TY - DATA T1 - Data underlying the research of Chemoenzymatic Synthesis of Sialic Acid Derivatives Using Immobilized N-Acetylneuraminate Lyase in a Continuous Flow Reactor PY - 2019/04/25 AU - Victor Bloemendal AU - S.J. (Sam) Moons AU - J.J.A. (Jurriaan) Hemming AU - M. (Mohamed) Chayoua AU - O. (Olaf) Niesink AU - Jan van Hest AU - T.J. (Thomas) Boltje AU - F.P.J.T. (Floris) Rutjes UR - 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 DO - 10.4121/uuid:74547c17-9760-4e07-b901-a6d9cd21d092 KW - Enzyme immobilization KW - Flow chemistry KW - N-acetylneuraminate lyase KW - N-acetylneuraminic acid KW - Sialic acids N2 - 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. ER -