Soy protein isolate (SPI) was first treated with glutaminase to yield modified SPI (E-SPI) before its complexation with curcumin. Comparisons were made between SPI and E-SPI concerning their characteristics and effectiveness in complexing with curcumin, along with changes in physicochemical properties, 2,2-diphenyl-1-picryhydrazyl (DPPH)-scavenging capacity and storage stability of curcumin upon complexation. The action of glutaminase did not markedly change SPI structure, but modified some secondary structures, causing greater protein unfolding with more hydrophobic clusters and amino acids exposed. Glutaminase treatment increased DPPH-scavenging capacity, foaming capacity and stability of SPI. The protein concentration played a role in the changes induced by glutaminase treatment and complexation with curcumin, and 1% protein seemed beneficial (highest DPPH scavenging activity; highest loading amount 10.07%; 98% and >90% curcumin retained in 1%-E-SPI at 4 °C for 2 h and 12 h, respectively). Therefore, glutaminase treatment of SPI before complexation with curcumin appeared to be appropriate.

大豆分离蛋白（SPI）首先用谷氨酰胺酶处理以产生修饰的SPI（E-SPI），然后再与姜黄素复合。比较了SPI和E-SPI在与姜黄素复合中的特性和有效性，以及理化特性，复合后2,2-二苯基-1-甲基肼基（DPPH ）的清除能力和储存稳定性的变化。谷氨酰胺酶的作用没有显着改变SPI结构，但修饰了一些二级结构，从而导致更大的蛋白质展开，同时带有更多的疏水簇和暴露的氨基酸。谷氨酰胺酶治疗可增加DPPH-SPI的清除能力，发泡能力和稳定性。蛋白质浓度在谷氨酰胺酶处理和与姜黄素的复合作用中引起的变化中起作用，并且1％的蛋白质似乎是有益的（DPPH清除活性最高；最高的上样量为10.07％； 1％-E-中保留了98％和> 90％的姜黄素SPI分别在4°C下持续2 h和12 h）。因此，在与姜黄素复合之前用谷氨酰胺酶处理SPI似乎是合适的。