z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom