Factors affecting the lipase catalyzed transesterification reactions of 3-hydroxy esters in organic solvents.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Uwe Bornscheuer
  • Andrea Herar
  • Lars Kreye
  • Volker Wendel
  • Andreas Capewell
  • Hartmut H. Meyer
  • Thomas Scheper
  • Fragiskos N. Kolisis

Externe Organisationen

  • Universität Nagoya
  • Westfälische Wilhelms-Universität Münster (WWU)
  • Nationale Technische Universität Athen (NTUA)
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Details

OriginalspracheEnglisch
Seiten (von - bis)1007-1016
Seitenumfang10
FachzeitschriftTetrahedron: Asymmetry
Jahrgang4
Ausgabenummer5
PublikationsstatusVeröffentlicht - 5 Mai 1993
Extern publiziertJa

Abstract

Chiral resolutions of racemic 3-hydroxy esters were performed in organic phases with lipases from Pseudomonas cepacia, Chromobacterium viscosum and Porcine pancreas. The reaction conditions have been optimized with 3-hydroxy octanoic acid methyl ester. Different organic solvents have been tested showing a tendentious correlation with the hydrophobicity of the solvents expressed as log P. The reaction time was shortened six fold by using irreversible acylating agents. We have found solvent type, lipase type and acylating agent acting as tools for changing the enantioselectivity. Lipase from Pseudomonas cepacia was lyophilized at different pH and the influence of the amount of water added was investigated, resulting in the highest activity at the pH optimum and a denaturation of the lipase above 1 % water (w/wlipase). The water activity was measured on-line with a humidity sensor. Water activities greater than 0.4 led to a decrease in enantioselectivity and reaction rate. In the optimized system the resolutions of other 3-hydroxy esters were tested. Aliphatic compounds reacted with lower enantioselectivity, only the substrates could be isolated in high enantiomeric purity. In contrast, aromatic 3-hydroxy esters were acylated by lipases with high stereoselectivity. A model of the active site of lipase from Pseudomonas sp. explained these experimental observations.

ASJC Scopus Sachgebiete

Zitieren

Factors affecting the lipase catalyzed transesterification reactions of 3-hydroxy esters in organic solvents. / Bornscheuer, Uwe; Herar, Andrea; Kreye, Lars et al.
in: Tetrahedron: Asymmetry, Jahrgang 4, Nr. 5, 05.05.1993, S. 1007-1016.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Bornscheuer U, Herar A, Kreye L, Wendel V, Capewell A, Meyer HH et al. Factors affecting the lipase catalyzed transesterification reactions of 3-hydroxy esters in organic solvents. Tetrahedron: Asymmetry. 1993 Mai 5;4(5):1007-1016. doi: 10.1016/S0957-4166(00)80145-7
Bornscheuer, Uwe ; Herar, Andrea ; Kreye, Lars et al. / Factors affecting the lipase catalyzed transesterification reactions of 3-hydroxy esters in organic solvents. in: Tetrahedron: Asymmetry. 1993 ; Jahrgang 4, Nr. 5. S. 1007-1016.
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abstract = "Chiral resolutions of racemic 3-hydroxy esters were performed in organic phases with lipases from Pseudomonas cepacia, Chromobacterium viscosum and Porcine pancreas. The reaction conditions have been optimized with 3-hydroxy octanoic acid methyl ester. Different organic solvents have been tested showing a tendentious correlation with the hydrophobicity of the solvents expressed as log P. The reaction time was shortened six fold by using irreversible acylating agents. We have found solvent type, lipase type and acylating agent acting as tools for changing the enantioselectivity. Lipase from Pseudomonas cepacia was lyophilized at different pH and the influence of the amount of water added was investigated, resulting in the highest activity at the pH optimum and a denaturation of the lipase above 1 % water (w/wlipase). The water activity was measured on-line with a humidity sensor. Water activities greater than 0.4 led to a decrease in enantioselectivity and reaction rate. In the optimized system the resolutions of other 3-hydroxy esters were tested. Aliphatic compounds reacted with lower enantioselectivity, only the substrates could be isolated in high enantiomeric purity. In contrast, aromatic 3-hydroxy esters were acylated by lipases with high stereoselectivity. A model of the active site of lipase from Pseudomonas sp. explained these experimental observations.",
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AU - Bornscheuer, Uwe

AU - Herar, Andrea

AU - Kreye, Lars

AU - Wendel, Volker

AU - Capewell, Andreas

AU - Meyer, Hartmut H.

AU - Scheper, Thomas

AU - Kolisis, Fragiskos N.

PY - 1993/5/5

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N2 - Chiral resolutions of racemic 3-hydroxy esters were performed in organic phases with lipases from Pseudomonas cepacia, Chromobacterium viscosum and Porcine pancreas. The reaction conditions have been optimized with 3-hydroxy octanoic acid methyl ester. Different organic solvents have been tested showing a tendentious correlation with the hydrophobicity of the solvents expressed as log P. The reaction time was shortened six fold by using irreversible acylating agents. We have found solvent type, lipase type and acylating agent acting as tools for changing the enantioselectivity. Lipase from Pseudomonas cepacia was lyophilized at different pH and the influence of the amount of water added was investigated, resulting in the highest activity at the pH optimum and a denaturation of the lipase above 1 % water (w/wlipase). The water activity was measured on-line with a humidity sensor. Water activities greater than 0.4 led to a decrease in enantioselectivity and reaction rate. In the optimized system the resolutions of other 3-hydroxy esters were tested. Aliphatic compounds reacted with lower enantioselectivity, only the substrates could be isolated in high enantiomeric purity. In contrast, aromatic 3-hydroxy esters were acylated by lipases with high stereoselectivity. A model of the active site of lipase from Pseudomonas sp. explained these experimental observations.

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