Oxidative coupling reaction of arbutin and gentisate catalyzed by horseradish peroxidase
| Autor: | Kenji Hozono, Tadamasa Terai, Taro Kiso, Motohiro Shizuma, Hirofumi Nakano, Hiromi Murakami, Takaaki Kiryu |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
biology Process Chemistry and Technology Tyrosinase Arbutin Glycoside Bioengineering Biochemistry Horseradish peroxidase Medicinal chemistry Catalysis Enzyme catalysis chemistry.chemical_compound Non-competitive inhibition chemistry biology.protein Moiety Organic chemistry Peroxidase |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic. 45:50-56 |
| ISSN: | 1381-1177 |
| DOI: | 10.1016/j.molcatb.2006.11.007 |
| Popis: | Horseradish peroxidase catalyzed an oxidative coupling reaction of 4′-hydroxyphenyl β-glucoside (arbutin) and 2,5-dihydroxybenzoic acid sodium salt (gentisate) using H2O2 as an electron acceptor to yield a precipitating yellow compound. An approximate arbutin/gentisate ratio of 1:2 was effective for the synthesis. The addition of 100–300 mM H2O2 to the mixtures of 100 mM arbutin and 200 mM gentisate attained optimized yields of 50–60% in the initial arbutin. Mass spectrometry, infrared spectroscopy, and nuclear magnetic resonance data revealed that the precipitated compound was a novel glycoside bound between the C3′-position of the hydroxyphenyl moiety of arbutin and the C6-position of gentisate, followed by the intramolecular esterification between the phenolic hydroxyl group of arbutin moiety and the carboxyl group of gentisate moiety. The product exerted anti-oxidation and competitive inhibition against mushroom tyrosinase higher than arbutin, while it inhibited mouse melanoma tyrosinase lower than arbutin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect