导生成具有高凝胶强度和持水力(water-holding capacity,WHC)的SPI凝胶,且凝胶强度与对照组相比分别提升2.43、1.51、2.32 倍。根据流变学分析,盐离子处理组的SPI凝胶储能模量(G’)和损耗模量(G”)均显著高于对照组,且表现出轻微的频率依赖性。分子对接实验显示盐离子可能通过直接影响TG交联后的SPI结构以促进其凝胶特性提升。具体而言,处理组的表面疏水性和荧光强度均有所下降,Zeta电位绝对值和平均粒径显著升高,表明不同盐离子可促进蛋白分子的聚集,使空间结构更加紧凑。傅里叶变换红外光谱结果进一步揭示,Na+、K+和Mg2+可诱导SPI凝胶中β-折叠含量增加,而α-螺旋和无规卷曲含量减少,说明蛋白质二级结构趋于有序化。低场核磁共振和核磁成像的数据表明,盐离子处理降低了SPI凝胶中水分的流动性,与处理组具有更高WHC的结果一致。此外,盐离子处理SPI凝胶微观结构呈现致密的堆叠聚集体的表观形貌特征。因此,Na+、K+和Mg2+在提升TG交联SPI凝胶食品加工过程中的凝胶特性方面具有一定潜力。

关键词: 大豆分离蛋白;转谷氨酰胺酶;盐离子;凝胶强度;蛋白二级结构

Abstract: This study aimed to systematically investigate the effects of different salt ions on the formation of transglutaminase (TG) cross-linked soybean isolate protein (SPI) gels and the underlying mechanisms. Our results showed that treatments with 0.1 mol/L Na+, K+ and Mg2+ induced the formation of SPI gels with high gel strength and water-holding capacity (WHC), and the gel strength of the treated groups was 2.43, 1.51 and 2.32-fold higher than that of the control group, respectively. According to rheological analysis, the storage modulus (G’) and loss modulus (G”) of the salt ion-treated groups were significantly higher than those of the control group, which exhibited a slight frequency dependence. Molecular docking analysis showed that salt ions might directly affect the structure of TG cross-linked SPI to improve its gel properties. Specifically, the surface hydrophobicity and fluorescence intensity of the three treated groups remarkably decreased, while the absolute value of the zeta potential and average particle size increased significantly, indicating that different salt ions could promote the aggregation of protein molecules, causing the spatial structure to become more compact. Fourier transform infrared spectroscopy (FTIR) revealed that the three salt ions could induce an increase in the content of β-folding in SPI gels and a decrease in the contents of α-helix and random coil, suggesting that the secondary structure tended to become ordered after treatment with salt ions. The results of low-field nuclear magnetic resonance (LF-NMR) and magnetic resonance imaging (MRI) confirmed that salt ion treatments reduced the mobility of water in SPI gels, which was consistent with increasing the WHC. Besides, the microstructure of salt ion-treated SPI gels exhibited the morphological features of dense stacked aggregates. Therefore, Na+, K+ and Mg2+ have potential in enhancing the gel properties of TG cross-linked SPI gels during food processing.

Key words: soybean isolate protein; transglutaminase; salt ions; gel strength; protein secondary structure

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