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Decolorization of melanin by lignin peroxidase fromPhanerochaete chrysosporium

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Abstract

Melanin was decolorized by lignin peroxidase fromPhanerochaete chrysosporium. This decolorization reaction showed a Michaelis-Mentens type relationship between the decolorization rate and concentration of two substrates: melanin and hydrogen peroxide. Kinetic constants of the decolorization reaction were 0.1 OD475/min (V max) and 99.7 mg/L (K m) for melanin and 0.08 OD475/min (V max) and 504.9 μM (K m) for hydrogen peroxide, respectively. Depletion of hydrogen peroxide interrupted the decolorization reaction, indicating the essential requirement of hydrogen peroxide. Pulsewise feeding of hydrogen peroxide continued the decolorizing reaction catalyzed by lignin peroxidase. These results indicate that enzymatic decolorization of melanin has applications in the development of new cosmetic whitening agents.

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Authors and Affiliations

  1. Department of Biological Engineering, Inha University, 402-751, Incheon, Korea

    Sung Hwan Woo, Jeung Suk Cho, Baek Seok Lee & Eun Ki Kim

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  1. Sung Hwan Woo
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  2. Jeung Suk Cho
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  3. Baek Seok Lee
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  4. Eun Ki Kim
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Correspondence to Eun Ki Kim.

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Woo, S.H., Cho, J.S., Lee, B.S. et al. Decolorization of melanin by lignin peroxidase fromPhanerochaete chrysosporium . Biotechnol. Bioprocess Eng. 9, 256–260 (2004). https://doi.org/10.1007/BF02942340

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  • DOI: https://doi.org/10.1007/BF02942340

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