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Continuous-Flow Reactor-Based Enzymatic Synthesis of Phosphorylated Compounds on a Large Scale

Acid phosphatase, an enzyme that is able to catalyze the transfer of a phosphate group from cheap pyrophosphate to alcoholic substrates, was covalently immobilized on polymethacrylate beads with an epoxy linker (Immobeads‐150 or Sepabeads EC‐EP). After immobilization 70 % of the activity was retaine...

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Bibliographic Details
Published in:Chemistry : a European journal 2012-05, Vol.18 (21), p.6604-6609
Main Authors: Babich, Lara, Hartog, Aloysius F., van der Horst, Michael A., Wever, Ron
Format: Article
Language:English
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Summary:Acid phosphatase, an enzyme that is able to catalyze the transfer of a phosphate group from cheap pyrophosphate to alcoholic substrates, was covalently immobilized on polymethacrylate beads with an epoxy linker (Immobeads‐150 or Sepabeads EC‐EP). After immobilization 70 % of the activity was retained and the immobilized enzyme was stable for many months. With the immobilized enzyme we were able to produce and prepare D‐glucose‐6‐phosphate, N‐acetyl‐D‐glucosamine‐6‐phosphate, allyl phosphate, dihydroxyacetone phosphate, glycerol‐1‐phosphate, and inosine‐5′‐monophosphate from the corresponding primary alcohol on gram scale using either a fed‐batch reactor or a continuous‐flow packed‐bed reactor. Phosphorylation made easy: Acid phosphatase was covalently immobilized on polymethacrylate beads with an epoxy linker (see scheme). The beads were used in a fed batch and in a small continuous‐flow packed‐bed reactor to prepare D‐glucose‐6‐phosphate, N‐acetyl‐D‐glucosamine‐6‐phosphate, allyl phosphate, dihydroxyacetone phosphate, glycerol‐1‐phosphate, and inosine‐5′‐monophosphate on a gram scale.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.201200101