(S)-1-phenylhexyl acetate | 1245821-69-5

• 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: (S)-1-phenylhexyl acetate
• 英文别名: [(1S)-1-phenylhexyl] acetate
• CAS: 1245821-69-5
• 化学式: C₁₄H₂₀O₂
• 分子量: 220.312
• InChiKey: CGHUKYHIHWBZBE-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  16
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 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：

  苯己酮 在 sodium tetrahydroborate 作用下， 以 甲醇 、 二氧化碳 为溶剂， 20.0 ℃ 、7.0 MPa 条件下， 反应 76.0h， 生成 (S)-1-phenylhexyl acetate
  参考文献：
  名称：

  Expanding substrate scope of lipase-catalyzed transesterification by the utilization of liquid carbon dioxide

  摘要：

  Secondary alcohols having bulky substituents on both sides of the chiral center are often poor substrates for most lipases. Here we reported that substrate scopes of two of the most used lipases, Candida antarctica lipase B and Burkholderia cepacia lipase, were found to be expanded toward more bulky secondary alcohols such as 1-phenyl-1-dodecanol and 2-methyl-1-phenyl-1-propanol by simply using them in liquid carbon dioxide as a solvent. The effects of solvents, reaction pressure, and pre-treatment of the enzyme with liquid CO2 on this acceleration phenomenon were also studied. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2015.11.052

文献信息

• Mutant Lipase-Catalyzed Kinetic Resolution of Bulky Phenyl Alkyl<i>sec</i>-Alcohols: A Thermodynamic Analysis of Enantioselectivity
  作者：Michaela Vallin、Per-Olof Syrén、Karl Hult

  DOI：10.1002/cbic.200900635

  日期：2010.2.15

  Open to persuasion: The rationally designed, single point mutated variant, Candida antarctica lipase B W104A, is a S‐selective catalyst for kinetic resolution of bulky phenyl alkyl alcohols. The catalyst's enantioselectivity differs within a homologous series of alcohols, depending on the different contributions from enthalpy and entropy.

  开放的说服力：合理设计的单点突变变体南极假丝酵母脂肪酶B W104A是一种S选择性催化剂，用于动力学分离大体积的苯基烷基醇。在同系列的醇中，催化剂的对映选择性不同，这取决于焓和熵的不同贡献。
• CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability
  作者：Xiu Xing、Jun-Qi Jia、Jing-Fan Zhang、Zi-Wen Zhou、Jun Li、Na Wang、Xiao-Qi Yu

  DOI：10.3390/molecules24030490

  日期：——

  immobilization of lipase and resolution of racemic 1-phenylethanol were investigated. Under optimal conditions, esters could be obtained with conversion of 50%, enantiomeric excess of product (eep) > 99%, enantiomeric excess of substrate (ees) > 99%, and enantiomeric ratio (E) > 1000. The magnetic CALB CLEAs were successfully used for enzymatic kinetic resolution of fifteen secondary alcohols. Compared with Novozym

  在这项研究中，开发并研究了南极假丝酵母脂肪酶B磁性交联酶聚集体的固定化策略。通过常规的共沉淀制备磁性颗粒。用3-氨基丙基三乙氧基硅烷（APTES）对磁性纳米粒子进行改性，以获得表面氨基官能化的磁性纳米粒子（APTES⁻Fe3 O 3）作为固定材料。戊二醛用作交联剂以使CALB与APTES⁻Fe₃O₃共价结合。研究了固定化脂肪酶和拆分外消旋1-苯基乙醇的最佳条件。在最佳条件下，可以以50％的转化率，产物的对映体过量（eep）> 99％，底物的对映体过量（ee）> 99％和对映体比率（E）> 1000获得酯。磁性CALB CLEAs已成功用于15种仲醇的酶动力学拆分。与Novozym 435相比，CALB CLEA磁性对大多数底物表现出更好的对映选择性。在48小时的反应周期中，将磁性CALB CLEA重复使用10次后，转化率仍大于49％。ee和eep都接近99％。此外，在-20℃下保存90天后，催化活性和对映选择性几乎没有降低。
• Ionic-Surfactant-Coated Burkholderia cepacia Lipase as a Highly Active and Enantioselective Catalyst for the Dynamic Kinetic Resolution of Secondary Alcohols
  作者：Hyunjin Kim、Yoon Kyung Choi、Jusuk Lee、Eungyeong Lee、Jaiwook Park、Mahn-Joo Kim

  DOI：10.1002/anie.201104141

  日期：2011.11.11

  With a coat for activity: A highly active enzyme was prepared by coating Burkholderia cepacia lipase with an ionic surfactant for use in dynamic kinetic resolution (DKR). Important features of this enzyme include: the fastest DKR of 1‐phenylethanol, the highly enantioselective DKR of a wide range of secondary alcohols (RCH(OH)Ar), and the switching of lipase enantioselectivity in DKR depending on the shape

  带有活性涂层：通过用动态动力学拆分（DKR）用离子表面活性剂包被洋葱伯克霍尔德氏菌脂肪酶制备高活性酶。该酶的重要特征包括：1-苯基乙醇的最快DKR，各种仲醇（RCH（OH）Ar）的高对映选择性DKR，以及取决于脂肪链形状的DKR中脂肪酶对映选择性的转换（R）。
• Redesign of enzyme for improving catalytic activity and enantioselectivity toward poor substrates: manipulation of the transition state
  作者：Tadashi Ema、Yasuko Nakano、Daiki Yoshida、Shusuke Kamata、Takashi Sakai

  DOI：10.1039/c2ob25614b

  日期：——

  altered the transition state. Substrate mapping analysis strongly suggested that the CH/π interaction partly enhanced the (R)-enantiomer reactivity, the estimated energy of the CH/π interaction being −0.4 kcal mol−1. The substrate scope of the I287F/I290A double mutant was broad. This biocatalyst was useful for the dynamic kinetic resolution of a variety of bulky secondary alcohols for which the wild-type

  对于大多数脂肪酶而言，在羟基的两侧均具有大的取代基的仲醇固有地是较差的底物。鉴于这种弱点，我们重新设计了洋葱伯克霍尔德氏菌脂肪酶，以创建具有改善的酶促特性的变体。对于野生型酶显示低转化率和低E值的不良底物，I287F / I290A双突变体显示出高转化率和E值（> 200）（5）。该变体的催化活性和对映体选择性的增强是由于两个突变的协同作用引起的：Phe287既有助于增强（R）-对映异构体反应性，又可以抑制（S）-对映体的反应性，而Ala290则为促进（R）-对映体的酰化创造了空间。动力学常数表明突变有效地改变了过渡状态。底物作图分析强烈表明，CH /π相互作用部分增强了（R）-对映异构体的反应性，CH /π相互作用的估计能量为-0.4 kcal mol -1。I287F / I290A双突变体的底物范围很广。这种生物催化剂可用于动态动力学拆分各种大体积的仲醇，而野生型酶几乎没有或没有活性。
• Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates
  作者：Tadashi Ema、Shusuke Kamata、Masahiro Takeda、Yasuko Nakano、Takashi Sakai

  DOI：10.1039/c001561j

  日期：——

  Catalytic activity and enantioselectivity of lipase toward poor substrates bearing bulky substituents on both sides have been dramatically improved by rational design; the E value for a poor substrate was increased from 5 (wild-type enzyme) to >200 (I287F/I290A double mutant) with an acceleration of the reaction rate.

  通过合理设计，脂肪酶对两侧具有大取代基的差质底物的催化活性和对映选择性得到了显著提高；差质底物的E值从5（野生型酶）提高到>200（I287F/I290A双突变体），反应速率也加快。