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

这一快速获奖项目是在胶束内的水池部分转化为笼状水合物的条件下，蛋白质在反胶束中的增溶特性的研究。在反胶束中形成水合物可能是控制蛋白质在胶束中增溶的一种新的、可行的方法。目前将发酵液中的蛋白质提取到反胶束中并随后从胶束中回收蛋白质的技术包括循环离子强度，促进低离子强度的增溶，高离子强度导致去溶。这种方法可能会削弱酶。所研究的萃取方法是在低离子强度下将蛋白质溶解在反胶束中，并在相对较低的温度(273-283K)和中等压力(0.2-5 Mpa)下诱导形成笼状水合物，以实现蛋白质从胶束中的回收。水合物的形成是冰状结构，将有效地减少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(A)在防止水合物形成的常温条件下，适度增强的压力对反胶束中蛋白质增溶的影响(B)低温下反胶束中水合物形成的研究，以及与散体水介质中水合物形成的比较，最重要的是(A)和(B)部分的合成，即(C)研究水合物形成对蛋白质在反胶束中增溶的影响。

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.