Effective melanin degradation by a synergistic laccase-peroxidase enzyme complex for skin whitening and other practical applications.

Affiliation

Department of Biotechnology, Korea University, Seoul, Republic of Korea. Electronic address: [Email]

Abstract

Melanin is major cause of dark skin, which is regarded as social status in eastern Asia. As a result, researchers in cosmetic industries are developing skin whitening agents. Melanin can be decolorized by many oxidative enzymes. Laccase (CueO) from Escherichia coli and dye-decolorizing peroxidase (DyP) from Bacillus subtilis were merged with the dockerin domain of endoglucanase B from Clostridium cellulovorans. Scaffoldin has great potential to exert structural benefits that enable complementary enzyme effects. The carbohydrate binding module (CBM) in scaffoldin was replaced with the melanin binding peptide (MBP) to increase melanin binding and thereby enhance melanin degradation. The modified scaffoldin exhibits a nearly 64% increase in specific binding to melanin over that of the native scaffoldin. Laccase was used to degrade melanin via the production of hydrogen peroxide, which produced synergistic activity with peroxidase. The activity of the optimized complex was approximately 6.4-fold greater than that of laccase alone. This enzyme complex can also reduce the number of melanin granules in corneocytes. Based on these results, a recombinant enzyme complex is suitable for use in melanin degradation by next generation whitening agents in the skin cosmetics industry.

Keywords

Melanin degradation,Peroxidase-laccase enzyme complex,Skin whitening,

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