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  Enzyme-assisted physicochemical enantioseparation processes - Part III: Overcoming yield limitations by dynamic kinetic resolution of asparagine via preferential crystallization and enzymatic racemization

Würges, K., Petrusevska-Seebach, K., Elsner, M. P., & Lütz, S. (2009). Enzyme-assisted physicochemical enantioseparation processes - Part III: Overcoming yield limitations by dynamic kinetic resolution of asparagine via preferential crystallization and enzymatic racemization. Biotechnology and Bioengineering, 104(6), 1235-1239. doi:10.1002/bit.22498.

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Datensatz-Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-93CF-D Versions-Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-B58A-8
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 Urheber:
Würges, K.1, Autor
Petrusevska-Seebach, K.2, Autor              
Elsner, M. P.2, Autor              
Lütz, S.1, Autor
Affiliations:
1Research Centre Juelich, Institute of Biotechnology 2, Juelich, Germany, ou_persistent22              
2Physical and Chemical Foundations of Process Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738150              

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Schlagwörter: amino acid racemase; dynamic kinetic resolution; preferential crystallization; integrated enantioseparation process; asparagine; in situ racemization; production of L-amino acids
 Zusammenfassung: The application of enantioseparation methods alone can only yield up to 50% of the desired chiral product. Thus enantioseparation becomes more attractive when accompanied by the racemization of the counter-enantiomer. Here we present first results of dynamic kinetic resolution of L-asparagine (L-Asn) via preferential crystallization and enzymatic racemization from a racemic, supersaturated solution on a 20 mL scale. An enzyme lyophilisate (WT amino acid racemase from P. putida KT2440 (E.C. 5.1.1.10), overexpressed in E. coli BL21(DE3)) was used for in situ racemization (enzyme concentrations varying from 0 to 1 mg/mL). When preferential crystallization was applied without any enzyme, a total of 31 mg of L-Asn monohydrate could be crystallized, before crystal formation of d-Asn started. Crystallization experiments accompanied by enzymatic racemization led to a significant increase of crystallized L-Asn (198 mg L-Asn monohydrate; >92%ee) giving the first experimental proof for this new process concept of dynamic kinetic resolution via preferential crystallization and enzymatic racemization. Measurements of the racemase activity before and after the crystallization process showed no significant differences, which would allow for enzyme recovery and recycling.Copyright © 2009 John Wiley & Sons, Inc. All Rights Reserved. [accessed November 19, 2009]

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Sprache(n): eng - Englisch
 Datum: 2009
 Publikationsstatus: Im Druck publiziert
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 438889
DOI: 10.1002/bit.22498
 Art des Abschluß: -

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Titel: Biotechnology and Bioengineering
  Andere : Biotechnol. Bioeng.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: New York : Wiley [etc.]
Seiten: - Band / Heft: 104 (6) Artikelnummer: - Start- / Endseite: 1235 - 1239 Identifikator: ISSN: 0006-3592
CoNE: /journals/resource/111088195273104