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Chemoenzymatic Synthesis of Sialic Acid Derivatives Using Immobilized N-Acetylneuraminate Lyase in a Continuous Flow Reactor.

Authors
  • Bloemendal, Victor R L J1
  • Moons, Sam J1
  • Heming, Jurriaan J A1
  • Chayoua, Mohamed1
  • Niesink, Olaf1
  • van Hest, Jan C M2
  • Boltje, Thomas J1
  • Rutjes, Floris P J T1
  • 1 Institute for Molecules and Materials Radboud University Heyendaalseweg 135 6525 AJ Nijmegen, The Netherlands. , (Netherlands)
  • 2 Bio-organic chemistry Eindhoven University of Technology P.O. Box 513 (STO 3.31) 5600 MB Eindhoven, The Netherlands. , (Netherlands)
Type
Published Article
Journal
Advanced Synthesis & Catalysis
Publisher
Wiley
Publication Date
Jun 06, 2019
Volume
361
Issue
11
Pages
2443–2447
Identifiers
DOI: 10.1002/adsc.201900146
PMID: 31598119
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The synthesis of N-acetylneuraminic acid (Neu5Ac) derivatives is drawing more and more attention in glycobiology research because of the important role of sialic acids in e. g. cancer, bacterial, and healthy cells. Chemical preparation of these carbohydrates typically relies on multistep synthetic procedures leading to low overall yields. Herein we report a continuous flow process involving N-acetylneuraminate lyase (NAL) immobilized on Immobead 150P (Immobead-NAL) to prepare Neu5Ac derivatives. Batch experiments with Immobead-NAL showed equal activity as the native enzyme. Moreover, by using a fivefold excess of either N-acetyl-D-mannosamine (ManNAc) or pyruvate the conversion and isolated yield of Neu5Ac were significantly improved. To further increase the efficiency of the process, a flow setup was designed providing a chemoenzymatic entry into a series of N-functionalized Neu5Ac derivatives in conversions of 48-82%, and showing excellent stability over 1 week of continuous use. © 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.

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