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Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments

机译:高强度超声预处理对大豆分离蛋白的酸诱导胶凝行为

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摘要

High intensity ultrasonic (HUS, 20 k Hz, 400 W) pre-treatments of soybean protein isolate (SPI) improved the water holding capacity (WHC), gel strength and gel firmness (final elastic moduli) of glucono-δ-lactone induced SPI gels (GISG). Sonication time (0, 5, 20, and 40 min) had a significant effect on the above three properties. 20 min HUS-GISG had the highest WHC (95.53 ± 0.25%), gel strength (60.90 ± 2.87 g) and gel firmness (96340 Pa), compared with other samples. Moreover, SH groups and non-covalent interactions of GISG also changed after HUS pre-treatments. The HUS GISG had denser and more uniform microstructures than the untreated GISG. Rheological investments showed that the cooling step (reduce the temperature from 95 to 25 °C at a speed of 2 °C/min) was more important for the HUS GISG network formation while the heat preservation step (keep temperature at 95 for 20 min) was more important for the untreated GISG. HUS reduced the particle size of SPI and Pearson correlation test showed that the particle size of SPI dispersions was negatively correlated with WHC, gel strength and gel firmness.
机译:大豆分离蛋白(SPI)的高强度超声(HUS,20 k Hz,400 W)预处理改善了葡萄糖酸-δ-内酯诱导的SPI的持水量(WHC),凝胶强度和凝胶硬度(最终弹性模量)凝胶(GISG)。超声处理时间(0、5、20和40分钟)对上述三个属性有重大影响。与其他样品相比,20分钟的HUS-GISG具有最高的WHC(95.53±0.25%),凝胶强度(60.90±2.87 g)和凝胶硬度(96340 Pa)。此外,HUS预处理后,GISG的SH基团和非共价相互作用也发生了变化。与未经处理的GISG相比,HUS GISG具有更致密,更均匀的微观结构。流变学投资表明,冷却步骤(以2°C / min的速度将温度从95降低到25°C)对于HUS GISG网络的形成更为重要,而保温步骤(将温度在95保持20分钟)更重要。对于未经处理的GISG更重要。 HUS降低了SPI的粒径,而Pearson相关测试表明,SPI分散体的粒径与WHC,凝胶强度和凝胶硬度呈负相关。

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