摘要
通过分析挤压组织化对小麦面筋蛋白的影响,探讨了小麦面筋蛋白挤压组织化的机理。研究结果表明:挤压组织化使小麦面筋蛋白的亚基以二硫键和酰胺键的形式发生聚合。挤压过程中有大量的二硫键生成,维持小麦组织化蛋白(TWP)的主要化学作用力是二硫键和非共价键的交互作用,其次是非共价键。挤压组织化并未完全破坏小麦面筋蛋白的二级结构,而是部分α-螺旋、无规则卷曲、β-折叠转化成了较稳定的β-转角。
the mechanism of textured wheat protein was explored and discussed by analyzing the influence of textured extrusion on the structure of wheat gluten protein. The result of the experiment showed that during the extruded process, the subunit of wheat protein aggregated in the form of disulfide bond and amido bond, and a lot of disulfide bond formed. The interaction of disulfide bond and non - covalent bond plays a more important role in maintai- ning the textured wheat protein than non -covalent bond alone. Not all secondary structure was destroyed during the textured extrusion, but some of α - helix, random coil and β - sheet turned into more stable β - turns.
出处
《中国粮油学报》
EI
CAS
CSCD
北大核心
2013年第1期60-64,共5页
Journal of the Chinese Cereals and Oils Association
关键词
小麦面筋蛋白
挤压组织化
蛋白质交联
二硫键
二级结构
wheat gluten protein, textured extrusion, protein cross - linking, disulfide bond, secondary structure
