Cationic surfactants and other factors that affect enzymatic activities and transport

Abstract

Surfactants influence functions of proteins in cell signalling. Because molecular mechanisms of surfactants are poorly understood, the cationic surfactant effect on three metabolically important enzymes--L-glutamate dehydrogenase, L-lactate dehydrogenase, and L-malate dehydrogenase--were investigated at a physiologically relevant pH range (6.5-7.4). How a cationic, a non-ionic, and an anionic surfactant could differentially influence these enzymes, and how these surfactants could influence the interfacial mass transport of these enzymes across a polycarbonate membrane in a separation cell were also investigated. Provided the charge density was the same, cationic surfactants affected enzymatic activities similarly, regardless of their molecular masses. Hence, a cationic surfactant behaved similarly to a hydrophilic anionic surfactant; however, the cationic surfactant also enhanced enzymatic activity at pH 6.5 and a moderately high concentration (150 ppm). The hydrophilic surfactant enhanced enzymatic activity and the hydrophobic surfactant depressed enzymatic activity. Addition of 0.1 ppm of the hydrophilic anionic surfactant decreased the amount of enzyme permeation through the membrane, but 0.1 ppm of the non-ionic surfactant had no effect, whereas 0.1 ppm of the hydrophobic surfactant increased enzyme permeation. These results have physiological and signalling implications in nanobiotechnology.