(2,2-dimethyl-1,3-dioxolane-4-yl)methyl sorbate | 63303-83-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (2,2-dimethyl-1,3-dioxolane-4-yl)methyl sorbate
• 英文别名: 1,2-Isopropyliden-3-sorboylglycerin；(2,2-dimethyl-1,3-dioxolan-4-yl)methyl (2E,4E)-hexa-2,4-dienoate
• CAS: 63303-83-3
• 化学式: C₁₂H₁₈O₄
• 分子量: 226.273
• InChiKey: XXHNIAXNKHLFSR-YTXTXJHMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  44.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  丙酮缩甘油 、 alkaline earth salt of/the/ methylsulfuric acid 在 吡啶 作用下， 反应 24.0h， 生成 (2,2-dimethyl-1,3-dioxolane-4-yl)methyl sorbate
  参考文献：
  名称：

  Lipase-mediated desymmetrization of glycerol with aromatic and aliphatic anhydrides

  摘要：

  Chirazyme L-2 (Candida antarctica) catalyzed esterification of glycerol with aromatic and aliphatic anhydrides in 1,4-dioxane is described. All the aromatic monoacylglycerols (MAGs) were produced as (R)-enantiomers, while aliphatic MAGs were obtained either as racemic mixtures or the (S)-enantiomers. The influence of substituted aromatic rings, chain length, and presence of a conjugated double bond in the acyl donor moiety on the enantiotopic selectivity as well as the efficiency of the enzyme was studied. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2004.09.033

文献信息

• Lipase-mediated desymmetrization of glycerol with aromatic and aliphatic anhydrides
  作者：Daniela I. Batovska、Shuichirou Tsubota、Yasuo Kato、Yasuhisa Asano、Makoto Ubukata

  DOI：10.1016/j.tetasy.2004.09.033

  日期：2004.11

  Chirazyme L-2 (Candida antarctica) catalyzed esterification of glycerol with aromatic and aliphatic anhydrides in 1,4-dioxane is described. All the aromatic monoacylglycerols (MAGs) were produced as (R)-enantiomers, while aliphatic MAGs were obtained either as racemic mixtures or the (S)-enantiomers. The influence of substituted aromatic rings, chain length, and presence of a conjugated double bond in the acyl donor moiety on the enantiotopic selectivity as well as the efficiency of the enzyme was studied. (C) 2004 Elsevier Ltd. All rights reserved.