TY - DATA
T1 - Data underlying the article: Chemoenzymatic Synthesis of Sialic Acid Derivatives Using Immobilized N-Acetylneuraminate Lyase in a Continuous Flow Reactor
PY - 2019/10/14
AU - Victor Bloemendal
AU - S.J. (Sam) Moons
AU - J.J.A. (Jurriaan) Heming
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_article_Chemoenzymatic_Synthesis_of_Sialic_Acid_Derivatives_Using_Immobilized_N-Acetylneuraminate_Lyase_in_a_Continuous_Flow_Reactor/12693590/1
DO - 10.4121/uuid:4c72b586-a07a-484e-9cb4-5ea4b3082962
KW - N-acetylneuraminate lyase
KW - N-acetylneuraminic acid
KW - enzyme immobilization
KW - flow chemistry
N2 - The synthesis of N-acetylneuraminic acid (Neu5Ac) derivatives is drawing more and more attention in glycobiology research because of the important role of sialic acids in e. g. cancer, bacterial, and healthy cells. Chemical preparation of these carbohydrates typically relies on multistep synthetic procedures leading to low overall yields. Herein we report a continuous flow process involving N-acetylneuraminate lyase (NAL) immobilized on Immobead 150P (Immobead-NAL) to prepare Neu5Ac derivatives. Batch experiments with Immobead-NAL showed equal activity as the native enzyme. Moreover, 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 -