n-propyl 3-hydroxyoctanoate | 929899-58-1

• 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-propyl 3-hydroxyoctanoate
• 英文别名: n-Propyl-3-hydroxyoctanoate；propyl 3-hydroxyoctanoate
• CAS: 929899-58-1
• 化学式: C₁₁H₂₂O₃
• 分子量: 202.294
• InChiKey: FYMJACPXJBFCKY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  14
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.91
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  丙醇 、 3-羟基辛酸乙酯 在 Novozyme 435 作用下， 反应 48.0h， 生成 n-propyl 3-hydroxyoctanoate
  参考文献：
  名称：

  Poly(3-hydroxyoctanoate) depolymerase from Pseudomonas fluorescens GK13: Catalysis of ester-forming reactions in non-aqueous media

  摘要：

  Several industrial processes based on lipase catalysis have been established. However, since there are still a vast number of catalytic processes that lack a suitable enzyme, the discovery of new biocatalysts is required to fulfil this purpose. The potential of using the medium-chain-length (mcl)-PHA depolymerase from Pseudomonas fluorescens GK13 in anhydrous media to catalyze ester-forming reactions has been investigated and compared with that of Novozyme 435. The mcl-PHA depolymerase catalyzes the ring-opening polymerization of racemic beta-butyrolactone (beta-BL). L- and D-lactide (LLA, DLA) with high yield resulting in low molecular weight polymers. On the other hand, epsilon-caprolactone and pentade-calactone, which show high polymerizability using Novozyme 435 as catalyst, were not polymerized by mcl-PHA depolymerase. Besides, the activity of mcl-PHA depolymerase toward transesterification and esterification of ethyl-3-hydroxyoctanoate, lauric acid, (R,S)-beta-BL, LLA and DLA has been studied. (C) 2012 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2012.01.011

文献信息

• Poly(3-hydroxyoctanoate) depolymerase from Pseudomonas fluorescens GK13: Catalysis of ester-forming reactions in non-aqueous media
  作者：Marta Santos、Joana Gangoiti、María J. Llama、Juan L. Serra、Helmut Keul、Martin Möller

  DOI：10.1016/j.molcatb.2012.01.011

  日期：2012.5

  Several industrial processes based on lipase catalysis have been established. However, since there are still a vast number of catalytic processes that lack a suitable enzyme, the discovery of new biocatalysts is required to fulfil this purpose. The potential of using the medium-chain-length (mcl)-PHA depolymerase from Pseudomonas fluorescens GK13 in anhydrous media to catalyze ester-forming reactions has been investigated and compared with that of Novozyme 435. The mcl-PHA depolymerase catalyzes the ring-opening polymerization of racemic beta-butyrolactone (beta-BL). L- and D-lactide (LLA, DLA) with high yield resulting in low molecular weight polymers. On the other hand, epsilon-caprolactone and pentade-calactone, which show high polymerizability using Novozyme 435 as catalyst, were not polymerized by mcl-PHA depolymerase. Besides, the activity of mcl-PHA depolymerase toward transesterification and esterification of ethyl-3-hydroxyoctanoate, lauric acid, (R,S)-beta-BL, LLA and DLA has been studied. (C) 2012 Elsevier B.V. All rights reserved.