Elimination of hydrogen peroxide enhances tyrosinase-catalyzed synthesis of theaflavins
| Autor: | Asako Narai-Kanayama, Tsutomu Nakayama, Aya Kawashima, Yuuka Uchida |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification 0303 health sciences Hydrogen biology Autoxidation Tyrosinase chemistry.chemical_element Bioengineering Gallate 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Catalysis 03 medical and health sciences chemistry.chemical_compound Enzyme chemistry Catalase 010608 biotechnology biology.protein Hydrogen peroxide 030304 developmental biology Nuclear chemistry |
| Zdroj: | Process Biochemistry. 85:19-28 |
| ISSN: | 1359-5113 |
| DOI: | 10.1016/j.procbio.2019.07.004 |
| Popis: | In this study, we found that hydrogen peroxide was generated during the separate incubation of four catechins, (-)-epicatechin, (-)-epigallocatechin, and their galloylated forms, in the absence or presence of mushroom tyrosinase (EC 1.14.18.1). In particular, autooxidation of (-)-epigallocatechin and enzymatic oxidation of (-)-epicatechin gallate contributed to the increase of hydrogen peroxide. We confirmed the hydrogen peroxide-induced inactivation of tyrosinase and found that hydrogen peroxide was also generated during the tyrosinase-catalyzed synthesis of theaflavins by selectively combining two types of catechins, diphenol- and pyrogallol-types. Elimination of hydrogen peroxide by co-incubation with bovine catalase (EC 1.11.1.6) increased the products in synthetic reactions for TF1, TF2A, TF2B, and TF3 by 15%, 16%, 45%, and 18%, respectively. Based on the prospective mechanism of the tyrosinase-catalyzed synthesis of theaflavins, the yield of TF2B increased by elevating the initial ratio of (-)-epigallocatechin/(-)-epicatechin gallate in the reaction media. Furthermore, under such conditions, there were clear ameliorative effects of catalase on the tyrosinase-catalyzed synthesis of TF2B, reaching 3.1-fold increase of the product compared to the reaction without catalase. These results support a novel strategy to use both tyrosinase and catalase for the efficient synthesis of theaflavins from catechins. |
| Databáze: | OpenAIRE |
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