• 食品化学 •

### 谷氨酰胺转氨酶对全麦面团特性及微观结构的影响

1. （1.哈尔滨商业大学食品工程学院，黑龙江?哈尔滨 150076；2.南京财经大学食品科学与工程学院，江苏省现代粮食流通与安全协同创新中心，江苏高校粮油质量安全控制及深加工重点实验室，江苏?南京 210023）
• 出版日期:2021-02-25 发布日期:2021-02-25
• 基金资助:
“十三五”国家重点研发计划重点专项（2018YFD0401000）；江苏高校优势学科建设工程资助项目（苏政办发〔2018〕87号）

### Effects of Glutamine Transaminase on the Properties and Microstructure of Whole Wheat Dough

WANG Jiayu, CHEN Fenglian, WU Di, TANG Xiaozhi

1. (1. College of Food Engineering, Harbin University of Commerce, Harbin 150076, China; 2. College of Food Science and Engineering, Collaborative Innovation Center for Modern Grain Circulation and Safety, Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, China)
• Online:2021-02-25 Published:2021-02-25

Abstract: The effects of glutamine transaminase (TG) on the mixing properties, stretching properties, rheological properties, microstructure and protein profile of whole wheat dough were investigated using Mixolab, texture analyzer, dynamic rheometer, scanning electron microscopy (SEM), confocal laser scanning microscopy (CLSM) and electrophoresis apparatus. The results showed that with increasing the amount of added TG, the water absorption rate of whole wheat dough decreased and the dough development time and dough stability time increased first and then decreased, the peak viscosity increased, the setback decreased, and the tensile strength increased first and then decreased. With increasing TG concentration and reaction time, the elastic modulus (G’) and viscosity modulus (G”) increased, and the tangent of loss angle (tanδ) decreased. However, when the TG concentration was higher than 2.4 U/g and the reaction time was longer than 120 min, excessive protein cross-linking and aggregation took place, accompanied by a decrease in the comprehensive viscoelasticity. The results of SEM and LCSM showed that the addition of TG made dough microstructure more continuous and compact, significantly improving gluten structure. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed that TG induced protein cross-linking and aggregation.