Purification and Characterization of Some Enzymatic Properties of Neuraminidase fromCorynebacterium ulcerans

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Abstract
Neuraminidase of C. ulcerans was purified by affinity chromatography using immobilized colominic acid preparations. Neuraminidase appears to be a thermolabile protein with a MW of 70,000 daltons. The pH optimum of 5.5 is independent of the substrate used; the optimal temperature is 37.degree. C, and the Km for N-acetylneuraminosyllactose is 5.2 .times. 10-4 M. Ca2+ and Ba2+ activated the enzyme, but Zn2+, Fe2+ and the chelating agent EDTA were inhibitory. The enzyme did not hydrolyze the (.alpha. -2.6) or (.alpha.-2.8) bonds of submaxillary pig mucin and colominic acid, respectively, but it hydrolyzed fetuin, ovomucin, orosomucoid and horse serum glycoproteins.