静电场辅助冷冻对面筋功能特性和聚集行为的影响

Yanyan Zhang , Siqi Zhang , Bingrui Wang , Hongwei Wang , Xingli Liu , Hua Zhang
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引用次数: 0

摘要

冷冻过程中面筋的变化可能会导致面团质量下降,这可以通过静电场处理来解决。研究了静电场辅助冷冻(EFAF)对面筋的功能特性、结构特征和聚集行为的影响。结果表明,EFAF改善了面筋的功能性,提高了面筋的保水性、乳化性和发泡性。当施加静电场时,面筋蛋白的α-螺旋含量和g-g-g构象分别增加了27.50%和40.05%,与对照组相比有显著差异(P<;0.05),EFAF后,AFM分析显示麦谷蛋白链结构更完整,醇溶蛋白粒径更小。这些结果表明,EFAF通过减缓面筋大分子的解聚、维持面筋的链结构、稳定醇溶蛋白的分子内二硫键和稳定面筋的微观结构来改善面筋蛋白的功能特性。
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Effects of electrostatic field-assisted freezing on the functional properties and aggregation behavior of gluten

Changes in gluten during the freezing process could cause a deterioration in dough quality, which would be solved by electrostatic field treatment. This paper investigated the effects of electrostatic field assisted freezing (EFAF) on the functional properties, structural characteristics and aggregation behavior of gluten. The results showed that EFAF improved the functional properties of gluten with enhanced water holding, emulsifying and foaming properties. When the electrostatic field was applied, the α-helix content and g-g-g conformation of gluten proteins increased with a maximum of 27.50 % and 40.05 %, respectively, which were significantly different from the control (P < 0.05). The degree of depolymerization of gluten macromolecules decreased when the electrostatic field was applied, and was obtained to be the lowest at 600 V with 5.71 %, which was significantly different from that without applied electrostatic field (P < 0.05). After EFAF, AFM analysis showed a more intact glutenin chain structure and smaller particle size of the gliadin. These results indicated that EFAF improved the functional properties of gluten proteins by the mechanism of slowing down the depolymerization of gluten macromolecules, maintaining the chain structure of gluten, stabilizing the intramolecular disulfide bonds of gliadin, and stabilizing the microstructure of gluten.

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