Investigation of Complexing Properties with Polyethyleneimine of Some Commercial Lipases

Abstract

Lipases are enzymes used in various industrial process and are immobilized to increase their applicability as biocatalysts. Ionic polymers such as polyethyleneimine (PEI) make possible the co-precipitation of enzymes. In this study, complexation and aggregation with PEI of enzymes were investigated with commercial enzymes from Novozyme 51032 (Fusarium solani pisi), Palatase 20000 L (Rhizomucor miehei), Lipolase 100 L (Thermomyces lanuginosus), Lipozyme CAL B L (Candida antarctica B) and Amano (Pseudomonas fluorescens) using PEI as a linker and aggregation agent. The highest percentage of PEI-enzyme agregate was obtained for Novozyme 51032, Palatase 20000 L and Lipolase 100 L at the PEI/enzyme ratio of a 1/20-1/80 range. This study documented that Lipozyme CAL B L and (Amano) P. fluorescens enzyme preparations failed to occur precipitates resulting PEI-enzyme aggregates. The some commercial lipase preparations may contain various impurity components that prevent complexation or aggregation with PEI. Complexing with PEI of lipases is based on of basis electrostatic interaction of enzyme with PEI as a cationic polymer resulting in PEI-lipase aggregates.