Glc(a1-4)Glc(b1-4)b-Glc | 1239458-28-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: Glc(a1-4)Glc(b1-4)b-Glc
• 英文别名: (2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6S)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R,6R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 1239458-28-6
• 化学式: C₁₈H₃₂O₁₆
• 分子量: 504.442
• InChiKey: FYGDTMLNYKFZSV-VBALGWFQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.9
• 重原子数：
  34
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  269
• 氢给体数：
  11
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  纤维素二糖 、 β-环糊精 在 cyclodextrin glycosyltransferase from Paenibacillus sp. A₁₁ 作用下， 反应 2.0h， 生成 Glc(a1-4)Glc(b1-4)b-Glc 、 Glc(a1-4)Glc(a1-4)Glc(b1-4)b-Glc
  参考文献：
  名称：

  Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11

  摘要：

  Intermolecular transglucosylation of cyclodextrin glycosyltransferase (CGTase) was investigated for its use in oligosaccharide synthesis. From the kinetic parameters of the CGTase-catalyzed transglucosylation reaction, using beta-cyclodextrin (beta-CD) as the glucosyl donor and various saccharides or derivatives as acceptors, the efficient acceptors of the Paenibacillus sp. All enzyme were glucose, sorbose, lactose and cellobiose. Amongst these acceptors, cellobiose showed the highest k(cat)/K-m value. The transglucosylation yields of the reactions for cellobiose, sorbose and glucose acceptors were 78, 57 and 54%, respectively, making cellobiose the most efficient acceptor of the tested saccharides in coupling with beta-CD. The optimal condition for the coupling reaction was determined as: 2%(w/v)beta-CD and 0.5% (w/v)cellobiose, incubated with 64 U/mL of CGTase at 30 degrees C for 2 h. Two main transfer products detected by HPLC, PC1 and PC2, with retention times of 3.81 and 4.42 min, respectively, and a product ratio of 3:1, had a molecular mass of 504 and 666 Da, respectively, as analyzed by mass spectrometry. The structures suggested by NMR were a trisaccharide and a novel tetrasaccharide-containing cellobiose of the structures glc (alpha 1 -> 4) glc (beta 1 -> 4) glc and glc(alpha 1 -> 4) glc (alpha 1 -> 4) glc (beta 1 -> 4) glc, respectively. The products were found to be resistant to hydrolysis by a-amylase. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.procbio.2010.02.024

文献信息

• Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11
  作者：Wannapa Wongsangwattana、Jarunee Kaulpiboon、Kazuo Ito、Piamsook Pongsawasdi

  DOI：10.1016/j.procbio.2010.02.024

  日期：2010.6

  Intermolecular transglucosylation of cyclodextrin glycosyltransferase (CGTase) was investigated for its use in oligosaccharide synthesis. From the kinetic parameters of the CGTase-catalyzed transglucosylation reaction, using beta-cyclodextrin (beta-CD) as the glucosyl donor and various saccharides or derivatives as acceptors, the efficient acceptors of the Paenibacillus sp. All enzyme were glucose, sorbose, lactose and cellobiose. Amongst these acceptors, cellobiose showed the highest k(cat)/K-m value. The transglucosylation yields of the reactions for cellobiose, sorbose and glucose acceptors were 78, 57 and 54%, respectively, making cellobiose the most efficient acceptor of the tested saccharides in coupling with beta-CD. The optimal condition for the coupling reaction was determined as: 2%(w/v)beta-CD and 0.5% (w/v)cellobiose, incubated with 64 U/mL of CGTase at 30 degrees C for 2 h. Two main transfer products detected by HPLC, PC1 and PC2, with retention times of 3.81 and 4.42 min, respectively, and a product ratio of 3:1, had a molecular mass of 504 and 666 Da, respectively, as analyzed by mass spectrometry. The structures suggested by NMR were a trisaccharide and a novel tetrasaccharide-containing cellobiose of the structures glc (alpha 1 -> 4) glc (beta 1 -> 4) glc and glc(alpha 1 -> 4) glc (alpha 1 -> 4) glc (beta 1 -> 4) glc, respectively. The products were found to be resistant to hydrolysis by a-amylase. (C) 2010 Elsevier Ltd. All rights reserved.