Purification and characterization of melanogenic enzyme tyrosinase from button mushroom
Open accessAbstract
Melanogenesis is a biosynthetic pathway for the formation of the pigment melanin in human skin. A key enzyme, tyrosinase, catalyzes the first and only rate-limiting steps in melanogenesis. Since the discovery of its melanogenic properties, tyrosinase has been in prime focus and microbial sources of the enzyme are sought.Agaricus bisporus widely known as the common edible mushroom, it’s taking place in high amounts of proteins, enzyme, carbohydrates, fibers, and low fat contents are frequently cited in the literature in relation to their nutritional value. In the present study tyrosinase from Agaricus bisporus was purified by ammonium sulphate precipitation, dialysis followed by gel filtration chromatography on Sephadex G-100, and ion exchange chromatography on DEAE-Cellulose; the enzyme was purified, 16.36-fold to give 26.6% yield on total activity in the crude extract and final specific activity of 52.19 U/mg. The SDS-PAGE electrophoresis showed a migrating protein band molecular weight of 95 kDa. The purified tyrosinase was optimized and the results revealed that the optimum values are pH 7.0 and temperature 35°C. The highest activity was reported towards its natural substrate, L-DOPA, with an apparent Km value of 0.933 mM. This indicated that tyrosinase purified from Agaricus bisporus is a potential source for medical applications.
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Fungi like Agaricus bisporus, A. niger, Sphacelotheca reiliana, and Dothistroma septosporum can synthesize natural DOPA melanin without exogenous substrate addition.
“In contrast, fungi like Agaricus bisporus [22,23], A. niger and Sphacelotheca reiliana [24], and Dothistroma septosporum [25] can synthesize natural DOPA melanin without exogenous substrate addition.”
From Fungal Melanin in Plant Pathogens: Complex Biosynthesis Pathways and Diverse Biological Functions (2025) · cites this paper as [22]
The Abstract identifies Agaricus bisporus as a source of tyrosinase active toward L-DOPA, and the Introduction links fungal tyrosinases to melanin biosynthesis. But the paper does not establish that A. bisporus synthesizes DOPA melanin without added substrate; the Methods (§2.4) describe an assay in which L-DOPA was added. This citation is attached to A. bisporus, not the other fungi in the sentence. (LLM, conf=0.86)
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Research works printed but not linked: 26
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Cited by
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Fungal Melanin in Plant Pathogens: Complex Biosynthesis Pathways and Diverse Biological Functions
Jia, H., Liu, N., Zhang, L., Li, P., Meng, Y., Yuan, W., Li, H., Tantai, D., Qu, Q., Cao, Z., et al. (2025) · Plants · doi:10.3390/plants14142121 · Cited by 18 · see citing works
- Authors
- Zaidi, K. U., Ali, A. S., & Ali, S. A.
- Affiliations
- People’s University (IN)
- Department of Biotechnology, Saifia College of Science, Bhopal 462001, India
- Corresponding author
- Ali, Ayesha S.
- Venue
- Enzyme Research
- Publisher
- Wiley
- Published
- 2014-08-14
- Volume
- 2014
- Pages
- 1-6
- ISSN
- 2090-0406 (ISSN-L)
- 2090-0414
- PMC
- PMC4150416
- OpenAlex
- W2103453409
- Cited by
- 76
- References
- 0
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 18 · 2023: 4 · 2022: 7 · 2021: 5 · 2020: 3 · 2019: 3 · 2018: 9 · 2017: 7 · 2016: 3 · 2015: 3
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Enzyme Research (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Metabolism and Applications
- Keywords
- tyrosinase, Agaricus bisporus, melanogenesis, enzyme purification, L-DOPA, substrate specificity, enzyme kinetics, pH and temperature optimum, mushroom proteins
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