食品科学 ›› 2011, Vol. 32 ›› Issue (17): 69-71.doi: 10.7506/spkx1002-6630-201117012

• 基础研究 • 上一篇    下一篇

酶法脱酰胺对米谷蛋白分子微观结构的影响

刘永乐,王发祥,周小玲,李向红,俞 健,王建辉   

  1. 长沙理工大学生物与食品工程学院
  • 发布日期:2011-08-30
  • 基金资助:
    国家“863”计划重点项目(2008AA100801);湖南省科技厅科技支撑计划项目(2010NK3003); 湖南省教育厅科研项目(10C0400)

Effect of Glutaminase-induced Deamidation on Microstructure of Rice Protein

LIU Yong-le,WANG Fa-xiang,ZHOU Xiao-ling,LI Xiang-hong,YU Jian,WANG Jian-hui   

  1. (College of Chemical and Biological Engineering, Changsha University of Science and Technology, Changsha 410114, China)
  • Published:2011-08-30

摘要: 大米蛋白经酶法脱酰胺后功能性质的显著改善与其分子微观结构的变化有关。通过扫描电镜(SEM)分析、二硫键含量测定和差示扫描量热分析(DSC)研究脱酰胺后米谷蛋白分子超微结构、分子间作用力和聚合度的变化。结果表明:米谷蛋白颗粒超微结构随着脱酰胺度的增加逐渐松散;脱酰胺后分子内部分二硫键被迅速还原,但酶法脱酰胺不会影响到其肽链内二硫键;DSC图谱分析表明脱酰胺后蛋白质热稳定性和聚合度均有降低。

关键词: 米谷蛋白, 谷氨酰胺酶, 超微结构, 二硫键, 差示扫描量热分析

Abstract: The change in functional properties of glutaminase-deamidated rice protein is correlated with its microstructure change. In this paper, scanning electron microscope (SEM), disulfide bond determination and differential scanning calorimetry (DSC) were used to analyze the ultra-microstructure, disulfide bond content and thermal properties of glutaminase-deamidated rice protein. The results showed that the ultra-microstructure of glutaminase-deamidated rice protein revealed gradually loose and well dispersed structure as well as rapidly reduced disulfide bond content due to the increased deamidation degree. Moreover, declined thermal stability and polymerization degree of rice protein were determined by DSC.

Key words: rice protein, glutaminase, ultra-microstructur, disulfide bond, DSC

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