(R)-1-Phenethyl valerate | 138457-63-3

• 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: (R)-1-Phenethyl valerate
• 英文别名: (R)-1-phenylethyl valerate；(R)-1-phenylethyl pentanoate；[(1R)-1-phenylethyl] pentanoate
• CAS: 138457-63-3
• 化学式: C₁₃H₁₈O₂
• 分子量: 206.285
• InChiKey: PTBSIZMEMKOIHX-LLVKDONJSA-N

物化性质

• 沸点：
  267.4±9.0 °C(Predicted)
• 密度：
  0.986±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  15
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 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：

  (S)-(-)-1-苯乙醇 在 Novozym 435 、 sulphate-doped anatase 、 氢化铝 作用下， 以 甲苯 为溶剂， 反应 16.0h， 生成 (R)-1-Phenethyl valerate
  参考文献：
  名称：

  使用低成本固体超强酸作为外消旋催化剂的仲芳族醇的高效动态动力学拆分

  摘要：

  利用自制的固体超强酸TiO2 / SO42-作为外消旋催化剂，开发了一种新型高效的仲芳族醇动力学动力学拆分方法（DKR）。低成本且易于生产的TiO2 / SO42-具有出色的消旋活性。当与脂肪酶Novozym 435偶联时，观察到良好的生物相容性，并以高收率获得了光学纯的芳族乙酸酯（> 99％）。值得注意的是，该系统可重复使用10次以上，而收率损失很小或产品的对映体过量（ee）值降低。

  DOI：

  10.1016/j.tetlet.2013.07.016

文献信息

• New air-stable iron catalyst for efficient dynamic kinetic resolution of secondary benzylic and aliphatic alcohols
  作者：Qiong Yang、Na Zhang、Mingke Liu、Shaolin Zhou

  DOI：10.1016/j.tetlet.2017.05.038

  日期：2017.6

  catalyst system for the dynamic kinetic resolution of secondary alcohols by combining the enzymatic resolution with an iron-catalyzed racemization. A new air-stable tricarbonyl (cyclopentadienone)iron complex is identified as the active racemization catalyst for this transformation without any additive. Various substrates including benzylic, heteroaromatic, aliphatic alcohols can be used and afford the

  我们在此报道了通过将酶促拆分与铁催化的外消旋相结合来实现仲醇的动态动力学拆分的催化剂体系。一种新型的空气稳定的三羰基（环戊二烯酮）铁络合物被确定为该外消旋的活性外消旋催化剂，无任何添加剂。可以使用各种底物，包括苄基，杂芳族，脂族醇，并以良好的收率和优异的对映选择性提供相应的酯。
• Utility of Acyloxypyridines and Acylazoles for the Lipasecatalyzed Enantioselective Acylation of 1-Phenylethanol
  作者：Takashi Keumi、Yasumasa Hiraoka、Takashi Ban、Ichiro Takahashi、Hidehiko Kitajima

  DOI：10.1246/cl.1991.1989

  日期：1991.11

  3-Acyloxypyridines and 4-acetyl-1,2,4-triazole were found to react enantioselectively with (RS)-1-phenylethanol to give (R)-1-phenethyl carboxylates in high purity, catalyzed by lipase P (from Pseudomonas fluorescens).

  研究发现，3-乙酰氧基吡啶和4-乙酰基-1,2,4-三唑在脂酶P（来自荧光假单胞菌）的催化下，能以立体选择性方式与（RS）-1-苯乙醇反应，生成高纯度的（R）-1-苯乙基羧酸酯。
• Highly efficient dynamic kinetic resolution of secondary aromatic alcohols at low temperature using a low-cost sulfonated sepiolite as racemization catalyst
  作者：Jian-Ping Wu、Xiao Meng、Liang Wang、Gang Xu、Li-Rong Yang

  DOI：10.1016/j.tetlet.2014.07.102

  日期：2014.9

  A highly efficient dynamic kinetic resolution system for secondary aromatic alcohol using low-cost sulfonated sepiolite as a racemization catalyst has been developed. The system operates at 25 °C, achieves good eep (>99%) and substrate conversion ratio (>99%), is applicable to a variety of substrates and can be reused more than 10 times.

  已开发出一种使用低成本磺化海泡石作为外消旋催化剂的仲芳族醇的高效动态动力学拆分系统。该系统在25°C下运行，可实现良好的ee p（> 99％）和基板转换率（> 99％），适用于各种基板，可重复使用10次以上。
• (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。
• Easy and Simple SiO2 Immobilization of Lipozyme CaLB-L: Its Use as a Catalyst in Acylation Reactions and Comparison with Other Lipases
  作者：Mateus Mittersteiner、Tayani Machado、Paulo Cesar de Jesus、Patrícia Brondani、Dilamara Scharf、Renato Wendhausen Jr.

  DOI：10.21577/0103-5053.20160277

  日期：——

  In this study, lipase from Candida antarctica B (Lipozyme CaLB-L) was successfully immobilized on SiO2 through adsorption and used to obtain (R)-(+)-esters derived from (R, S)-1-phenylethanol. The new immobilized enzyme was compared with commercially immobilized lipases (Novozyme 435, Lipozyme 435 and Pseudomonas cepacia (PSC-II and PSD-I)). Lipozyme CaLB-L adsorbed onto SiO2 was found to be a good catalyst and, under optimal conditions, esters could be obtained with conversion 44%, enantiomeric excess of product (ee(p)) > 99%, enantiomeric excess of substract (ee(s)) 77% and enantiomeric ratio (E) > 200. The lipase maintained enantioselectivity under adverse conditions, such as in organic solvents, with an excess of substrate and at different temperatures. The immobilized lipase could be reused five times with no significant loss of the activity.