ArticleScientific reports2020
Enzymatic decolorization of melanin by lignin peroxidase from Phanerochaete chrysosporium.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 41 citations in OpenAlex.
- Decoding Hyperpigmentation from Biological Mechanisms to Actives with Clinically Proven Topical Efficacy: A Narrative Review.Dermatology and therapy · 2026Review
- From structural complexity to circular applications: a comparative review of the enzymatic degradation of polydopamine, tannins, lignins, and melanins.RSC advances · 2026Review
- Dismantling darkness: interdisciplinary perspectives on melanin degradation.World journal of microbiology & biotechnology · 2026Review
- Identification and characterization of two AA9 lytic polysaccharide monooxygenases isolated from the enzymatic arsenal in Phanerochaete chrysosporium.Bioresources and bioprocessing · 2025Article
- Industrial applications of Phanerochaete chrysosporium lignin-degrading enzymes: current status, production challenges, and future directions.World journal of microbiology & biotechnology · 2025Review
- Self-disassembling nanoparticles as oral nanotherapeutics targeting intestinal microenvironment.Nature communications · 2025Article
- Potential of the Ethyl Acetate Fraction of Padina boergesenii as a Natural UV Filter in Sunscreen Cream FormulationLife (Basel, Switzerland) · 2023Article
- Laccase Mediator Cocktail System as a Sustainable Skin Whitening Agent for Deep Eumelanin Decolorization.International journal of molecular sciences · 2022Article
- A Secreted Lignin Peroxidase Required for Fungal Growth and Virulence and Related to Plant Immune Response.International journal of molecular sciences · 2022Article
- Functional Characterization of Melanin Decolorizing Extracellular Peroxidase ofJournal of fungi (Basel, Switzerland) · 2021Article
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Skin darkening results as a consequence of the accumulation of skin pigment melanin. To combat this, the amplitude of skin lightening agents are commercially available, most of which inhibit melanin synthesis. Decolorization of melanin is an alternative method of skin lightening. In this study, we show that lignin peroxidase (LiP), an extracellular enzyme purified from Phanerochaete chrysosporium NK-1 isolated from a forest soil can effectively degrade and decolorize melanin in vitro. Decolorization conditions including pH, temperature, incubation time, enzyme concentration, and mediator addition were investigated to optimize the reaction conditions. The results indicate that pH 3, 40 °C, 15 IU/ml, and 10 h incubation were the optimal conditions for the decolorization of the melanin. The use of the mediator, veratryl alcohol was also found effective to enhance the efficacy of the melanin decolonization, with up to 92% decolorization. The scanning electron microscopy results showed void spaces on the treated melanin granules as compared to the untreated sample, indicating the degradation of melanin. Changes in the fingerprint region of the melanin were observed. Between wavenumbers 1500-500 cm
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