中国农业科学 ›› 2010, Vol. 43 ›› Issue (22): 4687-4693 .doi: 10.3864/j.issn.0578-1752.2010.22.016

• 贮藏·保鲜·加工 • 上一篇    下一篇

超声波对小麦面筋蛋白结构的影响

张海华,朱科学,周惠明

  

  1. (江南大学食品学院)
  • 收稿日期:2010-06-12 修回日期:2010-09-23 出版日期:2010-11-15 发布日期:2010-11-15
  • 通讯作者: 周惠明

Effect of Ultrasonic on the Structure of Wheat Gluten Protein

ZHANG Hai-hua, ZHU Ke-xue, ZHOU Hui-ming

  

  1. (江南大学食品学院)
  • Received:2010-06-12 Revised:2010-09-23 Online:2010-11-15 Published:2010-11-15
  • Contact: ZHOU Hui-ming

摘要:

【目的】研究超声波对面筋蛋白结构的影响,为超声波处理改善面筋蛋白功能性质提供理论依据。【方法】借助红外光谱、扫描电镜、激光粒径仪了解超声波处理对面筋蛋白二级结构、非共价键、二硫键及显微结构的影响。【结果】超声波处理使面筋蛋白二级结构的α-螺旋结构增加、β-转角结构显著减少,而β-折叠结构则因超声功率不同变化不同;超声波处理破坏了面筋蛋白分子间/内氢键、SS键、疏水键的致密连接,导致面筋蛋白松散的显微结构形成和体积平均粒径的增大。【结论】超声波通过削弱面筋蛋白紧密结构赖以支持的作用力包括SS键、氢键、疏水键,而形成松散的结构。

关键词: 小麦面筋蛋白, 超声波, 红外光谱, SEM, 粒径

Abstract:

【Objective】 The information on the gluten protein structure alterations affected by ultrasonic would provide a theoretical basis for the changes of functional properties under ultrasonic. 【Method】 The secondary structure, inner/intra molecules interaction as well as micro structure of gluten after ultrasonic treatment were studied by using FTIR, SEM and laser particle mastersier 2000. 【Result】 The β-turn percentage of gluten protein significantly decreased while the α-helix percentage increased after ultrasonic under all power levels, but the β-sheet percentage altered as the ultrasonic power level differed. In addition, the SS bond, hydrogen bond and hydrophobic bond among inter/intra molecules were destroyed, which resulted in the formation of incompact structure shown by SEM and indicated by the increase of volume particle size of gluten protein. 【Conclusion】 Ultrasonic reduced the inner/intra molecules interaction among gluten molecules, whereby the incompact structure formed.

Key words: wheat gluten, ultrasonic, FTIR, SEM, particle size