食品科学 ›› 2026, Vol. 47 ›› Issue (14): 113-125.doi: 10.7506/spkx1002-6630-20260108-068

• 食品化学 • 上一篇    

甲基纤维素与六偏磷酸钠联合作用对大豆分离蛋白凝胶冻融稳定性及结构质地的影响

刘思淼,张宾洋,王浪,朱颖,朱秀清,孙冰玉,刘琳琳,黄雨洋,吕铭守,陈凤莲   

  1. (1.哈尔滨商业大学食品工程学院,黑龙江省食品科学与工程重点实验室,黑龙江省谷物食品与谷物资源综合加工重点实验室,黑龙江?哈尔滨 150076;2.黑龙江谱尼测试科技有限公司,黑龙江?哈尔滨 150029)
  • 发布日期:2026-08-24
  • 基金资助:
    “十四五”国家重点研发计划重点专项(2022YFF1103104)

Effects of Combined Use of Methylcellulose and Sodium Hexametaphosphate on Freeze-Thaw Stability, Structure and Texture of Soy Protein Isolate Gels

LIU Simiao, ZHANG Binyang, WANG Lang, ZHU Ying, ZHU Xiuqing, SUN Bingyu, LIU Linlin, HUANG Yuyang, LÜ Mingshou, CHEN Fenglian   

  1. (1. Key Laboratory of Food Science and Engineering of Heilongjiang Province, Key Laboratory of Grain Food and Comprehensive Processing of Grain Resources of Heilongjiang Province, College of Food Engineering, Harbin University of Commerce, Harbin 150076, China; 2. Heilongjiang Pony Testing Technology Co. Ltd., Harbin 150029, China)
  • Published:2026-08-24

摘要: 本研究探讨冻融循环对大豆分离蛋白(soy protein isolate,SPI)凝胶质地、结构及冻融稳定性的影响,并研究甲基纤维素(methylcellulose,MC)和六偏磷酸钠(sodium hexametaphosphate,SHMP)及其组合对凝胶性能的改善作用。通过制备不同的SPI凝胶,并进行冻融循环处理(0~5 次),采用持水能力、水分分布分析、全质构分析、流变学测定、表面疏水性分析、分子间作用力分析、浊度、粒径及电位分析、傅里叶变换红外光谱和扫描电子显微镜等方法对凝胶的质地、结构和冻融稳定性进行系统研究。结果表明,冻融循环显著降低了SPI凝胶的持水能力,增加了凝胶的硬度和黏性,破坏了凝胶的微观结构,并导致蛋白质分子间作用力和二级结构的变化。添加MC的凝胶表现出较高的持水能力和硬度,但冻融稳定性较差;添加SHMP的凝胶具有较高的冻融稳定性,但对凝胶网络结构的改善不显著。而MC与SHMP的联合作用显著提高了凝胶的持水能力、硬度和弹性,同时增强了凝胶的冻融稳定性。研究表明,MC与SHMP的联合作用能够形成更致密的凝胶网络结构,减少冰晶的形成,降低凝胶网络的破坏程度,为食品工业中大豆蛋白凝胶的应用提供了理论依据。

关键词: 大豆分离蛋白凝胶;冻融稳定性;质构;联合效应

Abstract: This study investigated the effects of freeze-thaw cycles on the texture, structure and freeze-thaw stability of soybean protein isolate (SPI) gels, and examined the improving effects of methylcellulose (MC), sodium hexametaphosphate (SHMP) and their combination on the gel properties of SPI. Different SPI gels were prepared and subjected to zero to five freeze-thaw cycles. Water-holding capacity (WHC), moisture distribution, texture profile analysis (TPA), rheological measurements, surface hydrophobicity, intermolecular forces, turbidity, particle size and zeta potential analysis, Fourier transform infrared (FTIR) spectroscopy, and scanning electron microscopy (SEM) were employed to systematically evaluate gel texture, structure, and freeze-thaw stability. The results showed that freeze-thaw cycles significantly reduced the water-holding capacity of SPI gels, increased their hardness and viscosity, disrupted the microstructure, and induced changes in intermolecular forces and secondary structure. Gels containing MC exhibited higher WHC and hardness but poorer freeze-thaw stability; gels containing SHMP demonstrated better freeze-thaw stability, although the improvement in gel network structure was not significant. The combined addition of MC and SHMP significantly enhanced WHC, firmness, resilience, and freeze-thaw stability. The combined cross-linking effect of MC and SHMP facilitated the formation of a denser gel network, suppressed ice crystal growth, and preserved network integrity. This study provides a theoretical basis for the utilization of soy protein gels in the food industry.

Key words: soy protein isolate gels; freeze-thaw stability; texture; combined effect

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