Changes of aggregation and structural properties of heat-denatured gluten proteins in fast-frozen steamed bread during frozen storage

被引：54

作者：

Qian, Xiaojie ^{[1
]}

Gu, Yujuan ^{[1
]}

Sun, Binghua ^{[1
]}

Wang, Xiaoxi ^{[1
]}

机构：

[1] Henan Univ Technol, Coll Food Sci & Engn, Zhengzhou, Henan, Peoples R China

来源：

FOOD CHEMISTRY | 2021年 / 365卷

关键词：

Fast-frozen steamed bread; Heat-denatured gluten; Frozen storage; Aggregation properties; Secondary structure; WHEAT GLUTEN; SIZE DISTRIBUTION; PHYSICOCHEMICAL PROPERTIES; FUNCTIONAL-PROPERTIES; PHYSICAL-PROPERTIES; HYDROPHILIC GUMS; MOLECULAR-WEIGHT; QUALITY; DOUGH; IMPACT;

D O I：

10.1016/j.foodchem.2021.130492

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The aim of this research was to clearly clarify the deterioration mechanism of heat-denatured gluten proteins by exploring the change of aggregation and structural characteristics of heat-denatured gluten proteins in the steamed bread system and the steamed gluten system during frozen storage. An increase in the total SDS-soluble protein content was determined, which mainly attributed to the soluble monomer protein content increased. Combined with the significant increase of free sulfhydryl, from 3.12 mu mol/g to 5.06 mu mol/g and 2.64 mu mol/g to 3.29 mu mol/g, respectively, it can be inferred that the proteins depolymerization induced by frozen storage was mainly involved in the breakdown of heat-induced glutenin-gliadin disulfide cross-linking. Frozen storage induced the conversion of random coil structure to 13-sheet structure and a ruptured microstructure with small fragment was observed. Moreover, the protein of steamed bread system was easier to depolymerize than that of the steamed gluten system.

引用

页数：7

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