Abstract
Lignin peroxidase has high potential as ingredient in skin whitening cosmetics due to its high redox potential to oxidize recalcitrant melanin. Currently crude mixtures of lignin peroxidase from fungal fermentation are usually applied to cosmetics due to the intrinsic difficulties of expression and purification. However, the present study focused on heterologous expression and purification of lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium and was further used for melanin decolorization. Results revealed that the optimum pH for melanin decolorization using LiPH8 was obtained at pH 4.0. The intermittent feeding of hydrogen peroxide (H2O2) was effectively elevating melanin decolorization efficiency up to 73%, since excessive H2O2 inactivated LiPH8. For cosmetic application, intermittent feeding of H2O2 is not feasible, thus glucose oxidase (GOx) from Aspergillus niger was employed for in-situ generation of H2O2. By optimizing the GOx and glucose concentrations, a melanin decolorization efficiency up to 63.3 ± 2.4% was obtained within 1 h and continued to 84.0 ± 1.8% in 8 h. Conclusively, lignin peroxidase-catalyzed decolorization of melanin with in-situ generated H2O2 revealed a promising approach for whitening cosmetics applications.
Highlights
The skin color is mainly determined by the presence of a pigmented polymer called melanin and their production is regulated by multiple genes in the specialized cells of skin epidermis called melanocytes [1]
Lignin peroxidase is a promising catalyst for efficient decolorization of melanin since it shows a high redox potential to oxidize veratryl alcohol
The results showed that melanin decolorization efficiency was approached to the highest level of 31.9 ± 0.9% at 250 μM H2O2, it further decreased gradually with increase in H2O2 concentration (Fig. 2)
Summary
The skin color is mainly determined by the presence of a pigmented polymer called melanin and their production is regulated by multiple genes in the specialized cells of skin epidermis called melanocytes [1]. Butin from Chinese herb Spatholobus suberectus is a most effective compound that is frequently used in whitening cosmetics for inhibition of tyrosinase related proteins TRP-1 and TRP-2 [10]. These inhibitors of melanogenesis have revealed many potential side effects on skin and may cause disease like vitiligo [11]. The use of these inhibitors as active ingredient in skin whitener cosmetics should not be a favorable approach For this reason, studies are underway to decolorize melanin using enzymes instead of chemicals since enzymes holds great promise to the selective melanin decolorization with less toxicity. Improved oxidation of melanin has been noticed with lignin peroxidase rather than other peroxidases as they exhibited less sufficient redox potential to oxidize melanin [18]
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