Recombinant Lignin Peroxidase with Superior Thermal Stability and Melanin Decolorization Efficiency in a Typical Human Skin-Mimicking Environment

• DOI: 10.1021/acs.biomac.3c00123
• Publication Date: 2023-04-19T18:54:35Z
• Authors: Hyeryeong Gye; Heeyeon Baek; Seunghyun Han; Haeun Kwon; Trang Vu Thien Ng...; Le Thanh Mai Pham; Seunghyun Kang; Youn Hwa Nho; Dong Woog Lee; Yong Hwan Kim
• Keywords: Human skin; Phanerochaete; Thermal Stability; Lignin peroxidase

Recently, the desire for a safe and effective method skin whitening has been growing in cosmetics industry. Commonly used tyrosinase-inhibiting chemical reagents exhibit side effects. Thus, recent studies have focused on performing melanin decolorization with enzymes as an alternative due to low toxicity of their ability decolorize selectively. Herein, 10 different isozymes were expressed recombinant lignin peroxidases (LiPs) from Phanerochaete chrysosporium (PcLiPs), PcLiP isozyme 4 (PcLiP04) was selected its high stability activity at pH 5.5 37 °C, which is close human conditions. In vitro results indicated that PcLiP04 exhibited least 2.9-fold higher efficiency than well-known peroxidase (PcLiP01) typical skin-mimicking environment. The interaction force between films measured by surface forces apparatus (SFA) revealed harbors disrupted structure, possibly interrupting π–π stacking and/or hydrogen bonds. addition, 3D reconstructed pigmented epidermis model showed decrease area 59.8% using PcLiP04, suggests exhibits strong potential whitening.