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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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 Creators:
Würges, K.1, Author
Petrusevska-Seebach, K.2, Author           
Elsner, M. P.2, Author           
Lütz, S.1, Author
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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Free keywords: amino acid racemase; dynamic kinetic resolution; preferential crystallization; integrated enantioseparation process; asparagine; in situ racemization; production of L-amino acids
 Abstract: 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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Language(s): eng - English
 Dates: 2009
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 438889
DOI: 10.1002/bit.22498
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Title: Biotechnology and Bioengineering
  Other : Biotechnol. Bioeng.
Source Genre: Journal
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Publ. Info: New York : Wiley [etc.]
Pages: - Volume / Issue: 104 (6) Sequence Number: - Start / End Page: 1235 - 1239 Identifier: ISSN: 0006-3592
CoNE: https://pure.mpg.de/cone/journals/resource/111088195273104