N-(2-Cyanoethyl)hexanamide | 194427-29-7

• 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: N-(2-Cyanoethyl)hexanamide
• CAS: 194427-29-7
• 化学式: C₉H₁₆N₂O
• 分子量: 168.239
• InChiKey: VXHAYAPMAZMYSY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  12
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  52.9
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  3-氨基丙腈 、 己酸甲酯 在 Candida antarctica lipase 作用下， 以 异丙醚 为溶剂， 反应 48.0h， 以82.6%的产率得到N-(2-Cyanoethyl)hexanamide
  参考文献：
  名称：

  有机介质中N-月桂酰-β-丙氨酸同系物的酶促合成

  摘要：

  AbstractEnyzmatic amidation of the primary amines β‐alanine ethyl ester and 3‐aminopropionitrile with methyl laurate by means of immobilized lipase (Candida antarctica lipase, CAL) resulted in the formation in good yield of N‐lauroyl‐β‐alanine ethyl ester and 3‐(N‐lauroylamino)‐propionitrile, respectively. When 3‐amino‐propionitrile was used as substrate, diisopropyl ether was a suitable solvent. Changing the reaction temperature (12–80°C) did not affect the yields, and room temperature was a suitable temperature for this reaction. In the investigation of reaction conditions, the use of equimolar amounts (5 mmol) of substrate and ester, along with 0.5 g of CAL, in diisopropyl ether gave the best yield (99.3%) after 24 h of incubation at 24°C. The enzyme activity in the amidation reaction did not decrease even after six uses. With β‐alanine ethyl ester hydrochloride as substrate, diisopropyl ether was unsuited as a solvent owing to the low solubility of the substrate in this solvent.In this reaction, the best yield (82.0%) was attained by using dioxane as solvent. CAL achieved higher extents of amide synthesis with long‐chain than with short‐chain ester substrates. The enzyme accepted only nonbulky primary amines as substrates.

  DOI：

  10.1007/s11746-997-0231-9

文献信息

• Enzymatic syntheses of N-lauroyl-β-alanine homologs in organic media
  作者：Taeko Izumi、Yoshihiro Yagimuma、Masanori Haga

  DOI：10.1007/s11746-997-0231-9

  日期：1997.7

  AbstractEnyzmatic amidation of the primary amines β‐alanine ethyl ester and 3‐aminopropionitrile with methyl laurate by means of immobilized lipase (Candida antarctica lipase, CAL) resulted in the formation in good yield of N‐lauroyl‐β‐alanine ethyl ester and 3‐(N‐lauroylamino)‐propionitrile, respectively. When 3‐amino‐propionitrile was used as substrate, diisopropyl ether was a suitable solvent. Changing the reaction temperature (12–80°C) did not affect the yields, and room temperature was a suitable temperature for this reaction. In the investigation of reaction conditions, the use of equimolar amounts (5 mmol) of substrate and ester, along with 0.5 g of CAL, in diisopropyl ether gave the best yield (99.3%) after 24 h of incubation at 24°C. The enzyme activity in the amidation reaction did not decrease even after six uses. With β‐alanine ethyl ester hydrochloride as substrate, diisopropyl ether was unsuited as a solvent owing to the low solubility of the substrate in this solvent.In this reaction, the best yield (82.0%) was attained by using dioxane as solvent. CAL achieved higher extents of amide synthesis with long‐chain than with short‐chain ester substrates. The enzyme accepted only nonbulky primary amines as substrates.