1-phenylethyl caprylate

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 1-phenylethyl caprylate
• 英文别名: [(1S)-1-phenylethyl] octanoate
• 化学式: C₁₆H₂₄O₂
• 分子量: 248.365
• InChiKey: KEKSMFRTVJMXLK-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5
• 重原子数：
  18
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  苏合香醇 、 (4-氯苯基)辛酸酯 在 Novozyme 435 lipase 作用下， 以 甲苯 为溶剂， 反应 6.0h， 以99%的产率得到1-phenylethyl caprylate
  参考文献：
  名称：

  Dynamic kinetic resolution of secondary aromatic alcohols with new efficient acyl donors

  摘要：

  A new and efficient dynamic kinetic resolution (DKR) process of secondary aromatic alcohols by using long carbon-chain esters as acyl donors has been developed. During the process, the transesterification catalyzed by CD8604 was found to be the main reason for the decrease in enantiomeric excess (ee). Using complex acyl donors, such as 4-chlorophenyl valerate, we could effectively inhibit the resin-catalyzed transesterification, and an excellent ee value (>99%) at high yield (>99%) was achieved. The mechanism for the inhibition of resin-catalyzed transesterification is believed to be the formation of micro-micelles in the pores of CD8604. It is noteworthy that the system can be reused more than 20 times without a loss of yield or ee value. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2011.06.034

文献信息

• (S)-Selective Kinetic Resolution and Chemoenzymatic Dynamic Kinetic Resolution of Secondary Alcohols
  作者：Linnéa Borén、Belén Martín-Matute、Yongmei Xu、Armando Córdova、Jan-E. Bäckvall

  DOI：10.1002/chem.200500758

  日期：2006.1

  (S)-Selective kinetic resolution was achieved through the use of a commercially available protease, which was activated with a combination of two different surfactants. The kinetic resolution (KR) process was optimized with respect to activation of the protease and to the acyl donor. The KR proved to be compatible with a range of functionalized sec-alcohols, giving good to high enantiomeric ratio values

  通过使用可商购的蛋白酶实现（S）-选择性动力学拆分，该蛋白酶被两种不同表面活性剂的组合激活。关于蛋白酶和酰基供体的活化，优化了动力学拆分（KR）过程。事实证明，KR与多种官能化仲醇兼容，对映体比率值高至高（高达> 200）。将酶促拆分与钌催化的消旋作用结合使用，可得到仲醇的（S）选择性动态动力学拆分（DKR）。DKR工艺在非常温和的反应条件下工作，以高收率和出色的对映选择性提供相应的酯。
• Hult, Karl; Norin, Torbjoern, Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 1993, vol. 32, # 1, p. 123 - 126
  作者：Hult, Karl、Norin, Torbjoern

  DOI：——

  日期：——
• Microwave-Promoted Lipase-Catalyzed Reactions. Resolution of (±)-1-Phenylethanol
  作者：José-Ramon Carrillo-Munoz、Denis Bouvet、Eryka Guibé-Jampel、André Loupy、Alain Petit

  DOI：10.1021/jo960309u

  日期：1996.1.1

  Microwave irradiation increased enzymatic affinity and selectivity of supported lipases in esterification and transesterification reactions carried out in dry media and at temperature near 100 degrees C.
• Esterase screening using whole cells of Brazilian soil microorganisms
  作者：Simone M. Mantovani、Luciana G. de Oliveira、Anita J. Marsaioli

  DOI：10.1590/s0103-50532010000800011

  日期：——

  A miniaturized enzymatic assay using fluorescent probes to reveal esterase producing microorganisms was optimized and applied to screen 64 soil bacterial strains. The best results were validated using traditional non-fluorogenic assays with acetyl and propanoyl phenylethanol to confirm the miniaturized results. The most active microorganisms belong to the genus Bacillus showing esterase activity and good enantiomeric ratios for the resolution of phenylethanol derivatives (E > 30). Part of the microorganisms are kept in our laboratory in glycerol or freeze-dried and the best microorganisms will be deposited in the CBMAI/CPQBA/Unicamp culture collection.
• Immobilization of lipase on aminopropyl-grafted mesoporous silica nanotubes for the resolution of (R, S)-1-phenylethanol
  作者：Wei Bai、Yun-Jie Yang、Xia Tao、Jian-Feng Chen、Tian-Wei Tan

  DOI：10.1016/j.molcatb.2011.11.005

  日期：2012.4

  Mesoporous silica nanotubes and aminopropyl-grafted mesoporous silica nanotubes were prepared as supports to immobilize lipase from Candida sp. 99-125(CILip) by physical adsorption. The immobilization conditions were investigated. Moreover, immobilized lipases on both kinds of supports were employed to catalyze olive oil hydrolization and resolution of 1-phenylethanol by esterification. The results showed that the hydrolization activity of the lipase immobilized on aminopropyl-grafted mesoporous silica nanotubes was almost twice of that on mesoporous silica nanotubes. In addition, the resolution of 1-phenylethanol catalyzed by the former catalyst also increased 22%. Circular dichroism spectra revealed a reduction of alpha-helix and an increase of beta-sheet when lipase was adsorbed on aminopropyl-grafted mesoporous silica nanotubes, which suggested that parts of alpha-helix were extended and reformed to be beta-sheet. (C) 2011 Elsevier B.V. All rights reserved.