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Physicochemical properties and gluten structures of frozen steamed bread dough under freeze–thaw treatment affected by gamma-polyglutamic acid

聚谷氨酸 面筋 食品科学 化学 低温保护剂 冰晶 流变学 化学工程 抗冻蛋白 结晶学 生物化学 低温保存 材料科学 物理 工程类 复合材料 光学 胚胎 细胞生物学 生物
作者
Erqi Guan,Tingjing Zhang,Wu Kun,Yuling Yang,Ke Bian
出处
期刊:Food Hydrocolloids [Elsevier BV]
卷期号:137: 108334-108334 被引量:34
标识
DOI:10.1016/j.foodhyd.2022.108334
摘要

Concerned to chemical structure, the viscous gamma-polyglutamic acid (γ-PGA) should have the similar characteristics with antifreeze hydrocolloids and polypeptides which have been broadly used in frozen foods. However, the cryoprotective functions of γ-PGA are little explored as compared to those of hydrocolloids and polypeptides. In this study, influences of γ-PGA addition on fermentative performance and rheological behavior of frozen steamed bread (SB) dough during frozen storage and freeze–thaw cycles were investigated, and the underlying mechanism governing these influences was clarified. Results showed the γ-PGA dispersed free water, remarkably reduced freezable water content, and restricted water migration, which facilitated the formation of smaller and more uniform ice crystals in frozen dough structure. In addition, γ-PGA interacted with gluten proteins through electrostatic attractions and hydrogen bonds, transforming the gluten protein conformation from loose coil structures to relatively compact β-structures. In these relatively compact structures, the free sulfhydryl (SH) groups, originally located far away in space, became closer and easier to be oxidized into disulfide bonds (SS) or be involved in SH–SS exchange reaction. This led to intensive protein aggregations and water–solid interplay, rendering the dough better resilience to cope with ice growth and recrystallization. Accordingly, the deterioration in frozen SB dough's fermentability and rheology was effectively alleviated, suggesting that γ-PGA has a great potential to serve as an effective cryoprotectant in frozen SB.
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