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首页> 外文期刊>Biotechnology Progress >Osmotic Second Virial Cross-Coefficient Measurements for Binary Combination of Lysozyme, Ovalbumin, and a-Amylase in Salt Solutions
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Osmotic Second Virial Cross-Coefficient Measurements for Binary Combination of Lysozyme, Ovalbumin, and a-Amylase in Salt Solutions

机译：盐溶液中溶菌酶，卵清蛋白和α-淀粉酶的二元组合的渗透性第二病毒交叉系数测量

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摘要

Interactions measurement is a valuable tool to predict equilibrium phase separation of a desired protein in the presence of unwanted macromolecules. In this study, cross-interactions were measured as the osmotic second virial cross-coefficients (B_(23)) for the three binary protein systems involving lysozyme, ovalbumin, and α-amylase in salt solutions (sodium chloride and ammonium sulfate). They were correlated with solubility for the binary protein mixtures. The cross-interaction behavior at different salt concentrations was interpreted by either electrostatic or hydrophobic interaction forces. At low salt concentrations, the protein surface charge dominates cross-interaction behavior as a function of pH. With added ovalbumin, the lysozyme solubility decreased linearly at low salt concentration in sodium chloride and increased at high salt concentration in ammonium sulfate. The B_(23) value was found to be proportional to the slope of the lysozyme solubility against ovalbumin concentration and the correlation was explained by preferential interaction theory.
机译：相互作用测量是在不想要的大分子存在下预测所需蛋白质平衡相分离的有价值的工具。在这项研究中，交叉相互作用被测量为盐溶液（氯化钠和硫酸铵）中涉及溶菌酶，卵清蛋白和α-淀粉酶的三个二元蛋白质系统的渗透第二病毒交叉系数（B_（23））。它们与二元蛋白质混合物的溶解度相关。在不同盐浓度下的交叉相互作用行为可以通过静电或疏水相互作用力来解释。在低盐浓度下，蛋白质表面电荷决定了交叉相互作用行为随pH的变化。加入卵清蛋白后，溶菌酶的溶解度在氯化钠中低盐浓度下线性降低，而在硫酸铵中高盐浓度下增加。发现B_（23）值与溶菌酶溶解度相对于卵清蛋白浓度的斜率成比例，并且通过优先相互作用理论解释了这种相关性。

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