杨静洁,张波,张影全,郭波莉,顾熟琴.冷冻温度对非发酵面团蛋白质结构及面团特性的影响[J].中国粮油学报,2020,35(5):11-
冷冻温度对非发酵面团蛋白质结构及面团特性的影响
Effect of freezing temperature on protein structure and dough properties of non-fermented dough
投稿时间:2019-08-16  修订日期:2019-12-17
DOI:
中文关键词:  冷冻温度 非发酵面团 蛋白质结构 质构特性
英文关键词:freezing temperature,non-fermented dough, protein structure,TPA properties
基金项目:现代农业产业技术体系建设专项资助(CARS-03);中国农业科学院科技创新工程
作者单位邮编
杨静洁 北京农学院食品科学与工程学院 北京 102206
张波 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 
张影全 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 
郭波莉 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 
顾熟琴* 北京农学院食品科学与工程学院 102206
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中文摘要:
      冷冻温度影响冷冻面团的质量。通过研究不同冷冻温度对非发酵面团中蛋白质结构、面团特性的影响,为冷冻非发酵面团产品冷冻工艺优化提供借鉴。结果表明,随着冷冻温度的降低,面团中聚合体蛋白、谷蛋白大聚体含量增加,游离巯基含量下降,蛋白解聚程度降低;与未冷冻面团相比,-20℃冷冻的面团中α-螺旋、β-转角结构显著下降,β-折叠结构显著上升,-30℃、-40℃冷冻的面团中α-螺旋、β-折叠结构无显著性变化;冷冻后,面团硬度、回复性、黏附性上升,弹性、内聚性下降;-20℃冷冻后面团的硬度最大,弹性、内聚性最低。冷冻面团中蛋白质结构与质构特性具有显著的相关性。降低冷冻温度,可以降低非发酵面团中聚合体蛋白的解聚程度,对蛋白二级结构和质构特性的稳定具有积极作用。
英文摘要:
      Freezing temperature affects the quality of frozen dough. In this study, the effects of freezing temperatures on the protein structure and TPA of non-fermented dough was investigated, which provided a theoretical basis for the optimization of frozen non-fermented dough products. As the freezing temperature decreased, the content of polymer protein and GMP in the dough increased, the free sulfhydryl content decreased. The secondary structure of the protein (α-helix and β-turn) in frozen dough freezing at -20 °C decreased while β-sheet structure increased significantly. While,the secondary structure in the frozen dough freezing at -30℃ and -40 °C have no great difference The hardness, resilience and adhesiveness of frozen dough increased, while springiness and cohesiveness decreased. The dough freezing at -20℃ had highest hardness and lowest springiness and cohesiveness. There is a significant correlation between protein structure and texture characteristics in frozen dough. Reducing the freezing temperature can reduce the degree of depolymerization of the polymer protein in the non-fermented dough, and have a positive effect on the stability of the secondary structure and texture characteristics of the protein.
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