International Dairy Journal ( IF 3.1 ) Pub Date : 2021-07-24 , DOI: 10.1016/j.idairyj.2021.105166 Xin Wang 1 , Chonghui Yue 1, 2 , Honghua Xu 1 , Chen Guan 1 , Ruichi Guo 1 , Xiaotong Yang 1 , Caihong Ma 1 , Meili Shao 1
The structural and emulsification properties of amyloid fibrils in whey protein concentrate (WPC) with certain ratios of added nuclei or nuclei fragments, generated using ultrasound, high-speed shear treatment and enzymatic hydrolysis methods, were compared. The emulsifying properties of nuclei fragments produced by high-speed shear treatment were effectively improved, but those of nuclei hydrolysed by alkaline protease decreased, since the determinant structures were destroyed. However, the emulsifying activity index and emulsifying stability index of fibrils subsequently formed by nuclei fragment induction (enzymatic hydrolysis method) were higher than those of fibrils formed by the heat-induced method and nuclei induction method in all pH environments. The fibril size induced by nuclei fragment induction was smaller, and the fibril level was higher, and thus the ability to improve the emulsifying properties of WPC was stronger.
中文翻译:
由细胞核和细胞核片段诱导后由乳清蛋白浓缩物形成的原纤维的乳化特性的比较
比较了乳清蛋白浓缩物 (WPC) 中淀粉样原纤维的结构和乳化特性,其中加入了一定比例的细胞核或细胞核片段,使用超声波、高速剪切处理和酶水解方法产生。高速剪切处理产生的细胞核碎片的乳化性能得到有效改善,但碱性蛋白酶水解的细胞核的乳化性能下降,因为行列式结构被破坏。然而,在所有pH环境下,随后通过核片段诱导(酶解法)形成的原纤维的乳化活性指数和乳化稳定性指数均高于由热诱导法和核诱导法形成的原纤维。细胞核片段诱导诱导的原纤维尺寸较小,