食品科学 ›› 2024, Vol. 45 ›› Issue (8): 153-160.doi: 10.7506/spkx1002-6630-20230614-117

• 食品工程 • 上一篇    下一篇

不同高静压的压力处理对豌豆7S、11S球蛋白形成凝胶的影响

王雪艳,李开鑫,李家豪,马玲君,陈芳,胡小松,季俊夫   

  1. (中国农业大学食品科学与营养工程学院,国家果蔬加工工程技术研究中心,北京 100083)
  • 出版日期:2024-04-25 发布日期:2024-05-01
  • 基金资助:
    国家自然科学基金青年科学基金项目(32101983);国家自然科学基金面上项目(32372360)

Effects of Different High Hydrostatic Pressure Treatments on Gel Formation of Pea 7S and 11S Globulins

WANG Xueyan, LI Kaixin, LI Jiahao, MA Lingjun, CHEN Fang, HU Xiaosong, JI Junfu   

  1. (National Engineering Research Center for Fruit and Vegetable Processing, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China)
  • Online:2024-04-25 Published:2024-05-01

摘要: 以豌豆7S、11S球蛋白为研究对象,以100~500 MPa高静压作用10 min诱导形成凝胶,通过测量流变特性、质构特性、持水力评估凝胶性能,再将凝胶溶解在不同溶剂中确定维持凝胶的主要相互作用力,通过扫描电子显微镜观察凝胶的微观结构。结果显示,当压强达到300 MPa时,豌豆7S、11S球蛋白溶液逐渐转变为凝胶状态。当压强持续升高到500 MPa,形成的凝胶变强、质地变硬、持水力提高。11S球蛋白相比于7S具有较弱的凝胶性,但具有较强的持水力(100%)。当两种蛋白按照比例(质量比为1∶2、1∶1、2∶1)混合后,凝胶整体的持水力和强度均显著提高。维持凝胶结构的作用力主要为氢键和疏水相互作用,其次为二硫键和静电相互作用。因此通过改变高静压的参数,可以实现豌豆球蛋白凝胶强度、质地等特性的调控。

关键词: 豌豆球蛋白;高静压;凝胶;流变特性;结构

Abstract: In this study, the rheological and textural properties and water-holding capacity of pea 7S and 11S globulin gels induced by high hydrostatic pressure (HHP) at 100–500 MPa for 10 min were measured. The major interaction forces maintaining gel morphology were determined by dissolving the gels in different solvents. The microscopic structure of the gels was observed using scanning electron microscopy (SEM). The results showed that after HHP treatment at 300 MPa, pea 7S and 11S globulin solutions gradually turned into gels. When the pressure continued to increase to 500 MPa, the formed gels exhibited higher strength, harder texture and higher water-holding capacity. The 11S globulin had weaker gel-forming ability, but higher water-holding capacity (100%) compared with 7S. Furthermore, the overall water-holding capacity and gel strength of 7S–11S mixed gels (in mass ratios of 1:2, 1:1 and 2:1) were significantly improved compared with those of the neat gels. The major forces that maintain the gel structure were hydrogen bonds and hydrophobic interaction, followed by disulfide bonds and electrostatic interaction. Therefore, by changing HHP conditions, the strength and texture of pea globulin gels could be controlled.

Key words: pea globulin; high hydrostatic pressure; gel; rheological properties; structure

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