卵清蛋白
化学
离子强度
球状蛋白
动力学
蛋白质聚集
β-乳球蛋白
生物物理学
色谱法
乳清蛋白
生物化学
物理化学
物理
生物
水溶液
量子力学
免疫学
免疫系统
作者
Roy J. B. M. Delahaije,Peter A. Wierenga,Marco L. F. Giuseppin,Harry Gruppen
标识
DOI:10.1021/acs.jafc.5b00927
摘要
Typically, heat-induced aggregation of proteins is studied using a single protein under various conditions (e.g., temperature). Because different studies use different conditions and methods, a mechanistic relationship between molecular properties and the aggregation behavior of proteins has not been identified. Therefore, this study investigates the kinetics of heat-induced aggregation and the size/density of formed aggregates for three different proteins (ovalbumin, β-lactoglobulin, and patatin) under various conditions (pH, ionic strength, concentration, and temperature). The aggregation rate of β-lactoglobulin was slower (>10 times) than that of ovalbumin and patatin. Moreover, the conditions (pH, ionic strength, and concentration) affected the aggregation kinetics of β-lactoglobulin more strongly than for ovalbumin and patatin. In contrast to the kinetics, for all proteins the aggregate size/density increased with decreasing electrostatic repulsion. By comparing these proteins under these conditions, it became clear that the aggregation behavior cannot easily be correlated to the molecular properties (e.g., charge and exposed hydrophobicity).
科研通智能强力驱动
Strongly Powered by AbleSci AI