酸性调控对大豆分离蛋白纤维功能性质的影响

近年来,蛋白淀粉样纤维因其独特的材料学特性,在结构化和功能化食品领域引起广泛的关注。然而人们对蛋白纤维基材料的功能特性及相关调控机理还不甚了解。本文研究了不同酸诱导剂对大豆分离蛋白(SPI)自组装纤维的结构、乳化特性、凝胶特性及成膜性质的影响。结果表明,经盐酸或醋酸诱导均能形成纤维化蛋白,蛋白质的二级结构则由α-螺旋转变为β-折叠结构。有趣的是,相较于盐酸诱导的短而硬的蛋白纤维(H-SPI),醋酸诱导的蛋白纤维(C-SPI)形状更加柔顺且规则。除此之外,C-SPI拥有更大的粒径、更高的凝胶硬度、更优的乳化稳定性和成膜性。因此,通过选择适宜的酸诱导剂种类能够改善蛋白纤维的理化和功能性质。

The influence of acidity regulation on the functional properties of soybean isolate protein fiber

Due to their distinctive material characteristics, protein amyloid fibrils have recently received a lot of attention in the field of structured and functionalized foods. However, little is known about the functional traits and associated regulation processes of materials made of protein fibers. In this job, we examined how the structure, emulsification, gelation, and film-forming capabilities of soybean isolated protein self-assembled fibers were affected by acid inducers. The outcomes demonstrated that either hydrochloric acid or acetic acid could cause the formation of protein fibrils at high temperature circumstances, and circular dichroism demonstrated that the protein secondary structure changed from α-helical to β-folded structure. Interestingly, the acetate induced protein fibrils were more pliable and regular in shape compared to the short and stiff protein fibrils induced by hydrochloric acid. In addition, the acetic acid-induced protein fibrils have larger particle size, higher gel hardness, better emulsion stability and film formation properties. Therefore, the physicochemical and functional properties of the protein fibers could be improved by selecting the appropriate acid inducer species.