食品科学 ›› 2017, Vol. 38 ›› Issue (23): 1-7.doi: 10.7506/spkx1002-6630-201723001

• 基础研究 •    下一篇

不同谷物麸皮对面团流变学特性及面筋蛋白结构的影响

黄莲燕1,张小爽1,张君慧2,张慧娟1,*,王 静1   

  1. 1.北京市食品添加剂工程技术研究中心,北京食品营养与人类健康高精尖创新中心,北京工商大学,北京 100048;2.中粮营养健康研究院有限公司,北京 102209
  • 出版日期:2017-12-15 发布日期:2017-12-07
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2017YFD0401105);国家自然科学基金青年科学基金项目(31401522); 北京市教委科研类专项科技创新平台项目(19008001226);北京市优秀人才教育资助青年拔尖团队项目; 北京工商大学2017年研究生科研能力提升计划项目

Effect of Different Cereal Brans on Dough Rheological Properties and Gluten Secondary Structure

HUANG Lianyan1, ZHANG Xiaoshuang1, ZHANG Junhui2, ZHANG Huijuan1,*, WANG Jing1   

  1. 1. Beijing Engineering and Technology Research Center of Food Additives, Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University, Beijing 100048, China; 2. Nutrition & Health Research Institute, COFCO Corporation, Beijing 102209, China
  • Online:2017-12-15 Published:2017-12-07

摘要: 本实验选用小麦麸皮、黑小麦麸皮、燕麦麸皮为原材料,探究在高添加量(质量分数30%)情况下不同谷 物麸皮对面团流变学特性、面筋蛋白组成及结构的影响。结果表明,谷物麸皮含有丰富的膳食纤维,麸皮的加入使 面团的吸水率、黏度崩解值显著增加,回生值显著降低,面团的形成时间、稳定时间虽与麸皮种类有关,但整体 均呈上升趋势;添加麸皮的面筋蛋白中麦谷蛋白与麦醇溶蛋白比例增加了24.7%~73.0%、二硫键含量显著下降了 26.0%~35.5%;面筋蛋白中的二级结构以β-折叠为主,小麦麸皮和黑小麦麸皮的加入使得面筋蛋白中的β-转角结构 向β-折叠结构转化;扫描电子显微镜图显示麸皮的加入破坏了面筋蛋白原本均匀致密的微观结构。综上所述,谷物 麸皮的加入改变了面筋蛋白的组成及二级结构,这些变化可能是导致面团流变学特性及面制品品质下降的原因。

关键词: 热机械学特性, 面筋蛋白, 二硫键, 二级结构, 微观结构

Abstract: The effects of a high level (30%, m/m) of different cereal brans (wheat, triticale and oat) added to wheat flour on dough rheological properties, and gluten composition and secondary structure were studied. The results showed that addition of cereal bran, rich in dietary fiber, resulted in a remarkable increase of water-absorbing capacity and breakdown viscosity, a distinct decrease of setback viscosity and in general an increase of dough development time and stability time, which were dependent on cereal varieties. Moreover, an increase in gliadin and glutenin of 24.7%–73.0% and a reduction in disulfide bond content of 26.0%–35.5% were found. β-Sheet was the predominant secondary structure of gluten proteins, and addition of wheat and triticale brans led to the conversion of β-turn to β-sheet. The scanning electron microscopy showed that addition of cereal bran destroyed the compact and uniform microstructure of gluten. Together these findings indicated that bran addition could result in changes in gluten composition and secondary structure, leading to the deterioration of dough rheological properties and the final product quality.

Key words: thermomechanical property, gluten protein, disulfide bonds, secondary structure, microstructure

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