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TGas交叉连接对大豆隔离蛋白的结构,乳化和凝性能的影响

Ziqi Peng¹, Kunlun Liu¹, Ning Liao¹

¹College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Foods (Basel, Switzerland)

|June 26, 2025

概括

转胺酶 (TGase) 酶交联增强大豆隔离蛋白 (SPI) 的特性. 这种修改通过增加共价键来改善乳化,凝强度和纳米粒子稳定性.

科学领域:

食品科学食品科学食品科学
生物化学生物化学
材料科学材料科学材料科学

背景情况:

豆分离蛋白 (SPI) 是一种有价值的植物性蛋白质来源.
了解SPI的功能性质对于食品应用至关重要.
酶修饰提供了一条改善蛋白质功能的途径.

研究的目的:

研究转谷氨酸酶 (TGase) 对SPI物理化学性质的影响.
为了将TGase诱导的变化与乳化和质行为相关联.
为了确定最佳的TGas处理条件,以提高SPI功能.

主要方法:

二甲基硫酸盐-多烯胺凝电泳 (SDS-PAGE) 用于蛋白质结构分析.
福里埃变换红外光谱 (FTIR) 用于化学键变化.
内生光谱学用于蛋白质微环境分析.
测量乳化性能和凝的风湿性质 (储存模量).

主要成果:

在SPI中,TGase促进了氨酸和谷氨酸残留物之间的共价交联.
适度的TGase预交联 (5-7.5U/g2小时或5U/g2-3小时) 提高了乳化性能24.35%.
在最佳的TGase处理下,凝储存模量增加了288%.
TGas交联增加了SPI表面电荷,静电潜力和疏水性,同时减少了自由硫基.

结论:

TGase酶性交联显著增强了SPI的乳化和凝特性.
交叉连接通过增加共价键的形成来提高SPI纳米颗粒的结构稳定性.
优化TGase处理提供了一种方法来为改善食品应用量身定制SPI功能.

关键词:

形状的变化形状的变化交叉连接交叉连接交叉连接属性属性属性属性蛋白质纳米颗粒蛋白质纳米颗粒转氨酸酶是什么意思

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