Department of Chemical Engineering Massachusetts Institute of Technology Cambridge, Massachusetts USA.
Biotechnol Prog. 1985 Mar;1(1):69-74. doi: 10.1002/btpr.5420010113.
The controlled solubilization of proteins in a reverse micelle-containing organic phase is considered as a method for separation of proteins by liquid-liquid extraction. Cytochrome-C was transferred between a bulk aqueous phase and a micellar phase, using the Aerosol OT-isooctane system of surfactant and solvent. It was observed that the extent of protein solubilization could be controlled by varying the ionic strength of the aqueous phase equilibrated with the micellar phase.The protein transferred into the micellar phase rapidly, under conditions of low ionic strength, and transferred out of the micelles relatively slowly, under conditions of high ionic strength. It is proposed that the effect of the ionic strength was to alter the electrostatic interaction between the surface charge of the protein and the charged interior of the reverse micelle by Debye screening.
反胶束相中蛋白质的可控溶解被认为是通过液-液萃取分离蛋白质的一种方法。使用表面活性剂和溶剂的气溶胶 OT-异辛烷体系，将细胞色素 C 从本体水相转移到胶束相中。观察到通过改变与胶束相平衡的水相的离子强度，可以控制蛋白质的溶解程度。在离子强度低的条件下，蛋白质迅速转移到胶束相中，而在离子强度高的条件下，蛋白质相对缓慢地从胶束中转移出来。据推测，离子强度的影响是通过德拜屏蔽来改变蛋白质表面电荷与反胶束带电内部之间的静电相互作用。
