中国农业科学 ›› 2023, Vol. 56 ›› Issue (21): 4318-4329.doi: 10.3864/j.issn.0578-1752.2023.21.014

• 食品科学与工程 • 上一篇    下一篇

不同盐离子对藜麦蛋白凝胶特性及分子间作用力的影响

冯潇(), 武朝升(), 杨玉玲, 付丽霄, 陈龙薇, 汤晓智()   

  1. 南京财经大学食品科学与工程学院/江苏省现代粮食流通与安全协同创新中心/江苏高校粮油质量安全控制及深加工重点实验室,南京 210023
  • 收稿日期:2023-02-06 接受日期:2023-08-18 出版日期:2023-11-01 发布日期:2023-11-06
  • 通信作者:
    汤晓智,E-mail:
  • 联系方式: 冯潇,E-mail:fengxiao@nufe.edu.cn。武朝升,E-mail:wuchaosheng3@163.com。冯潇和武朝升为同等贡献作者。
  • 基金资助:
    国家自然科学基金(32001643); 国家自然科学基金(32372380); 江苏省自然科学基金(BK20200831); 江苏高校优势学科建设工程资助项目(PAPD)

Effects of Different Salt Ions on the Gel Properties and Molecular Interactions of Quinoa Protein

FENG Xiao(), WU ChaoSheng(), YANG YuLing, FU LiXiao, CHEN LongWei, TANG XiaoZhi()   

  1. College of Food Science and Engineering, Nanjing University of Finance and Economics/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory for Quality Safety Control and Deep Processing of Cereals and Oils, Nanjing 210023
  • Received:2023-02-06 Accepted:2023-08-18 Published:2023-11-01 Online:2023-11-06

摘要:

【目的】研究添加不同盐离子对藜麦蛋白凝胶特性的影响,探究盐离子影响凝胶特性的分子机理,为藜麦蛋白凝胶加工提供理论依据。【方法】采用碱提酸沉法提取藜麦蛋白。在pH 7.0条件下制备添加50 mmol∙L-1不同盐离子(NaCl、CaCl2、CaSO4、MgCl2)的藜麦蛋白溶液(20%,w/v)。水浴加热后制备凝胶,测定盐离子对凝胶质构、持水力、色差以及水分分布的影响。通过扫描电镜和流变仪研究不同盐离子对藜麦蛋白凝胶微观结构和流变特性的影响,分析分子间相互作用及其二级结构。【结果】中性条件下,盐离子的加入降低了藜麦蛋白凝胶的硬度和持水力(P<0.05),增强了凝胶的弹性。添加MgCl2的藜麦蛋白凝胶具有最低的硬度和持水力。NaCl对凝胶的色差没有显著影响。相同浓度下,二价盐离子的加入显著提高了凝胶的亮度和白度,CaCl2的加入使凝胶白度从59.62提高至67.80。添加盐离子促进藜麦蛋白的颗粒聚集,使凝胶的网络结构更加粗糙,加入二价盐离子的蛋白凝胶的微观结构表现出更粗糙和更大的缝隙。同时,相较于空白组和添加NaCl的凝胶,添加二价盐离子显著降低了藜麦蛋白凝胶内的二硫键含量,并削弱了凝胶内的静电相互作用。盐离子的加入使蛋白凝胶的β-折叠和β-转角含量降低,α-螺旋结构和无规则卷曲结构含量增加,降低了二级结构的有序性。【结论】在中性条件下,不同盐离子的加入在不同程度上影响藜麦蛋白的凝胶特性和凝胶的微观结构;相同摩尔浓度下,所有二价盐离子比NaCl制备的凝胶微观结构更粗糙,凝胶硬度和持水力更低,主要是因为添加二价盐离子显著降低了藜麦蛋白凝胶内二硫键的含量,并削弱了凝胶内的静电相互作用。

关键词: 藜麦分离蛋白, 蛋白凝胶, 二级结构, 水分分布, 分子间作用力

Abstract:

【Objective】This research studied the effects of different salt ions on the gel properties of quinoa protein, and explored its molecular mechanisms, so as to provide a theoretical basis for the processing of quinoa protein gels.【Method】Quinoa protein was extracted by alkali extraction and acid precipitation. Quinoa protein solution (20%, w/v) was prepared at pH 7.0. NaCl, CaCl2, CaSO4 and MgCl2 was added in quinoa protein solution till the concentration was 50 mmol∙L-1, and then the solution was heated in a water bath to prepare quinoa protein gels. The effects of salt ions on the texture, water retention, color properties and water distribution of quinoa protein gels were analyzed. Meanwhile, the effects of salt ions on the microstructure and rheological properties of quinoa protein gels were studied by scanning electron microscopy and rheometer. The effects of salt ions on the molecular interactions and secondary structure of protein gels were also analyzed.【Result】The addition of salt ions significantly decreased the hardness and water holding capacity, while increased the springiness of quinoa protein gels under pH 7.0. Quinoa protein gels with MgCl2 showed the lowest hardness and water holding capacity. NaCl addition had no significant influence on the color properties of protein gels. However, the addition of bivalent salt ions significantly improved the lightness and whiteness of quinoa protein gels, and their whiteness increased from 59.62 to 67.80 with the addition of CaCl2. Furthermore, the addition of salt ions promoted granular aggregation of quinoa protein, which made the gel network structure become coarse. Coarse and larger gaps were observed in the microstructure of quinoa protein gels when divalent salt ions were added. Meanwhile, compared with blank gels and gels added with NaCl, the addition of divalent salt ions significantly decreased the content of disulfide bond, and weakened the electrostatic interactions within quinoa protein gels. Furthermore, the addition of salt ions decreased the contents of β-sheets and β-turns, increased the contents of α-helix and random coil, which affected the orderliness of protein secondary structure.【Conclusion】Under neutral conditions, the gel properties of quinoa protein and microstructure of gels were affected by the presence of different salt ions to various degrees. Compared with the gel prepared with NaCl, quinoa protein gels with the same concentration of CaCl2, CaSO4, and MgCl2 showed rougher microstructure, lower gel hardness and water holding capacity, as divalent salt ions significantly decreased the disulfide bond content and weakened the electrostatic interactions within quinoa protein gels.

Key words: quinoa protein isolate, protein gels, secondary structure, water distribution, molecular interaction