[(1R)-1-phenylethyl] hexadecanoate | 174462-77-2

• 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: [(1R)-1-phenylethyl] hexadecanoate
• CAS: 174462-77-2
• 化学式: C₂₄H₄₀O₂
• 分子量: 360.58
• InChiKey: JAHQQDQKBBIBAF-JOCHJYFZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.3
• 重原子数：
  26
• 可旋转键数：
  17
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 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：

  棕榈酸甲酯 、 苏合香醇 在 lipase LipK₁₀₇ from Proteus sp. E₁₃₀L and K₁₃₁I mutant 、 水 作用下， 以 异辛烷 为溶剂， 反应 24.0h， 生成 (S)-(-)-1-苯乙醇 、 [(1R)-1-phenylethyl] hexadecanoate
  参考文献：
  名称：

  Improving the catalytic activity of lipase LipK107 from Proteus sp. by site-directed mutagenesis in the lid domain based on computer simulation

  摘要：

  The capacity of lipase LipK107 from Proteus sp. catalyzing the kinetic resolution of racemates was investigated. The resolution of racemic 1-phenylethanol in organic medium was selected as model reaction. The conversion was dramatically dependent on the water content and the LipK107 showed high activity in a wide range of water content without appreciable loss of enzyme enantiodiscrimination. Besides, the chain length of acyl donor also had a significant effect on the conversion, and the highest enantioselectivity was achieved when methyl palmitate was used. Based on the analysis of computer model structure of LipK107, different mutations were introduced into the lid region. Each derivative of LipK107 was expressed, purified, and assessed of the activity. According to the prediction, using mutants El 30L + K131I and T138V as catalyst, respectively, the conversions of 1-phenylethanol improved greatly with a slight increase of enantiodiscrimination. In addition, the effects of hydrophobicity and electrostatic of the lid on lipase activity were determined. This work indicated that the modification of the lid might considerably enhance the activity and improve the yield of catalytic reactions, which could apply to other lipases. The computer simulations would make the process of identifying amino acids for substitution efficiently. (C) 2010 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2010.12.001

文献信息

• Optical resolution for producing optically active alcohol
  申请人：The Nisshin Oil Mills, Ltd.

  公开号：EP0709465A2

  公开（公告）日：1996-05-01

  A process for producing an optically active alcohol comprising carrying out interesterification between a racemic alcohol and an ester selected from the group consisting of (a) a diester between a lower monohydric alcohol and a saturated dicarboxylic acid having 14 or more carbon atoms, (b) a triglyceride of a saturated fatty acid having 16 or more carbon atoms, and (c) a monoester between a lower monohydric alcohol and a saturated fatty acid having 18 or more carbon atoms in the presence of lipase, preferably heat-resistant lipase, and in the presence or absence of a solvent, preferably in the absence of a solvent, under a substantially water-free condition, separating an optically active alcohol rich in either one of R- and S-forms from the reaction mixture, and adding an optically inactive non-racemic alcohol to the residue of the previous step to carry out interesterification under the same conditions as in the previous reaction to separate the other enantiomer. According to the present invention a racemic alcohol can easily be resolved into each enantiomer with high purity in good yield.

  一种生产光学活性醇的工艺，包括在脂肪酶存在下，在外消旋醇和选自以下组别的酯 之间进行酯化反应：(a)低级一元醇与具有 14 个或更多碳原子的饱和二羧酸之间的二酯；(b)具有 16 个或更多碳原子的饱和脂肪酸的甘油三酯；(c)低级一元醇与具有 18 个或更多碳原子的饱和脂肪酸之间的单酯、在有或无溶剂（最好是无溶剂）的条件下，在基本上无水的条件下，从反应混合物中分离出富含 R 型和 S 型中任一型的光学活性醇，并将光学不活泼的非外消旋醇加入到上一步的残留物中，在与上一步反应相同的条件下进行酯交换反应，以分离出另一种对映体。 根据本发明，外消旋醇可以很容易地以高纯度和高产率分离成每种对映体。
• US5696299A
  申请人：——

  公开号：US5696299A

  公开（公告）日：1997-12-09
• Improving the catalytic activity of lipase LipK107 from Proteus sp. by site-directed mutagenesis in the lid domain based on computer simulation
  作者：Bei Gao、Tao Xu、Jinping Lin、Lujia Zhang、Erzheng Su、Zhengbing Jiang、Dongzhi Wei

  DOI：10.1016/j.molcatb.2010.12.001

  日期：2011.3

  The capacity of lipase LipK107 from Proteus sp. catalyzing the kinetic resolution of racemates was investigated. The resolution of racemic 1-phenylethanol in organic medium was selected as model reaction. The conversion was dramatically dependent on the water content and the LipK107 showed high activity in a wide range of water content without appreciable loss of enzyme enantiodiscrimination. Besides, the chain length of acyl donor also had a significant effect on the conversion, and the highest enantioselectivity was achieved when methyl palmitate was used. Based on the analysis of computer model structure of LipK107, different mutations were introduced into the lid region. Each derivative of LipK107 was expressed, purified, and assessed of the activity. According to the prediction, using mutants El 30L + K131I and T138V as catalyst, respectively, the conversions of 1-phenylethanol improved greatly with a slight increase of enantiodiscrimination. In addition, the effects of hydrophobicity and electrostatic of the lid on lipase activity were determined. This work indicated that the modification of the lid might considerably enhance the activity and improve the yield of catalytic reactions, which could apply to other lipases. The computer simulations would make the process of identifying amino acids for substitution efficiently. (C) 2010 Elsevier B.V. All rights reserved.