C12G8β | 1190987-70-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: C12G8β
• 英文别名: n-dodecyl (1,4)-β-maltooctaoside；dodecyl-β-D-maltooctaoside
• CAS: 1190987-70-2
• 化学式: C₆₀H₁₀₆O₄₁
• 分子量: 1483.48
• InChiKey: STXZXEAVJVWWSL-LIABQWHISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -13.51
• 重原子数：
  101.0
• 可旋转键数：
  34.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  653.43
• 氢给体数：
  25.0
• 氢受体数：
  41.0

反应信息

• 作为产物：
  描述：

  十二烷基-β-D-麦芽糖苷 、 α-环糊精 在 Bacillus macerans cyclodextrin glycosyltransferase 、 calcium chloride 作用下， 生成 C12G8β
  参考文献：
  名称：

  Immobilisation of CGTase for continuous production of long-carbohydrate-chain alkyl glycosides

  摘要：

  Bacillus macerans cyclodextrin glycosyltransferase (CGTase) (EC 2.4.1.19) was covalently immobilised on Eupergit C and used in a packed-bed reactor to investigate the continuous production of long-carbohydrate-chain alkyl glycosides from alpha-cyclodextrin (alpha-CD) and n-dodecyl-(1,4)-beta-maltopyranoside (C(12)G(2)beta). The effects of buffer ion strength and pH, and enzyme loading on the immobilisation yield and the enzyme activity were evaluated. Approximately 98% of the protein and 33% of the total activity were immobilised. At pH 5.15, the enzymatic half-life was 132 min at 60 degrees C and 18 min at 70 degrees C. The immobilised enzyme maintained 60% of its initial activity after 28 days storage at 4 degrees C. The degree of conversion was controlled by simple regulation of the flow rate through the reactor, making it possible to optimise the product distribution. It was possible to achieve a yield of the primary coupling product n-dodecyl-(1,4)-beta-maltooctaoside (C(12)G(8)beta) of about 50%, with a ratio between the primary and the secondary coupling product of about 10. Thermoanaerobacter sp. CGTase (Toruzyme 3.0 L) immobilised on Eupergit C had good operational stability at 60 and 70 degrees C thus showing the advantages of using more thermostable enzymes in biocatalysis. However, this enzyme was unsuitable for the production of C(12)G(8)beta due to extensive disproportionation reactions, giving a broad product range. (C) 2011 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2011.01.009

文献信息

• Enzymatic route to alkyl glycosides having oligomeric head groups
  作者：David Svensson、Stefan Ulvenlund、Patrick Adlercreutz

  DOI：10.1039/b904849a

  日期：——

  Cyclodextrin glycosyl transferase (CGTase) from Bacillus macerans was used to catalyse the coupling of α-cyclodextrin to alkyl β-glycosides. The acceptor substrate dodecyl β-maltoside was thus converted to dodecyl β-D-maltooctaoside. Further coupling steps and disproportionation reactions occurred, but by optimisation of the reaction time, a yield of 50% of the primary coupling product was obtained. The method worked well for a range of acceptors with different length of the carbohydrate part (1–3 glucose residues) and the hydrocarbon chain (10–14 carbon atoms). With respect to the principles of green chemistry, the method is superior to previously used methods involving protection/deprotection reactions.

  研究人员利用枯草芽孢杆菌（Bacillus macerans）的环糊精糖基转移酶（CGTase）催化α-环糊精与烷基β-糖苷的偶联反应。受体底物十二烷基 β-麦芽糖苷由此转化为十二烷基 β-D-麦芽糖苷。虽然还需要进一步的偶联步骤和歧化反应，但通过优化反应时间，一次偶联产物的收率达到了 50%。该方法适用于一系列具有不同长度碳水化合物部分（1-3 个葡萄糖残基）和碳氢链（10-14 个碳原子）的受体。就绿色化学原理而言，该方法优于以前使用的涉及保护/脱保护反应的方法。