Hydrate Formation and Protein Solubilization in Reversed Micelles (Expedited Award)

这个加速奖项目是一个关于蛋白质溶解的研究 反胶束中的水的条件下， 胶束内的池部分转化为包合物 水合物 在反胶束中的Hybridium形成可能是一种新的， 控制蛋白质溶解的可行方法 胶束 目前从发酵中提取蛋白质的技术 将肉汤转化为反胶束，随后将它们从反胶束中回收。 胶束涉及循环离子强度，促进增溶 低离子强度，高离子强度引起脱溶。 这些方法可以削弱酶。 提取方法根据 研究是在较低温度下在反胶束中增溶蛋白质 离子强度和倾向于诱导笼形水合物的形成 在相对较低的温度（273-283 K）和中等压力下 （0.2-5 MPa）以实现从胶束中回收蛋白质。 形成 水合物是冰状结构， 胶束内的微水相体积，从而控制 脱溶特性 探索性研究项目分为三个部分： 适度提高压力对蛋白质溶解的影响 在环境温度条件下的反胶束，其中水合物 （B）研究了水合物的形成， 低温下的胶束，以及与水合物形成的比较 在大量的水介质中，最重要的是， (a)和（B），即（c）水合物形成对 反胶束中的蛋白质溶解。

This expedited award project is a study on protein solubilization characteristics in reversed micelles under conditions where the water pools within the micelles are partially converted to clathrate hydrates. Hydrate formation in reversed micelles may be a novel and viable method to control the solubilization of proteins within the micelles. The present technique to extract proteins from fermentation broths into reversed micelles and subsequently recover them from the micelles involves cycling the ionic strength, promoting solubilization with low ionic strenth, high ionic strength causing desolubilization. Such approaches can weaken enzymes. The extraction approach under investigation is to solubilize protein in reversed micelles at low ionic strength, and ten to induce the formation of clathrate hydrates under relatively low temperatures (273-283 K) and moderate pressures (0.2-5 MPa) to effect protein recovery out of the micelles. Formation of hydrates, which are ice-like structures, would effectively reduce the microaqueous phase volume within the micelles, and thus control desolubilization characteristics. The exploratory research project is divided into three parts (a) the effect of moderately enhanced pressures on protein solubilization in reversed micelles under ambient temperature conditions where hydrate formation is prevented (b) the study of hydrate formation in reversed micelles at low temperatures, and comparisons with hydrate formation in bulk aqueous media, and most importantly, the synthesis of parts (a) and (b), i.e. (c) a study of the effects of hydrate formation on protein solubilization in reversed micelles.