4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-maltotriosyl-α-(1,6)-maltotrioside | 1616794-66-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-maltotriosyl-α-(1,6)-maltotrioside
• CAS: 1616794-66-1
• 化学式: C₄₉H₆₈ClNO₃₃
• 分子量: 1234.52
• InChiKey: PHFJGTAJGLZHMR-FTRDEBNCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -8.69
• 重原子数：
  84.0
• 可旋转键数：
  19.0
• 环数：
  9.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  516.27
• 氢给体数：
  17.0
• 氢受体数：
  33.0

反应信息

• 作为反应物：
  描述：

  4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-maltotriosyl-α-(1,6)-maltotrioside 在 β-glucosidase 、 α-glucosidase 、 pullulanase from Klebsiella planticola 作用下， 以 aq. acetate buffer 为溶剂， 生成 2-氯-4-硝基苯酚
  参考文献：
  名称：

  Colourimetric and fluorometric substrates for measurement of pullulanase activity

  摘要：

  Specific and highly sensitive colourimetric and fluorometric substrate mixtures have been prepared for the measurement of pullulanase and limit-dextrinase activity and assays employing these substrates have been developed. These mixtures comprise thermostable a-and b-glucosidases and either 4,6-Obenzylidene-2-chloro-4-nitrophenyl-b-maltotriosyl (1-6) a-maltotrioside (BzCNPG3G3, 1) as a colourimetric substrate or 4,6-O-benzylidene-4-methylumbelliferyl-b-maltotriosyl (1-6) a-maltotrioside (BzMUG3G3, 2) as a fluorometric substrate. Hydrolysis of substrates 1 and 2 by exo-acting enzymes such as amyloglucosidase, b-amylase and a-glucosidase is prevented by the presence of the 4,6-O-benzylidene group on the non-reducing end D-glucosyl residue. The substrates are not hydrolysed by any a-amylases studied, (including those from Aspergillus niger and porcine pancreas) and are resistant to hydrolysis by Pseudomonas sp. isoamylase. On hydrolysis by pullulanase, the 2-chloro-4-nitrophenyl-b-maltotrioside (3) or 4-methylumbelliferyl-b-maltotrioside (4) liberated is immediately hydrolysed to D-glucose and 2-chloro-4-nitrophenol or 4-methylumbelliferone. The reaction is terminated by the addition of a weak alkaline solution leading to the formation of phenolate ions in solution whose concentration can be determined using either spectrophotometric or fluorometric analysis. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2014.04.014
• 作为产物：
  描述：

  苯甲醛二甲缩醛 、 2-chloro-4-nitrophenyl-β-maltotriosyl-α-(1,6)-maltotrioside 在 对甲苯磺酸 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 14.0h， 以215 mg的产率得到4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-maltotriosyl-α-(1,6)-maltotrioside
  参考文献：
  名称：

  Colourimetric and fluorometric substrates for measurement of pullulanase activity

  摘要：

  Specific and highly sensitive colourimetric and fluorometric substrate mixtures have been prepared for the measurement of pullulanase and limit-dextrinase activity and assays employing these substrates have been developed. These mixtures comprise thermostable a-and b-glucosidases and either 4,6-Obenzylidene-2-chloro-4-nitrophenyl-b-maltotriosyl (1-6) a-maltotrioside (BzCNPG3G3, 1) as a colourimetric substrate or 4,6-O-benzylidene-4-methylumbelliferyl-b-maltotriosyl (1-6) a-maltotrioside (BzMUG3G3, 2) as a fluorometric substrate. Hydrolysis of substrates 1 and 2 by exo-acting enzymes such as amyloglucosidase, b-amylase and a-glucosidase is prevented by the presence of the 4,6-O-benzylidene group on the non-reducing end D-glucosyl residue. The substrates are not hydrolysed by any a-amylases studied, (including those from Aspergillus niger and porcine pancreas) and are resistant to hydrolysis by Pseudomonas sp. isoamylase. On hydrolysis by pullulanase, the 2-chloro-4-nitrophenyl-b-maltotrioside (3) or 4-methylumbelliferyl-b-maltotrioside (4) liberated is immediately hydrolysed to D-glucose and 2-chloro-4-nitrophenol or 4-methylumbelliferone. The reaction is terminated by the addition of a weak alkaline solution leading to the formation of phenolate ions in solution whose concentration can be determined using either spectrophotometric or fluorometric analysis. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2014.04.014