Functional characterization of melanin decolorizing extracellular peroxidase of bjerkandera adusta

Jina Baik, Anwesha Purkayastha, Kyung Hye Park, Taek Jin Kang

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

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 Mn2+ . 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.

Original languageEnglish
Article number762
JournalJournal of Fungi
Volume7
Issue number9
DOIs
StatePublished - Sep 2021

Keywords

  • Bjerkandera adusta
  • Enzymatic melanin decolorization
  • Peroxidase

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