The use of liposomes as enzyme carriers. I. Dependence of enzyme stability on the method of preparation.

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Abstract
The stability of liposomal enzymes and the encapsulation efficiency of reverse-phase evaporation vesicles (REV) were investigated in comparison with those of the original small multilamellar liposomes (SML), using elastase as a model enzyme. The encapsulation efficiency of REV was greatly superior to that of SML. REV retarded the inactivation of elastase in the neutral pH region, as did SML. The REV method should be useful for the preparation of carriers to encapsulate not only elastase but other macromolecules. At lower pH, pH 2.63, in which elastase was rapidly inactivated, REV accelerated the inactivation of the enzyme; however, SML retarded it, as at neutral pH. Since liposomes prepared by different methods have significantly different physicochemical properties, further and more precise studies on the methods of preparation are required.