Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Biotechnol Bioeng. 1993 Nov 20;42(10):1199-208. doi: 10.1002/bit.260421010.
Affinity cosurfactants, consisting of hydrophilic ligands derivatized with hydrophobic tails, increase the efficiency of selective protein recoveries using reversed micelles by extending the operating range of pH and salt concentration over which an extraction can be performed. Three different affinity cosurfactant-protein pairs have been used to demonstrate the principles of this extractive technique: (i) concanavalin A, a lectin, was extracted with the addition of octyl glucoside; (ii) natural amphiphiles, such as lecithin, were used to extract myelin basic protein, a membrane-associated protein known to recognize and bind the phosphatidylcholine headgroup; and (iii) alkyl boronic acids were used to extract chymotrypsin. The enhancement in protein transfer correlated with the binding strength of the free ligand and protein in aqueous solution. Several control studies confirmed the biospecificity of the interactions of protein and affinity cosurfactant.
亲和助表面活性剂由亲水配体与疏水尾组成，通过扩展 pH 和盐浓度的操作范围，增加了使用反胶束进行选择性蛋白质回收的效率，在此范围内可以进行萃取。已经使用了三种不同的亲和助表面活性剂-蛋白质对来证明这种萃取技术的原理：（i）伴刀豆球蛋白 A 是一种凝集素，加入辛基葡糖苷后进行萃取；（ii）天然两亲物，如卵磷脂，用于提取髓鞘碱性蛋白，这是一种已知能识别和结合磷脂酰胆碱头基的膜相关蛋白；（iii）烷基硼酸用于提取糜蛋白酶。蛋白质转移的增强与游离配体和蛋白质在水溶液中的结合强度相关。几项对照研究证实了蛋白质和亲和助表面活性剂之间相互作用的生物特异性。
