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Continuous‐Flow Reactor‐Based Enzymatic Synthesis of Phosphorylated Compounds on a Large Scale
Author(s) -
Babich Lara,
Hartog Aloysius F.,
van der Horst Michael A.,
Wever Ron
Publication year - 2012
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201200101
Subject(s) - dihydroxyacetone phosphate , chemistry , phosphate , immobilized enzyme , enzyme , pyrophosphate , chromatography , phosphatase , inosine , covalent bond , organic chemistry , biochemistry
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.