(S)-2-(butanoyloxy)-2-phenylacetic acid

• 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)-2-(butanoyloxy)-2-phenylacetic acid
• 英文别名: (S)-2-butyroyloxy-2-phenylacetic acid；S-(-)-2-O-butyrylmandelic acid；(2S)-2-butanoyloxy-2-phenylacetic acid
• 化学式: C₁₂H₁₄O₄
• 分子量: 222.241
• InChiKey: GHUCRYGFTIDQAE-NSHDSACASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  16
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  63.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  (+/-)-2-(butanoyloxy)-2-phenylacetic acid 在 水 作用下， 以 aq. phosphate buffer 为溶剂， 反应 96.0h， 以55% ee的产率得到
  参考文献：
  名称：

  Purification and improvement of the functional properties of Rhizopus oryzae lipase using immobilization techniques

  摘要：

  The adsorption/immobilization of Rhizopus oryzae lipase (ROL) has permitted the development of several strategies to improve the properties of this industrial enzyme. The enzyme can be purified, immobilized, hyperactivated and stabilized, though its enantioselectivity could still be improved. A moderately hydrophobic support (e.g., phenyl-Toyopearl) allows the almost-quantitative immobilization of the enzyme via selective hydrophobic adsorption, while any contaminant proteins are not adsorbed. A further desorption of the adsorbed enzyme with surfactants (e.g., 0.5% sucrose laurate) allows the complete purification of the enzyme in only one step, with a 90% purification yield and an 8-fold purification factor. By using a more hydrophobic support, the ROL can be immobilized and hyperactivated. The enzyme is completely adsorbed on octyl-Sepharose and C18-Sepabeads. The pure enzyme (when adsorbed on these supports) becomes hyperactivated to approximately 250% of the activity of the soluble enzyme. In this study, two protocols for the covalent immobilization of ROL were developed: a one-point immobilization on CNBr-activated Sepharose and a multipoint covalent immobilization on highly activated glyoxyl-agarose supports. The multipoint attached enzyme decreased in activity to 50% of the activity of the soluble enzyme, but the derivatives were 300-fold more stable than the soluble enzyme. The hydrolysis of racemic 2-O-butyryl-2-phenylacetic acid was modulated by the different immobilized derivatives. In fact, the most active and selective preparation was demonstrated to be the C18-SB-ROL derivative (0.05 UI/mg and E = 22) when compared with the CNBr-ROL enzyme preparation (0.0073 UI/mg and E = 3.5). (C) 2014 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2014.09.012

文献信息

• Purification and improvement of the functional properties of Rhizopus oryzae lipase using immobilization techniques
  作者：N. Ghattas、M. Filice、F. Abidi、J.M. Guisan、A. Ben Salah

  DOI：10.1016/j.molcatb.2014.09.012

  日期：2014.12

  The adsorption/immobilization of Rhizopus oryzae lipase (ROL) has permitted the development of several strategies to improve the properties of this industrial enzyme. The enzyme can be purified, immobilized, hyperactivated and stabilized, though its enantioselectivity could still be improved. A moderately hydrophobic support (e.g., phenyl-Toyopearl) allows the almost-quantitative immobilization of the enzyme via selective hydrophobic adsorption, while any contaminant proteins are not adsorbed. A further desorption of the adsorbed enzyme with surfactants (e.g., 0.5% sucrose laurate) allows the complete purification of the enzyme in only one step, with a 90% purification yield and an 8-fold purification factor. By using a more hydrophobic support, the ROL can be immobilized and hyperactivated. The enzyme is completely adsorbed on octyl-Sepharose and C18-Sepabeads. The pure enzyme (when adsorbed on these supports) becomes hyperactivated to approximately 250% of the activity of the soluble enzyme. In this study, two protocols for the covalent immobilization of ROL were developed: a one-point immobilization on CNBr-activated Sepharose and a multipoint covalent immobilization on highly activated glyoxyl-agarose supports. The multipoint attached enzyme decreased in activity to 50% of the activity of the soluble enzyme, but the derivatives were 300-fold more stable than the soluble enzyme. The hydrolysis of racemic 2-O-butyryl-2-phenylacetic acid was modulated by the different immobilized derivatives. In fact, the most active and selective preparation was demonstrated to be the C18-SB-ROL derivative (0.05 UI/mg and E = 22) when compared with the CNBr-ROL enzyme preparation (0.0073 UI/mg and E = 3.5). (C) 2014 Elsevier B.V. All rights reserved.