ArticleFolia microbiologica2021
Production and characterization of crude laccase from Irpex sp. JS7 that decolorizes synthetic and natural melanin.
Article in Folia microbiologica, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed, 3 citations in OpenAlex.
- Purification and characterization of an alkali-organic solvent-stable laccase with dye decolorization capacity from newly isolated Lysinibacillus fusiformis W11.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
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2 authors at 1 institution in 1 country.
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Abstract
The JS7 strain, isolated from an old forest tree, produces extracellular enzymes that decolorize synthetic and natural melanin from human hair. Phylogenetic analysis based on the internal transcribed spacer (ITS) sequence indicated that JS7 belongs to the genus Irpex. The JS7 strain has laccase activity while it lacks manganese and lignin peroxidase activity, which suggests that the JS7 strain melanin decolorization activity originated from laccase. Laccase production from the Irpex sp. JS7 improved three-fold in the presence of veratryl alcohol, compared to without an inducer. The optimum pH and temperature for melanin decolorization were 7.5 and 40 °C, respectively. The crude enzyme half-life at 25 °C was about 100 days, and it had high storage stability. The melanin decolorization reaction rate by the crude enzyme conformed to typical enzyme kinetic principles. In the presence of syringaldehyde as a redox mediator, the melanin decolorization rate was 75% within 5 days, similar to the decolorization percentage obtained using the enzyme alone. Based on these results, the Irpex sp. JS7 enzyme is suitable for use in melanin decolorization by whitening agents in the cosmetics industry.
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