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Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta
Melanin pigmentation in the human skin results from complicated cellular mechanisms that remain to be entirely understood. Uneven melanin pigmentation has been counteracted by inhibiting synthesis or transfer of melanin in the skin. Recently, an enzymatic approach has been proposed, wherein the mela...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8466778/ https://www.ncbi.nlm.nih.gov/pubmed/34575800 http://dx.doi.org/10.3390/jof7090762 |
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author | Baik, Jina Purkayastha, Anwesha Park, Kyung Hye Kang, Taek Jin |
author_facet | Baik, Jina Purkayastha, Anwesha Park, Kyung Hye Kang, Taek Jin |
author_sort | Baik, Jina |
collection | PubMed |
description | Melanin pigmentation in the human skin results from complicated cellular mechanisms that remain to be entirely understood. Uneven melanin pigmentation has been counteracted by inhibiting synthesis or transfer of melanin in the skin. Recently, an enzymatic approach has been proposed, wherein the melanin in the skin is decolorized using lignin peroxidase. However, not many enzymes are available for decolorizing melanin; the most studied one is lignin peroxidase derived from a lignin degrading fungus, Phanerochaete chrysosporium. Our current study reveals that versatile peroxidase from Bjerkandera adusta can decolorize synthetic melanin. Melanin decolorization was found to be dependent on veratryl alcohol and hydrogen peroxide, but not on Mn(2+). The degree of decolorization reached over 40% in 10 min at 37 °C and a pH of 4.5. Optimized storage conditions were slightly different from those for the reaction; crude enzyme preparation was the most stable at 25 °C at pH 5.5. Since the enzyme rapidly lost its activity at 50 °C, stabilizers were screened. As a result, glycerol, a major component in several cosmetic formulations, was found to be a promising excipient. Our results suggest that B. adusta versatile peroxidase can be considered for future cosmetic applications aimed at melanin decolorization. |
format | Online Article Text |
id | pubmed-8466778 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-84667782021-09-27 Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta Baik, Jina Purkayastha, Anwesha Park, Kyung Hye Kang, Taek Jin J Fungi (Basel) Article Melanin pigmentation in the human skin results from complicated cellular mechanisms that remain to be entirely understood. Uneven melanin pigmentation has been counteracted by inhibiting synthesis or transfer of melanin in the skin. Recently, an enzymatic approach has been proposed, wherein the melanin in the skin is decolorized using lignin peroxidase. However, not many enzymes are available for decolorizing melanin; the most studied one is lignin peroxidase derived from a lignin degrading fungus, Phanerochaete chrysosporium. Our current study reveals that versatile peroxidase from Bjerkandera adusta can decolorize synthetic melanin. Melanin decolorization was found to be dependent on veratryl alcohol and hydrogen peroxide, but not on Mn(2+). The degree of decolorization reached over 40% in 10 min at 37 °C and a pH of 4.5. Optimized storage conditions were slightly different from those for the reaction; crude enzyme preparation was the most stable at 25 °C at pH 5.5. Since the enzyme rapidly lost its activity at 50 °C, stabilizers were screened. As a result, glycerol, a major component in several cosmetic formulations, was found to be a promising excipient. Our results suggest that B. adusta versatile peroxidase can be considered for future cosmetic applications aimed at melanin decolorization. MDPI 2021-09-15 /pmc/articles/PMC8466778/ /pubmed/34575800 http://dx.doi.org/10.3390/jof7090762 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Baik, Jina Purkayastha, Anwesha Park, Kyung Hye Kang, Taek Jin Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta |
title | Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta |
title_full | Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta |
title_fullStr | Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta |
title_full_unstemmed | Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta |
title_short | Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta |
title_sort | functional characterization of melanin decolorizing extracellular peroxidase of bjerkandera adusta |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8466778/ https://www.ncbi.nlm.nih.gov/pubmed/34575800 http://dx.doi.org/10.3390/jof7090762 |
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