Transglycosylation of Hydroquinone and Epicatechin by .BETA.-Fructofuranosidase from Arthrobacter sp

Autor:	Koki Fujita, Hirofumi Nakano, Kozo Hara, Hiromi Murakami, Kenichi Hamayasu, Sumio Kitahata, Kaname Nakagawa, Taro Kiso, Akinori Tabata
Rok vydání:	2002
Předmět:	chemistry.chemical_classification Glycosylation Chromatography biology Hydroquinone Tyrosinase Size-exclusion chromatography Glycoside Substrate (chemistry) biology.organism_classification chemistry.chemical_compound Enzyme chemistry Arthrobacter
Zdroj:	Journal of Applied Glycoscience. 49:115-121
ISSN:	1880-7291 1344-7882
DOI:	10.5458/jag.49.115
Popis:	Hydroquinone (HQ) and epicatechin (EC) were glycosylated by transfer reaction by β-fructofranosidases using sucrose (Suc) as a donor substrate. An enzyme from Arthrobacter sp. was the most effective among several enzymes tested. The glycosylation product from HQ, HQ βfructofuranoside (HQF), was synthesized most effectively at a HQ concentration of 0 .4 M and a Suc concentration of 1.0 M. HQF was isolated by gel filtration and its structure was confirmed by 13C -NMR spectroscopy. Fructosylation of EC was conducted in the presence of 5% 2-propanol in order to increase the solubility of the acceptor in the reaction system. EC gave two transfer products in a ratio of almost 7 : 2. Of the products, the main one (ECF) was isolated by silica gel chromatography, gel filtration, and preparative HPLC. 13C-NMR spectroscopy suggested glycosylation occurred at the OH group of site 3 in EC. HQF and ECF exhibited inhibition activities against mouse melanoma cell tyrosinase, a key enzyme for melanin synthesis, suggesting their potential application as skin-whitening substances.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8a056347656239735a428c33b2479439 https://doi.org/10.5458/jag.49.115 Zobrazit plný text záznamu