%0 Generic
%A Bloemendal, Victor
%A Moons, S.J. (Sam)
%A Hemming, J.J.A. (Jurriaan)
%A Chayoua, M. (Mohamed)
%A Niesink, O. (Olaf)
%A van Hest, Jan
%A Boltje, T.J. (Thomas)
%A Rutjes, F.P.J.T. (Floris)
%D 2019
%T Data underlying the research of Chemoenzymatic Synthesis of Sialic Acid Derivatives Using Immobilized N-Acetylneuraminate Lyase in a Continuous Flow Reactor
%U https://data.4tu.nl/articles/dataset/Data_underlying_the_research_of_Chemoenzymatic_Synthesis_of_Sialic_Acid_Derivatives_Using_Immobilized_N-Acetylneuraminate_Lyase_in_a_Continuous_Flow_Reactor/12704774/1
%R 10.4121/uuid:74547c17-9760-4e07-b901-a6d9cd21d092
%K Enzyme immobilization
%K Flow chemistry
%K N-acetylneuraminate lyase
%K N-acetylneuraminic acid
%K Sialic acids
%X NMR research data related to a continuous flow process involving N‐acetylneuraminate lyase (NAL) immobilized on Immobead 150P to prepare Neu5Ac derivatives. Batch experiments with Immobead‐NAL showed equal activity as the native enzyme. 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.
%I 4TU.Centre for Research Data