Arthrobacter属由来のβ-フルクトフラノシダーゼの糖転移反応によるヒロドキノンとエピカテキンの配糖化反応
書誌事項
- タイトル別名
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- Transglycosylation of Hydroquinone and Epicatechin by .BETA.-Fructofuranosidase from Arthrobacter sp.
- Transglycosylation of Hydroquinone and Epicatechin by β-Fructofuranosidase from Arthrobacter sp
- Transglycosylation of Hydroquinone and Epicatechin by ベータ Fructofuranosidase from Arthrobacter sp
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抄録
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.
収録刊行物
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 49 (2), 115-121, 2002
日本応用糖質科学会
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詳細情報
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- CRID
- 1390282681270237568
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- NII論文ID
- 10008253494
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- NII書誌ID
- AN10453916
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- ISSN
- 13403494
- 18807291
- 13447882
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- NDL書誌ID
- 6142257
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可