β-N-Acetylglucosaminase in bovine milk

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Abstract
A [beta] -N-acetylglucosami-nase was found in bovine milk, and its properties were investigated. The highest specific activity of the enzyme was found to be associated with cellular material that can be readily sedimented. The enzyme resembles catalase in its distribution within the subf ractions of milk, and may be derived from milk leukocytes. The optimum pH for the hydrolysis of p-nitrophenyl [beta]-N-acetylglucosaminide is 4. 2 and the apparent Michaelis constant for this hydrolysis is 1.0 mM. The enzyme is inhibited by acetate ions, N-acetylglucosamine, and heparin. Inhibition by p-chloromercuribenzoate is not overcome by excess dithiothreitol.

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