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Characterization of enzymatic cross-linking soy protein isolate xerogels and its shape memory effect induced by ethylcellulose
Food Chemistry ( IF 8.5 ) Pub Date : 2023-01-25 , DOI: 10.1016/j.foodchem.2023.135564
Yangyang Li 1 , Shengnan Wang 1 , Xiulin Liu 1 , Lina Yang 1 , He Liu 1 , Yutang He 1
Affiliation  

In this study, the deformation behavior of soybean protein isolate (SPI) xerogels cross-linked with different transglutaminase (TGase) concentrations was investigated. The gel properties of TGase cross-linked SPI were analyzed by rheology and texture. Results showed that 0.4% TGase completely promoted the intermolecular cross-linking, SPI molecules had more binding sites and α-helix content and less irregular curl structure. The presence of 0.4% TGase enhanced the water binding ability and thermal stability of SPI xerogel, and its denaturation temperature was up to 181.50°C. The corresponding texture characteristics showed that hardness and elasticity were significantly increased by 182.90% and 25.00%, respectively. Results showed that SPI containing 0.4% TGase had the best 3D (three-dimension) shape change after hydration. However, excessive TGase (1.0% w/v) led to excessive lysine covalent cross-linking, which increases the porosity of the gel surface, causing the disrupted gel network. The research provides insights and new ideas for food-processing technology called 4D (four-dimension) food.



中文翻译:

酶促交联大豆分离蛋白干凝胶的表征及其由乙基纤维素诱导的形状记忆效应

在本研究中,研究了与不同转谷氨酰胺酶 (TGase) 浓度交联的大豆分离蛋白 (SPI) 干凝胶的变形行为。通过流变学和质地分析了 TGase 交联 SPI 的凝胶特性。结果表明,0.4%的TGase完全促进了分子间交联,SPI分子具有更多的结合位点和α-螺旋含量以及更少的不规则卷曲结构。0.4% TGase的存在增强了SPI干凝胶的水结合能力和热稳定性,其变性温度高达181.50℃。相应的质地特征表明,硬度和弹性分别显着提高了182.90%和25.00%。结果表明,含有 0.4% TGase 的 SPI 在水合后具有最佳的 3D(三维)形状变化。然而,过量的 TGase (1.0% w/v) 导致过量的赖氨酸共价交联,这会增加凝胶表面的孔隙率,从而导致凝胶网络被破坏。该研究为称为 4D(四维)食品的食品加工技术提供了见解和新思路。

更新日期:2023-01-26
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