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Abstract
Lipase from Candida cylindracea (CCL) was incorporated into vesicles of a polymerisable zwitterionic surfactant: bis[2-(pentacosa-10,12-diynoyloxy)ethyl]-2-aminoethanesulfonic acid (BPAS). Vesicle systems of BPAS were characterised in terms of morphology (Electron Microscopy) and stability. Polymerisation of BPAS vesicles did not alter the morphology and polymeric vesicles were considerably more stable than the monomeric analogues. CCL was incorporated into the vesicle membrane by spontaneous insertion. The enzyme remained fully active after incorporation into the vesicle bilayer; especially in homogeneous assay mixtures the vesicle incorporated enzyme showed an increased activity when compared to the free lipase. The stability of free and incorporated lipase was determined by measuring the residual activity of the various systems when mixed with ethanol (50% v/v) or 2-(n-butoxy)ethanol (37.5% v/v), at 50°C and 60°C and in the presence of the proteolytic enzyme trypsin. In all cases the vesicle incorporated enzyme showed an increased stability against the denaturating conditions.