THE SYNTHESES OF CATECHIN-GLUCOSIDES BY TRANSGLYCOSYLATION WITH LEUCONOSTOC-MESENTEROIDES SUCROSE PHOSPHORYLASE
THE SYNTHESES OF CATECHIN-GLUCOSIDES BY TRANSGLYCOSYLATION WITH LEUCONOSTOC-MESENTEROIDES SUCROSE PHOSPHORYLASE
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DOI：
10.1271/bbb.57.2010
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发表时间：
1993-12-01
影响因子：
1.6
通讯作者：
SEKINE, H
中科院分区：
文献类型：
--
作者：
KITAO, S;ARIGA, T;SEKINE, H
来自肠膜明串珠菌的蔗糖磷酸化酶被发现催化从蔗糖到儿茶素的转糖基化。所有儿茶素都是有效的糖基受体，它们的转移率都在40%以上。酶的受体专一性顺序为：（-）-表儿茶素没食子酸酯=（+）-儿茶素>（-）-表儿茶素>（-）-表没食子儿茶素没食子酸酯>（-）-表没食子儿茶素。从100 mg（+）-儿茶素中获得约150 mg纯化的转移产物。经二次离子质谱分析、酶解产物成分分析和核磁共振分析，确定其结构为（+）-儿茶素3 '-O-α-D-吡喃葡萄糖苷（C-G）。C-G的抗布朗宁能力明显高于（+）-儿茶素。C-G在水中的溶解度比（+）-儿茶素高50倍。C-G在核黄素水溶液体系中的抗氧化活性与（+）-儿茶素相当。此外，C-G强烈抑制酪氨酸酶，与酪氨酸酶的底物（+）-儿茶素相反。以L-β-3，4-二羟基苯丙氨酸为底物，C-G的抑制模式为竞争性。
Sucrose phosphorylase from Leuconostoc mesenteroides was found to catalyze transglycosylation from sucrose to catechins. All catechins were efficient glycosyl acceptors and their transfer ratios were more than 40%. The acceptor specificity of the enzyme decreased in the following order: (-)-epicatechin gallate=(+)-catechin>(-)-epicatechin>(-)-epigallocatechin gallate>(-)-epigallocatechin. About 150 mg of the purified transfer product was obtained from 100 mg of (+)-catechin. Its structure was identified as (+)-catechin 3'-O-alpha-D-glucopyranoside (C-G) on the bases of the secondary ion mass spectrometry analysis, the component analyses of its enzymatic hydrolyzates, and the nulcear magnetic resonance analysis. The browning resistance of C-G to light irradiation was greatly increased compared to that of (+)-catechin. The solubility of C-G in water was 50-fold higher than that of (+)-catechin. The antioxidative activity of C-G in the aqueous system with riboflavin was almost equal to that of (+)-catechin. In addition, C-G strongly inhibited tyrosinase, in contrast with (+)-catechin, which is the substrate of tyrosinase. The inhibitory pattern of C-G was competitive using L-beta-3,4-dihydroxyphenylalanine as a substrate.