期刊
JOURNAL OF FUNGI
卷 7, 期 9, 页码 -出版社
MDPI
DOI: 10.3390/jof7090762
关键词
Bjerkandera adusta; peroxidase; enzymatic melanin decolorization
资金
- Ministry of Trade, Industry, and Energy through the Korea Evaluation Institute of Industrial Technology [20002810]
- Korea Evaluation Institute of Industrial Technology (KEIT) [20002810] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Melanin pigmentation in the human skin is a complex cellular mechanism that can be decolorized enzymatically; the study reveals that versatile peroxidase from Bjerkandera adusta shows promising results in decolorizing synthetic melanin.
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 degrees 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 degrees C at pH 5.5. Since the enzyme rapidly lost its activity at 50 degrees 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.
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