Seborrheic dermatitis (SD) is the most common dermatological disease in more than 50% of the population all over the world. Malassezia species are lipophilic yeasts that cause seborrheic dermatitis and dandruff in humans. The treatment of SD is mainly based on azole antifungal drugs that are targeted against biosynthesis of sterols. But these chemicals have poor compliance, emerging resistance, and low bioavailability. Interestingly, Malassezia species secrete several lipases that are responsible of the production of fatty acids and inflammatory cytokines. Novel synthetic and natural agents act on lipase but has low solubility and bioavailability. β-cyclodextrin (β-CD) as an additive has attracted attention for enhance solubility and drug delivery. Therefore, the aim of study was evaluation of β-CD influence on lipase structure and enzymatic activity for hydrolysis of acylglycerides by lipase. Modern methods as UV-spectroscopy, fluorescence assay and electron microscopy with TEM were used. The results showed that lipase could decrease yield of oleic acid in presence of β-CD. The UV spectroscopy and fluorescence assay demonstrated that the absorbance and fluorescence of lipase decreased with increasing concentration of β-CD due to surface interaction and change of enzyme configuration. Moreover, electron microscopy with TEM showed that lipase formed a special conglomerate with β-CD for changing hydrolysis that can be useful for drug delivery of lipase inhibitors. Overall results indicate that β-CD could change enzymatic activity of the lipase and can be considered as promising carrier for drug delivery of lipase inhibitors.
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