DENATURATION AND DEACTIVATION OF PORCINE PANCREAS LIPASE IN REVERSE MICELLE EXTRACTION

Reverse micelle extraction of porcine pancreas lipase was studied, focusing on activity yield or denaturation of the lipase as well as its fraction extracted. On the fraction extracted of the lipase, the effect of size exclusion and hydrophobic interaction are more important than that of electrostatic interaction due to the relatively high molecular weight and strong hydrophobicity of the lipase. The lipase can be solubilized into micellar phase up to 30 % in a two-phase extraction system in which two bulk solutions contact through a flat interface. The activity yield is, however, found to be very poor in this extraction system. This is related to a noncompetitive strong interaction between the lipase and anionic detergent AOT in the extraction and stripping processes. A feasible extraction system is the injection method, in which a small volume of concentrated lipase solution is mixed vigorously with micellar solution and the extraction is completed in a few seconds. An addition of adsorbents for AOT into stripping solution can be used for the stripping to reduce the inevitable interaction between the lipase and AOT. © 1990, The Society of Chemical Engineers, Japan. All rights reserved.