EXTRACTION OF PROTEIN ALPHA-AMYLASE BY REVERSE MICELLES

Reverse micelles can be used for the recovery and concentration of pro teins by traditional liquid-liquid extraction techniques. The efficien cy of protein extraction depends on some parameters such as pH value o f the aqueous phase because the main factor governing the solubilizati on process is the electrostatic interaction between the protein and th e charged surfactant headgroups. The extraction of enzymatic protein a lpha-amylase has been carried out using an aqueous phase composed of a borate buffer 25 mM and an organic phase consisting of isooctan, octa nol (1% v/v) and cationic surfactant TOMAC. The experiments have been performed at different pH values and surfactant concentrations. The re sults have shown that the enzyme extraction improved through the incre ase of the aqueous pH value and TOMAC concentration. The molar ratio w ater to surfactant (W0) depended on the amount of protein transferred into the organic phase.