Medium and reaction engineering for the establishment of a chemo-enzymatic dynamic kinetic resolution of rac-benzoin in batch and continuous mode

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Annika Petrenz
  • Pablo Domínguez De María
  • Anand Ramanathan
  • Ulf Hanefeld
  • Marion B. Ansorge-Schumacher
  • Selin Kara

Externe Organisationen

  • Technische Universität Dresden
  • University of Kansas (KU)
  • Delft University of Technology
  • Sustainable Momentum SL
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Details

OriginalspracheEnglisch
Seiten (von - bis)42-49
Seitenumfang8
FachzeitschriftJournal of Molecular Catalysis B: Enzymatic
Jahrgang114
Frühes Online-Datum27 Okt. 2014
PublikationsstatusVeröffentlicht - Apr. 2015
Extern publiziertJa

Abstract

The effect of the reaction parameters water activity and reaction solvent was investigated for the dynamic kinetic resolution (DKR) of rac-benzoin with immobilized Lipase TL as biocatalyst for transesterification and the heterogeneous chemo-catalyst Zr-TUD-1 (Si/Zr = 25) for in situ racemization. Overall dry reaction conditions led to the best results for both catalysts. The immobilized lipase in a more environmentally benign solvent like cyclopentyl methyl ether (CPME) exhibited a 1.6-fold higher activity and an up to 1.5-fold higher half-life time than in the standard solvents such as toluene and 2-methyltetrahydrofuran (2-MeTHF). Among a variety of deep eutectic solvents (DESs) choline chloride:isosorbide (ChCl:Iso) was found to be suitable for the reaction system. The activity was lower than in the aforementioned solvents, but the very low solubility of the product (S)-benzoin butyrate in ChCl:Iso compared to the investigated organic solvents possesses great potential with respect to downstream processing. Optimized reaction parameters (dry CPME) were applied for DKR in batch and continuous mode yielding comparable or slightly better results than in toluene or 2-MeTHF.

ASJC Scopus Sachgebiete

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Medium and reaction engineering for the establishment of a chemo-enzymatic dynamic kinetic resolution of rac-benzoin in batch and continuous mode. / Petrenz, Annika; María, Pablo Domínguez De; Ramanathan, Anand et al.
in: Journal of Molecular Catalysis B: Enzymatic, Jahrgang 114, 04.2015, S. 42-49.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Petrenz A, María PDD, Ramanathan A, Hanefeld U, Ansorge-Schumacher MB, Kara S. Medium and reaction engineering for the establishment of a chemo-enzymatic dynamic kinetic resolution of rac-benzoin in batch and continuous mode. Journal of Molecular Catalysis B: Enzymatic. 2015 Apr;114:42-49. Epub 2014 Okt 27. doi: 10.1016/j.molcatb.2014.10.011
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abstract = "The effect of the reaction parameters water activity and reaction solvent was investigated for the dynamic kinetic resolution (DKR) of rac-benzoin with immobilized Lipase TL as biocatalyst for transesterification and the heterogeneous chemo-catalyst Zr-TUD-1 (Si/Zr = 25) for in situ racemization. Overall dry reaction conditions led to the best results for both catalysts. The immobilized lipase in a more environmentally benign solvent like cyclopentyl methyl ether (CPME) exhibited a 1.6-fold higher activity and an up to 1.5-fold higher half-life time than in the standard solvents such as toluene and 2-methyltetrahydrofuran (2-MeTHF). Among a variety of deep eutectic solvents (DESs) choline chloride:isosorbide (ChCl:Iso) was found to be suitable for the reaction system. The activity was lower than in the aforementioned solvents, but the very low solubility of the product (S)-benzoin butyrate in ChCl:Iso compared to the investigated organic solvents possesses great potential with respect to downstream processing. Optimized reaction parameters (dry CPME) were applied for DKR in batch and continuous mode yielding comparable or slightly better results than in toluene or 2-MeTHF.",
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AU - María, Pablo Domínguez De

AU - Ramanathan, Anand

AU - Hanefeld, Ulf

AU - Ansorge-Schumacher, Marion B.

AU - Kara, Selin

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