蛋白质对人类健康至关重要,具有巨大的食品应用。尽管他们的优势,植物和动物蛋白通常由于氢键而表现出有限的分子灵活性和较差的溶解度,疏水相互作用,以及它们分子结构中的离子相互作用。因此,迫切需要修饰蛋白质的刚性结构以增强其稳定性和功能特性。超声辅助离子液体(UA-IL)处理用于开发化合物修饰并生产具有优异功能特性的蛋白质已受到关注。然而,没有评论专门讨论UA-IL和蛋白质之间的相互作用。因此,这篇综述集中在有关UA-IL对物理化学性质的影响和潜在反应机理的最新研究进展(包括粒径;次要,和三级结构;和表面形态)以及功能(如溶解度,乳化性能,和起泡能力)的蛋白质。此外,还从不同角度讨论了修饰蛋白的安全性评估,如急性和慢性毒性,遗传毒性,细胞毒性,以及环境和微生物毒性。本综述证明UA-IL处理诱导的蛋白质结构变化显著影响蛋白质的功能特性。这种处理方法通过空化有效促进蛋白质结构拉伸和空间重排,热效应,和离子相互作用。因此,修饰蛋白的功能特性表现出明显的增强,从而为在食品工业中利用修饰的蛋白质产品带来了更多的机会。还提出了使用UA-IL进行蛋白质修饰的潜在未来方向。
Proteins are essential to human health with enormous food applications. Despite their advantages, plant and animal proteins often exhibit limited molecular flexibility and poor solubility due to hydrogen bonds, hydrophobic interactions, and ionic interactions within their molecular structures. Thus, there is an urgent need to modify the rigid structure of proteins to enhance their stability and functional properties. Ultrasound-assisted ionic liquid (UA-IL) treatment for developing compound modification and producing proteins with excellent functional properties has received interest. However, no
review specifically addresses the interactions between UA-ILs and proteins. Hence, this
review focused on recent research advancements concerning the effects and potential reaction mechanisms of UA-ILs on the physicochemical properties (including particle size; primary, secondary, and tertiary structure; and surface morphology) as well as the functionality (such as solubility, emulsifying properties, and foaming ability) of proteins. Moreover, the safety evaluation of modified proteins was also discussed from various perspectives, such as acute and chronic toxicity, genotoxicity, cytotoxicity, and environmental and microbial toxicity. This
review demonstrated that UA-IL treatment-induced protein structural changes significantly impact the functional characteristics of proteins. This treatment approach efficiently promotes protein structure stretching and spatial rearrangement through cavitation, thermal effects, and ionic interactions. As a result, the functional properties of modified proteins exhibited an obvious enhancement, thereby bringing more opportunities to utilize modified protein products in the food industry. Potential future directions for protein modification using UA-ILs were also proposed.