Tyrosinase from Mushroom

Tyrosinase from Mushroom Research Use Only

Tyrosinase from Mushroom is a highly purified polyphenol oxidase (also known as catechol oxidase or monophenol monooxygenase) isolated from common mushroom (Agaricus bisporus). Supplied as a 50 kU lyophilized powder with a molecular weight of approximately 119.5133 kDa, this biotechnology-grade enzyme catalyzes the ortho-hydroxylation of monophenols and the oxidation of o-diphenols to o-quinones, making it a valuable tool for melanin biosynthesis studies, biosensor development, and enzymatic assays.

Scientific Overview

Mushroom tyrosinase is a copper-containing oxidase that catalyzes two key reactions: the ortho-hydroxylation of monophenols (monophenolase activity) and the oxidation of o-diphenols to o-quinones (diphenolase activity). These reactions are the rate-limiting steps in melanin biosynthesis. Due to its high stability and well-characterized kinetics, tyrosinase from Agaricus bisporus is extensively used as a model enzyme for studying copper-dependent oxidases, developing biosensors for phenolic compounds, and investigating inhibitors for cosmetic and therapeutic applications.

This Tyrosinase from Mushroom is suitable for:

• Kinetic studies of monophenolase and diphenolase activities
• Screening of tyrosinase inhibitors for skin-whitening or anti-melanoma research
• Development of biosensors for detection of phenolic compounds and catecholamines
• Protein cross-linking and melanin-like polymer synthesis
• Enzymatic assays in food science and biochemistry

Usage & Handling Guidance

Store the lyophilized powder at 20 C. Reconstitute in ultrapure water or appropriate buffer (e.g., 50 mM phosphate buffer, pH 6.57.0) immediately before use. Prepare fresh working solutions or single-use aliquots to maintain maximum enzymatic activity. The enzyme is most active near neutral to slightly acidic pH.

• Recommended applications: Enzyme kinetics, inhibitor screening, biosensor development, and phenolic oxidation assays
• Working concentration: Typically 150 U/mL depending on the substrate and assay format (optimize empirically)
• Stability: Stable when stored dry at 20 C; activity is copper-dependent and may require addition of Cu in some reconstituted forms
• Handling: Avoid strong oxidants and chelating agents that may inactivate the copper centers

What You Get

• 50 kU Tyrosinase from Mushroom as a high-purity lyophilized powder
• Well-characterized molecular weight (119.5133 kDa depending on method)
• Biotechnology-grade enzyme suitable for precise biochemical and analytical applications
• Batch-specific documentation available upon request
• For research use only (RUO)

Why Researchers Choose It

• High-purity mushroom tyrosinase with robust monophenolase and diphenolase activity
• Excellent model enzyme for studying copper-containing oxidases and melanin biosynthesis
• Widely used for inhibitor screening in cosmetic and therapeutic research
• Stable powder format for convenient long-term storage and reconstitution
• Manufactured under strict biotechnology-grade quality controls

Frequently Asked Questions (FAQ)

• What reactions does mushroom tyrosinase catalyze?
  It catalyzes the ortho-hydroxylation of monophenols (monophenolase activity) and the oxidation of o-diphenols to o-quinones (diphenolase activity).
• What is the optimal pH for activity?
  The enzyme is most active in the neutral to slightly acidic range (pH 6.07.0), though it retains activity up to pH 8.0.
• How should I reconstitute the enzyme?
  Reconstitute in ultrapure water or 50 mM phosphate buffer (pH 6.57.0). Prepare fresh solutions or aliquots for best activity.
• Is copper required for activity?
  Yes. Tyrosinase is a copper-dependent enzyme; low levels of Cu may enhance or restore activity in some preparations.
• Can this enzyme be used for biosensor development?
  Yes. It is frequently used in electrochemical and optical biosensors for detection of phenolic compounds and catecholamines.

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use in humans or animals.

References

• Mann T, Gerwat W, Batzer J, Eggers K, Scherner C, Wenck H, Stb F, Hearing VJ, Rhm KH, Kolbe L. Inhibition of Human Tyrosinase Requires Molecular Motifs Distinctively Different from Mushroom Tyrosinase. J Invest Dermatol. 2018 Jul;138(7):1601-1608.
• Strzpek-Gomka M, Gawe-Bben K, Angelis A, Antosiewicz B, Sakipova Z, Kozhanova K, Gowniak K, Kukula-Koch W. Identification of Mushroom and Murine Tyrosinase Inhibitors from Achillea biebersteinii Afan. Extract. Molecules. 2021 Feb 11;26(4):964.
• Wu X, Yin S, Zhong J, Ding W, Wan J, Xie Z. Mushroom tyrosinase inhibitors from Aloe barbadensis Miller. Fitoterapia. 2012 Dec;83(8):1706-11.
• Seo SY, Sharma VK, Sharma N. Mushroom tyrosinase: recent prospects. J Agric Food Chem. 2003 May 7;51(10):2837-53.
• Yao Y, Cheng X, Wang L, Wang S, Ren G. Mushroom tyrosinase inhibitors from mung bean (Vigna radiata L.) extracts. Int J Food Sci Nutr. 2012 May;63(3):358-61.
• Gupta SD, Masakapalli SK. Mushroom tyrosinase inhibition activity of Aloe vera L. gel from different germplasms. Chin J Nat Med. 2013 Nov;11(6):616-20.
• Ismaya WT, Tjandrawinata RR, Rachmawati H. Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials. Molecules. 2020 May 20;25(10):2368.
• Farajzadeh N, Salam , Akin M, Saki N, Koak MB. Investigation of tyrosinase enzyme (from mushroom) inhibitory activities and antioxidant properties of new fluorine-containing phthalocyanines. Arch Pharm (Weinheim). 2021 Apr;354(4):e2000340.
• Lopes TIB, Coelho RG, Honda NK. Inhibition of Mushroom Tyrosinase Activity by Orsellinates. Chem Pharm Bull (Tokyo). 2018;66(1):61-64.