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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Effect of protein-surfactant interactions on aggregation of beta-lactoglobulin.
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Effect of protein-surfactant interactions on aggregation of beta-lactoglobulin.

机译：蛋白质-表面活性剂相互作用对β-乳球蛋白聚集的影响。

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The milk protein beta-lactoglobulin (betaLG) dominates the properties of whey aggregates in food products. Here we use spectroscopic and calorimetric techniques to elucidate how anionic, cationic and non-ionic surfactants interact with bovine betaLG and modulate its heat-induced aggregation. Alkyl trimethyl ammonium chlorides (xTAC) strongly promote aggregation, while sodium alkyl sulfates (SxS) and alkyl maltopyranosides (xM) reduce aggregation. Sodium dodecyl sulfate (SDS) binds to non-aggregated betaLG in several steps, but reduction of aggregation was associated with the first binding step, which occurs far below the critical micelle concentration. In contrast, micellar concentrations of xMs are required to reduce aggregation. The ranking order for reduction of aggregation (normalized to their tendency to self-associate) was C10-C12>C8>C14 for SxS and C8>C10>C12>C14>C16 for xM. xTAC promote aggregation in the same ranking order as xM reduce it. We conclude that SxS reduce aggregation by stabilizing the protein's ligand-bound state (the melting temperature t(m) increases by up to 10 degrees C) and altering its charge potential. xM monomers also stabilize the protein's ligand-bound state (increasing t(m) up to 6 degrees C) but in the absence of charged head groups this is not sufficient by itself to prevent aggregation. Although micelles of both anionic and non-ionic surfactants destabilize betaLG, they also solubilize unfolded protein monomers, leaving them unavailable for protein-protein association and thus inhibiting aggregation. Cationic surfactants promote aggregation by a combination of destabilization and charge neutralization. The food compatible surfactant sodium dodecanoate also inhibited aggregation well below the cmc, suggesting that surfactants may be a practical way to modulate whey protein properties.
机译：牛奶蛋白β-乳球蛋白（betaLG）主导着食品中乳清聚集物的特性。在这里，我们使用分光光度法和量热技术来阐明阴离子，阳离子和非离子表面活性剂如何与牛βLG相互作用并调节其热诱导的聚集。烷基三甲基氯化铵（xTAC）强烈促进聚集，而烷基硫酸钠（SxS）和烷基麦芽吡喃糖苷（xM）减少聚集。十二烷基硫酸钠（SDS）在几个步骤中与未聚集的βLG结合，但聚集的减少与第一步结合有关，该步骤远低于临界胶束浓度。相反，需要胶束浓度的xMs来减少聚集。 SxS的聚集减少的排序顺序（标准化为它们的自缔合趋势）是C10-C12> C8> C14，xM的是C8> C10> C12> C14> C16。 xTAC以与xM减少聚合相同的排序顺序促进聚合。我们得出的结论是，SxS通过稳定蛋白质的配体结合状态（熔化温度t（m）升高高达10摄氏度）并改变其电荷电位来减少聚集。 xM单体还可以稳定蛋白质的配体结合状态（将t（m）升高至6摄氏度），但是在没有带电头基的情况下，这本身不足以防止聚集。尽管阴离子和非离子表面活性剂的胶束都会破坏betaLG的稳定性，但它们也会溶解未折叠的蛋白质单体，从而使它们无法用于蛋白质与蛋白质的缔合，从而抑制了聚集。阳离子表面活性剂通过去稳定和电荷中和的组合促进聚集。与食品相容的表面活性剂十二烷酸钠也抑制了远低于cmc的聚集，表明表面活性剂可能是调节乳清蛋白特性的实用方法。

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