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Cross-linking of Soybean Proteins by Transglutaminase in the Presence of Gelatin to Improve Their Rheological Properties: Rheology of a cross-linked soybean proteins

机译:转基谷氨酰胺酶在明胶存在下的交联蛋白质,提高其流变性质:交联大豆蛋白的流变学

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Soybean protein isolates (SPI) was cross-linked by transglutaminase in the presence of gelatin in this work to prepare a cross-linked composite soybean protein-gelatin, a modified SPI. The concentration of total proteins was fixed at 5% (w/v), and the ratio of SPI to gelatin was fixed at 4:1 (w/w). The cross-linking of the proteins was carried out as fellows: enzyme addition level at 20U/g proteins, reaction time of 2 h and temperature of 40°C. Compared to the original SPI and transglutaminase-induced cross-linked SPI, the dispersion of the modified SPI exhibited improved apparent viscosity and viscoelastic behaviors, indicating that cross-linking of SPI by transglutaminase in the presence of gelatin could improve the rheological properties of soybean proteins.
机译:大豆蛋白分离株(SPI)在本作加工中通过转谷氨酰胺酶交联,以制备交联复合大豆蛋白 - 明胶,改性SPI。总蛋白质的浓度固定为5%(w / v),并且SPI与明胶的比例在4:1(w / w)下固定。蛋白质的交联作为研究员进行:20U / g蛋白的酶添加水平,2小时的反应时间和40℃的温度。与原始SPI和转谷氨酰胺酶诱导的交联SPI相比,改性SPI的分散表现出改善的表观粘度和粘弹性行为,表明在明胶存在下通过转谷氨酰胺酶的交联可以改善大豆蛋白的流变性质。

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