Abstract
Catalase-loaded solid lipid nanoparticles (SLNs) were prepared by the double emulsion method (w/o/w) and solvent evaporation techniques, using acetone/methylene chloride (1:1) as an organic solvent, lecithin and triglyceride as oil phase and Poloxmer 188 as a surfactant. The optimized SLN was prepared by lecithin: triglyceride ratio (5%), 20-second + 30-second sonication, and 2% Poloxmer 188. The mean particle size of SLN was 296.0 ± 7.0 nm, polydispersity index range and zeta potential were 0.322–0.354 and −36.4 ± 0.6, respectively, and the encapsulation efficiency reached its maximum of 77.9 ± 1.56. Catalase distributed between the solid lipid and inner aqueous phase and gradually released from Poloxmer coated SLNs up to 20% within 20 h. Catalase-loaded SLN remained at 30% of H2O2-degrading activity after being incubated with Proteinase K for 24 h, while free catalase lost activity within 1 h.
Highlights
Active oxygen species such as hydrogen peroxide are readily generated in many cells by metabolic processes such as respiration, ischemia/reperfusion, and oxidation of fatty acids, and they are highly toxic to cells by damaging such components as DNA, lipids, and enzymes
Influence of Organic Solvent Species and Emulsifying Operation on Catalase Activity. Experimental constraints such as sonication and organic solvent might disturb the activity of catalase
SDS-PAGE and circular dichroism spectroscopy analysis showed that loading into solid lipid nanoparticles (SLNs) neither induced catalase fragmentation nor significantly changed in secondary structure
Summary
Active oxygen species such as hydrogen peroxide are readily generated in many cells by metabolic processes such as respiration, ischemia/reperfusion, and oxidation of fatty acids, and they are highly toxic to cells by damaging such components as DNA, lipids, and enzymes. Catalase (CAT, EC 1.11.1.6), an enzyme that reduces hydrogen peroxide to water, is a potential drug to prevent the accumulation of toxic levels of hydrogen peroxide. Targeting catalase to endothelial cells lining the blood vessel lumen alleviates vascular oxidative stress in animal models. As a therapeutic protein, it does not possess the required physicochemical properties to be absorbed at their target site, or reach or enter the cell. Premature elimination from circulation, as well as inactivation by inhibitors and proteases, limits the effectiveness and utility of this enzyme [1]. The study of delivery and targeting systems is needed to overcome these disadvantages and improve its performance
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