Recombinant lignin peroxidase-catalyzed decolorization of melanin using in-situ generated H2O2 for application in whitening cosmetics

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 (H 2 O 2 ) was effectively elevating melanin decolorization efficiency up to 73%, since excessive H 2 O 2 inactivated LiPH8. For cosmetic application, intermittent feeding of H 2 O 2 is not feasible, thus glucose oxidase (GOx) from Aspergillus niger was employed for in-situ generation of H 2 O 2 . 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 H 2 O 2 revealed a promising approach for whitening cosmetics applications.