华南理工大学学报(自然科学版) ›› 2012, Vol. 40 ›› Issue (5): 115-120.

• 食品科学与技术 • 上一篇    下一篇

冻藏对面筋蛋白二级结构的影响

刘国琴 阎乃珺 赵雷 李琳 李冰 杨晓泉   

  1. 华南理工大学 轻工与食品学院,广东 广州 510640
  • 收稿日期:2011-11-28 修回日期:2011-12-31 出版日期:2012-05-25 发布日期:2012-03-31
  • 通信作者: 刘国琴(1962-) ,女,博士,教授,主要从事油脂与植物蛋白研究. E-mail:liuguoqin2009@126.com
  • 作者简介:刘国琴(1962-) ,女,博士,教授,主要从事油脂与植物蛋白研究.
  • 基金资助:

    国家自然科学基金重点项目( 31130042) ; 广东省科技计划项目( 2010B050600003, 2010B031700014) ; 国家自然科学基金资助项目( 20976036)

Effect of Frozen Storage on Secondary Structure of Gluten Proteins

Liu Guo-qin  Yan Nai-jun  Zhao Lei  Li Bing  Li Lin  Yang Xiao-quan   

  1. School of Light Industry and Food Sciences,South China University of Technology,Guangzhou 510640,Guangdong,China
  • Received:2011-11-28 Revised:2011-12-31 Online:2012-05-25 Published:2012-03-31
  • Contact: 刘国琴(1962-) ,女,博士,教授,主要从事油脂与植物蛋白研究. E-mail:liuguoqin2009@126.com
  • About author:刘国琴(1962-) ,女,博士,教授,主要从事油脂与植物蛋白研究.
  • Supported by:

    国家自然科学基金重点项目( 31130042) ; 广东省科技计划项目( 2010B050600003, 2010B031700014) ; 国家自然科学基金资助项目( 20976036)

摘要: 采用圆二色谱法表征了不同冻藏模式和冻藏时间对小麦面筋蛋白二级结构的影响.结果表明: 在SDS 溶液中,未经冻藏的面筋蛋白二级结构主要由β 折叠和无规则卷曲组成; 当冻藏时间小于60 天时,两种冻藏模式对小麦面筋蛋白的二级结构影响不大; 恒温冻藏模式中面筋蛋白二级结构在冻藏90 天时变化最显著,易溶部分中α 螺旋转化为β 折叠和β 转角,难溶部分中β 折叠和β 转角转化为α 螺旋和无规则卷曲; 冻融冻藏模式中面筋蛋白二级结构在冻藏60 天时变化最显著,易溶部分中α 螺旋转化为β 折叠和无规则卷曲,难溶部分中β 折叠和β 转角转化为α 螺旋和无规则卷曲.这说明,在恒温冻藏模式下,只有当冻藏时间达到或超过90 天的时候,才对面筋蛋白的二级结构产生影响,而在冻融模式下,冻藏时间仅为60 天时便可对面筋蛋白的二级结构产生影响.

关键词: 冻藏, 面筋蛋白, 二级结构, 圆二色谱法

Abstract:

This paper deals with the influences of frozen mode and frozen time on the secondary structure of wheat gluten proteins by means of circular dichroism spectroscopy. The results show that the secondary structure of the non-frozen gluten proteins in SDS solution is mainly composed of β sheets and random coils,that the two adopted frozen storage modes have no obvious effect on the secondary structure of the gluten proteins when the frozen time is less than 60 d,and that,in the thermostatic frozen storage mode,the secondary structure obviously changes after a storage for 90 d,the α helixes of the soluble gluten proteins turn into β sheets and β turns,and the β sheets and the β turns of the insoluble gluten proteins turn into α helixes and random coils. However,in the freeze-thaw storage mode,the secondary structure significantly changes after a storage for 60 d,the α helixes of the soluble gluten proteins turn into β sheets and random coils,and the β sheets and the β turns of the insoluble gluten proteins turn into α helixes and random coils. Thus,it is concluded that,in the thermostatic frozen storage mode,the secondary structure of the gluten proteins changes only when the frozen time is equal to or greater than 90 d,while in the
freeze-thaw storage mode,the storage only for 60 d may affect the secondary structure.

Key words: frozen storage, gluten protein, secondary structure, circular dichroism spectroscopy