coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase
efficient method for N-acetyl-D-neuraminic acid production using coupled bacterial cells with a safe temperature-induced system, a precursor for producing many pharmaceutical drugs such as zanamivir which have been used in clinical trials to treat and prevent the infection with influenza virus, such as the avian influenza virus H5N1 and the current 2009 H1N1
production of N-acetyl-D-neuraminic acid, which is the major representative of amino sugars. The synthesis of N-acetyl-D-neuraminic acid is of interest in studies towards inhibitors of neuraminidase, hemagglutinin and selectin-mediated leucocyte adhesion
method to produce N-acetylneuraminic acid efficiently. Using a recombinant human renin binding protein (rhRnBp) showing GlcNAc-2-epimerase activity and Escherichia coli sialic acid aldolase, about 80% conversion yield of Neu5Ac is obtained in the coupling reaction under 10fold excess of pyruvate to GlcNAc based on the initial concentration of GlcNAc. The equilibrium of GlcNAc-2-epimerase reaction is not affected by temperature, whereas that of sialic acid aldolase reaction is shifted toward Neu5Ac by lowering the reaction temperature. Low temperatures improve the conversion yield of Neu5Ac, but decrease the reaction rate in the coupling reaction. A high reaction rate as well as a high conversion yield can be achieved by shifting the temperature of the coupling reaction during the reaction
4.1.3.3 N-acetylneuraminate lyase
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