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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Comparison of Heat-Induced Aggregation of Globular Proteins
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Comparison of Heat-Induced Aggregation of Globular Proteins

机译：热诱导球状蛋白聚集的比较

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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, 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).
机译：通常，在各种条件（例如温度）下使用单一蛋白质研究热诱导的蛋白质聚集。由于不同的研究使用不同的条件和方法，因此尚未确定分子性质与蛋白质聚集行为之间的机械关系。因此，本研究调查了在各种条件（pH，离子强度，浓度和温度）下三种不同蛋白质（卵清蛋白，β-乳球蛋白和patatin）的热诱导聚集动力学以及形成的聚集体的大小/密度。 β-乳球蛋白的聚集速率比卵清蛋白和patatin的聚集速率慢（> 10倍）。而且，与卵清蛋白和patatin相比，条件（pH，离子强度和浓度）对β-乳球蛋白的聚集动力学的影响更大。与动力学相反，对于所有蛋白质，聚集体的大小/密度随静电排斥力的降低而增加。通过在这些条件下比较这些蛋白质，很明显，聚集行为不能容易地与分子特性（例如，电荷和暴露的疏水性）相关。

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