Comparison of Heat-Induced Aggregation of Globular Proteins
Comparison of Heat-Induced Aggregation of Globular Proteins
复制标题
DOI：
10.1021/acs.jafc.5b00927
复制
发表时间：
2015-06-03
影响因子：
6.1
通讯作者：
Gruppen, Harry
中科院分区：
文献类型：
--
作者：
Delahaije, Roy J. B. M.;Wierenga, Peter A.;Gruppen, Harry
通常，在不同的条件下(例如，温度)，使用单个蛋白质来研究蛋白质的热诱导聚集。由于不同的研究使用不同的条件和方法，分子性质和蛋白质聚集行为之间的机制关系尚未确定。因此，本研究研究了三种不同蛋白质(卵清蛋白、β-乳球蛋白和巴曲丁)在不同条件(pH、离子强度、浓度和温度)下的热诱导聚集动力学和形成的聚集体的大小/密度。β-乳球蛋白的聚集速度比卵清蛋白和巴曲丁慢10倍。此外，条件(pH、离子强度和浓度)对β-乳球蛋白聚集动力学的影响比对卵清蛋白和巴丁的影响更大。与动力学相反，所有蛋白质的聚集尺寸/密度都随着静电斥力的减小而增加。通过在这些条件下比较这些蛋白质，很明显，聚集行为不容易与分子性质(例如，电荷和暴露的疏水性)相关联。
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, beta-lactoglobulin, and patatin) under various conditions (pH, ionic strength, concentration, and temperature). The aggregation rate of beta-lactoglobulin was slower (>10 times) than that of ovalbumin and patatin. Moreover, the conditions (pH, ionic strength, and concentration) affected the aggregation kinetics of beta-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).