超高温瞬时灭菌牛乳酪蛋白与β-乳球蛋白形成老化凝胶的机制研究  

Mechanistic study on aged gel formation by casein andβ-lactoglobulin in ultra-high temperature milk

作　　者：张太 刘伊索 曹佳媛 陈志伟[3] 易华西[1,2] ZHANG Tai;LIU Yisuo;CAO Jiayuan;CHEN Zhiwei;YI Huaxi(College of Food Science and Engineering,Ocean University of China,Qingdao 266000,China;Zhongyuan Food Laboratory,Luohe 462300,China;Institute of Food and Nutrition Sciences,Shandong University of Technology,Zibo 255000,China)

机构地区：[1]中国海洋大学食品科学与工程学院,山东青岛266000 [2]中原食品实验室,河南漯河462300 [3]山东理工大学食品与营养科学研究院,山东淄博255000

出　　处：《食品与发酵工业》2025年第8期85-91,共7页Food and Fermentation Industries

基　　金：山东省重点研发计划项目(2023CXGC010711);国家重点研发计划课题(2024YFD1301305)。

摘　　要：超高温瞬时灭菌(ultra-high temperature,UHT)乳是目前液态奶的主要产品,具有保质期长等优点。但是UHT处理会促使牛乳酪蛋白与乳清蛋白结合,导致UHT乳在贮藏中产生老化凝胶,目前尚不清楚酪蛋白与乳清蛋白的结合机制。该研究以不同加热温度和时间制备的UHT乳为研究对象,通过实际实验和计算机模拟,探究了UHT条件下酪蛋白与β-乳球蛋白(β-lactoglobulin,β-Lg)的相互作用及老化凝胶的形成机理。扫描电镜结果表明,UHT乳老化凝胶呈现粗糙多孔的形貌。SDS-PAGE结果表明,老化凝胶主要含有牛乳酪蛋白和β-Lg。HPLC和透射电子显微镜进一步证实了酪蛋白和β-Lg发生了结合。微量热泳动结果发现,β-Lg与酪蛋白单体通过非共价作用自发结合。通过对酪蛋白单体建模与β-Lg进行分子对接,分子动力学模拟发现,酪蛋白与β-Lg的相互作用主要受静电力和范德华力驱动,其中氢键和疏水相互作用对稳定复合体具有关键作用。该研究为优化UHT乳热加工工艺和延长产品货架期提供了理论依据。Ultra-high temperature(UHT)sterilized milk is currently the main product in the liquid milk market,offering advantages such as a long shelf life.However,UHT treatment promotes the binding of milk casein and whey proteins,leading to the formation of age gelation during storage,and the binding mechanism remains unclear.This study investigated UHT milk prepared at different heating temperatures and durations,using both practical experiments and in silico simulations,to explore the interaction between casein andβ-lactoglobulin(β-Lg)under UHT conditions and the mechanism of age gelation.Scanning electron microscopy(SEM)results showed that the aging gel in UHT milk had a rough and porous morphology.SDS-PAGE analysis revealed that the aging gel mainly contained caseins andβ-Lg.High performance liquid chromatography(HPLC)and transmission electron microscopy(TEM)further confirmed the binding between casein andβ-Lg.Microcalorimetry indicated thatβ-Lg spontaneously bound to casein monomers through non-covalent interactions.Molecular docking and molecular dynamics simulations revealed that the interaction between casein andβ-Lg was primarily driven by electrostatic forces and van der Waals forces,with hydrogen bonding and hydrophobic interactions playing a crucial role in stabilizing the complex.This study provided a theoretical basis for optimizing UHT milk heat processing techniques and extending product shelf life.

关 键 词：超高温处理 酪蛋白 Β-乳球蛋白 老化凝胶 

分 类 号：TS252.1[轻工技术与工程—农产品加工及贮藏工程]