综述小麦面团制造中麦谷蛋白大聚体的变化  

Review on Changes of Glutenin Macropolymer in Wheat Dough Processing

作　　者：苏婷 刘鸿飞 李芳 代美瑶 张波[1] Su Ting;Liu Hongfei;Li Fang;Dai Meiyao;Zhang Bo(Institute of Food Science and Technology CAAS,Key Laboratory of Agro-Products Processing,Ministry of Agriculture,Beijing 100193)

机构地区：[1]中国农业科学院农产品加工研究所,农业农村部农产品加工综合性重点实验室,北京100193

出　　处：《中国食品学报》2023年第4期481-489,共9页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家现代农业产业技术体系资助项目(CARS-03)。

摘　　要：高分子量麦谷蛋白亚基通过分子间二硫键形成骨架,低分子量麦谷蛋白亚基通过二硫键结合在骨架上,骨架间通过疏水作用、氢键、静电作用等非共价作用形成聚集体。聚集体内相互作用或聚集复杂到一定程度,使用十二烷基硫酸钠溶液仍无法分散或溶解的被称为麦谷蛋白大聚体。麦谷蛋白大聚体的聚集和解聚对面团黏弹性、面团操作性和感官品质有较大影响。本文概述了从小麦籽粒到面粉再到面团制造过程中麦谷蛋白大聚体含量及聚集状态的变化。在籽粒储藏过程中,麦谷蛋白大聚体含量增加,表明麦谷蛋白逐渐聚集。在籽粒中心,麦谷蛋白大聚体占总蛋白的比例较高,表明籽粒中心的蛋白质发生更多的聚集。在面粉加水搅拌形成面团的过程中,麦谷蛋白颗粒吸水溶胀,麦谷蛋白大聚体含量逐渐下降,表明聚集程度下降。在面团醒发过程中,麦谷蛋白大聚体含量增加,表明麦谷蛋白重新聚集。在更多尺度或层级下解析蛋白质的聚集和解聚动态平衡,有助于揭示麦谷蛋白大聚体在小麦面团制造过程中的变化机理,对调控面筋形成、面团黏弹性等具有重要意义。The high molecular weight glutenin subunit forms the skeleton by intermolecular disulfide bond,while the low molecular weight glutenin subunit binds to the skeleton by disulfide bond,and the aggregates are further formed by non-covalent interactions such as hydrophobic interaction,hydrogen bond and electrostatic interaction between the skeletons.Aggregates that are so complex that even sodium dodecyl sulfate solution cannot disperse or dissolve are called glutenin macropolymer.The aggregation and deaggregation of glutenin macropolymer has great influence on flour production,dough viscoelasticity and relative sensory quality.The article summarizes the variation in glutenin macropolymer content and aggregation behavior from wheat kernel to flour and dough processing.During wheat storage,the content of glutenin macropolymer increased,indicating that glutenin gradually accumulated.In the center of wheat,the proportion of glutenin macropolymer to total protein was higher,indicating that more protein aggregation occurred in grain center.When mixing flour and water to form dough,the glutenin particles absorb water and swell,and the glutenin macropolymer content gradually decreases,indicating that the aggregation degree decreases as well.During the resting process,glutenin macropolymer content increased,indicating glutenin reaggregation.The analysis of dynamic equilibrium of protein aggregation and deaggregation at different levels is helpful to reveal the mechanism of glutenin macropolymers changes in wheat dough processing,which has importance in modulating gluten formation and dough viscoelasticity.

关 键 词：麦谷蛋白大聚体 面团结构 高分子谷蛋白亚基 流变学性质 

分 类 号：TS213.2[轻工技术与工程—粮食、油脂及植物蛋白工程]