glucosyl-α-(1->6)-puerarin

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 异黄酮类化合物
• 英文名称: glucosyl-α-(1->6)-puerarin
• 英文别名: 7-hydroxy-3-(4-hydroxyphenyl)-8-[(2R,3R,4R,5S,6R)-3,4,5-trihydroxy-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxymethyl]oxan-2-yl]chromen-4-one
• 化学式: C₂₇H₃₀O₁₄
• 分子量: 578.527
• InChiKey: LNYIOXJTNSDQBI-UMUAIXDKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.1
• 重原子数：
  41
• 可旋转键数：
  6
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  236
• 氢给体数：
  9
• 氢受体数：
  14

反应信息

• 作为产物：
  描述：

  maltotriose 、 8-β-D-glucopyranosyl-7,4'-dihydroxyisoflavone 在 Bacillus stearothermophilus maltogenic amylase 、 soluble starch 作用下， 反应 0.75h， 生成 glucosyl-α-(1->6)-puerarin 、 maltosyl-α-(1->6)-puerarin
  参考文献：
  名称：

  In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase

  摘要：

  Puerarin (daidzein 8-C-glucoside), the most abundant isoflavone in Puerariae radix, is prescribed to treat coronary heart disease, cardiac infarction, problems in ocular blood flow, sudden deafness, and alcoholism. However, puerarin cannot be given by injection due to its low solubility in water. To increase its solubility, puerarin was transglycosylated using various enzymes. Bacillus stearothermophilus maltogenic amylase (BSMA) was the most effective transferase used compared with Thermotoga maritinta maltosyl transferase (TMMT), Thermus scotoductus 4-alpha-glucanotransferase (TS4alphaGTase), and Bacillus sp. 1-5 cyclodextrin glucanotransferase (BSCGTase). TMMT and TS4alphaGTase lacked acceptor specificity for puerarin, which lacks an O-glucoside linkage between D-glucose and 7-OH-daidzein. The yield exceeded 70% when reacting 1% puerarin (acceptor), 3.0% soluble starch (donor), and 5U/100muL BSMA at 55degreesC for 45 min. The two major transfer products of the BSMA reaction were purified using C-18 and GPC chromatography. Their structures were identified as alpha-D-glucosyl-(1-->6)-puerarin and alpha-D-maltosyl-(1-->6)-puerarin using ESI* TOF MS-MS and C-13 NMR spectroscopy. The solubility of the transfer products was 14 and 168 times higher than that of puerarin, respectively. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2004.09.017

文献信息

• In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase
  作者：Dan Li、Sung-Hoon Park、Jae-Hoon Shim、Hee-Seob Lee、Shuang-Yan Tang、Cheon-Seok Park、Kwan-Hwa Park

  DOI：10.1016/j.carres.2004.09.017

  日期：2004.12

  Puerarin (daidzein 8-C-glucoside), the most abundant isoflavone in Puerariae radix, is prescribed to treat coronary heart disease, cardiac infarction, problems in ocular blood flow, sudden deafness, and alcoholism. However, puerarin cannot be given by injection due to its low solubility in water. To increase its solubility, puerarin was transglycosylated using various enzymes. Bacillus stearothermophilus maltogenic amylase (BSMA) was the most effective transferase used compared with Thermotoga maritinta maltosyl transferase (TMMT), Thermus scotoductus 4-alpha-glucanotransferase (TS4alphaGTase), and Bacillus sp. 1-5 cyclodextrin glucanotransferase (BSCGTase). TMMT and TS4alphaGTase lacked acceptor specificity for puerarin, which lacks an O-glucoside linkage between D-glucose and 7-OH-daidzein. The yield exceeded 70% when reacting 1% puerarin (acceptor), 3.0% soluble starch (donor), and 5U/100muL BSMA at 55degreesC for 45 min. The two major transfer products of the BSMA reaction were purified using C-18 and GPC chromatography. Their structures were identified as alpha-D-glucosyl-(1-->6)-puerarin and alpha-D-maltosyl-(1-->6)-puerarin using ESI* TOF MS-MS and C-13 NMR spectroscopy. The solubility of the transfer products was 14 and 168 times higher than that of puerarin, respectively. (C) 2004 Elsevier Ltd. All rights reserved.