Kinetic of Mushroom Tyrosinase Inhibition by Benzaldehyde Derivatives
| Author | Shabnam Maghsoudi | en |
| Author | Hadi Adibi | en |
| Author | Marzieh Hamzeh | en |
| Author | Mohammad Reza Ashrafi-Kooshk | en |
| Author | Mostafa Rezaei-Tavirani | en |
| Author | Reza Khodarahmi | en |
| Orcid | Mostafa Rezaei-Tavirani [0000-0003-1767-7475] | en |
| Issued Date | 2013-12-31 | en |
| Abstract | Polyphenol oxidase (PPO), known as tyrosinase (EC 1.14.18.1), is a multifunctional copper-containing oxidase which catalyzes the rate-limiting step in the formation of melanin from tyrosine. This enzyme is responsible not only for enzymatic browning in plants but also for melanogenesis in mammals. Thus, tyrosinase inhibitors have a huge impact on industry and the economy. In the current study, at first the enzyme was purified and then we evaluated inhibitory potency of three benzaldehyde derivatives: 2,4-dihydroxybenzaldehyde, 3,4-dihydroxybenzaldehyde and 4-dimethylaminobenzaldehyde on diphenolase activity of the purified mushroom tyrosinase, compared to kojic acid. Despite their close structural similarity, 2,4-dihydroxybenzaldehyde was found as a potent and competitive inhibitor while a weak uncompetitive inhibition was observed for 4-dimethylaminobenzaldehyde. Further complementary studies on these types of inhibitors, as potential drug candidates for treating abnormal melanin pigmentation, are needed. | en |
| DOI | https://doi.org/ | en |
| URI | https://brieflands.com/journals/jrps/articles/147749 | en |
| Keyword | Tyrosinase | en |
| Keyword | Polyphenol Oxidase (PPO) | en |
| Keyword | Benzaldehyde Derivatives | en |
| Publisher | Brieflands | en |
| Title | Kinetic of Mushroom Tyrosinase Inhibition by Benzaldehyde Derivatives | en |
| Type | Research Article | en |
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