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TYROSINASE

Base Information
  • Chemical Name:TYROSINASE
  • CAS No.:9002-10-2
  • Molecular Formula:NULL
  • Molecular Weight:0.00000
  • Hs Code.:
TYROSINASE

Synonyms:Oxygenase, monophenol mono- (9CI);Tyrosine-dopa oxidase;Cresolase;Chlorogenic acid oxidase;Tyrosinase;Chlorogenic oxidase;Polyphenol oxidase;Triphenolase;Polyphenolase;Phenolase;Chlorogenate oxidase;T 7755;Monophenol oxidase;Laccase M 120;Sigma T 7755;Polyaromatic oxidase;Monophenol monooxidase;o-Phenolase;E.C. 1.14.18.1;Suberase;Dihydroxyphenylalanine oxidase;Phenol oxidase;Gluteomorphinase;Pyrocatechol oxidase;Monophenolase;

Suppliers and Price of TYROSINASE
Supply Marketing:
Business phase:
The product has achieved commercial mass production*data from LookChem market partment
Manufacturers and distributors:
  • Manufacture/Brand
  • Chemicals and raw materials
  • Packaging
  • price
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000?unit/mg solid
  • 1000000 units
  • $ 1890.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000unit/mg solid
  • 1mu
  • $ 1820.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000?unit/mg solid
  • 500000 units
  • $ 1210.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000unit/mg solid
  • 500ku
  • $ 1170.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000?unit/mg solid
  • 250000 units
  • $ 803.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000unit/mg solid
  • 250ku
  • $ 774.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000?unit/mg solid
  • 50000 units
  • $ 195.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000unit/mg solid
  • 50ku
  • $ 187.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000?unit/mg solid
  • 25000 units
  • $ 114.00
  • Sigma-Aldrich
  • Tyrosinase from mushroom lyophilized powder, ≥1000unit/mg solid
  • 25ku
  • $ 110.00
Total 38 raw suppliers
Chemical Property of TYROSINASE
Chemical Property:
  • Melting Point:89-94 °C 
  • PSA:0.00000 
  • LogP:0.00000 
  • Storage Temp.:−20°C 
Purity/Quality:

99%, *data from raw suppliers

Tyrosinase from mushroom lyophilized powder, ≥1000?unit/mg solid *data from reagent suppliers

Safty Information:
  • Pictogram(s):  
  • Hazard Codes:Xn 
  • Statements: 42 
  • Safety Statements: 22-24/25-45 
MSDS Files:

Total 1 MSDS from other Authors

Useful:
  • General Description Tyrosinase is a key enzyme in melanin biosynthesis, and its inhibition is of significant interest in treating hyperpigmentation disorders and developing cosmetic agents. Studies have shown that certain compounds, such as daedalin A and quercinol, exhibit tyrosinase inhibitory activity, with daedalin A demonstrating stronger effects at higher concentrations, likely due to structural differences. Additionally, 3-hydroxyflavone derivatives have been synthesized and evaluated as potent tyrosinase inhibitors, with molecular modeling revealing their binding interactions with the enzyme. These findings highlight the potential of tyrosinase inhibitors in both therapeutic and cosmetic applications.
Refernces

Asymmetric syntheses of daedalin A and quercinol and their tyrosinase inhibitory activity

10.1016/j.bmcl.2009.12.034

The study focuses on the asymmetric syntheses of daedalin A and quercinol, which are compounds derived from mushroom mycelia cultures with potential tyrosinase inhibitory activity, important for preventing hyperpigmentation in cosmetics. The chemicals used in the study include 4-methoxyphenol, vinyloxirane, Pd(PPh3)4 (a palladium catalyst), acetic anhydride, ethyl acetate, and various other reagents for reactions such as acetylation, Claisen rearrangement, Sharpless asymmetric epoxidation, reduction, oxidation, and deprotection. These chemicals served the purpose of synthesizing daedalin A and quercinol through a series of chemical reactions, with the aim of studying their inhibitory effects on tyrosinase, a key enzyme in melanin biosynthesis. The study found that daedalin A had stronger tyrosinase inhibitory activity than quercinol at high concentrations, suggesting different mechanisms of action due to their opposite stereochemistry at the C-2 position.

Exploring 3-hydroxyflavone scaffolds as mushroom tyrosinase inhibitors: synthesis, X-ray crystallography, antimicrobial, fluorescence behaviour, structure-activity relationship and molecular modelling studies

10.1080/07391102.2020.1805364

The study focuses on the synthesis and evaluation of 3-hydroxyflavone derivatives as inhibitors of mushroom tyrosinase, an enzyme involved in melanin production. A series of 3-hydroxyflavone scaffolds were synthesized using the Algar-Flynn-Oyamada reaction, and these compounds were screened for their in vitro inhibitory activity against tyrosinase. The chemicals used in the study included o-hydroxyacetophenone, various substituted benzaldehydes, sodium hydroxide, methanol, and hydrogen peroxide. These chemicals served the purpose of reacting together to form the desired 3-hydroxyflavone derivatives, which were then tested for their antimicrobial potential and their ability to inhibit tyrosinase, providing insights into their potential use as therapeutic agents for pigmentation-related disorders and as antimicrobial agents. The study also involved the use of spectroscopic techniques and mass spectrometry for compound characterization, as well as molecular modeling to explore binding interactions with the tyrosinase enzyme.

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