Purification and some properties of neuraminidase isolated from the culture medium of oral bacterium Streptococcus mitis ATCC 9811.

Neuraminidase acting on the salivary bacterial agglutinating factor was isolated and purified from the culture medium of Streptococcus mitis ATCC 9811. The molecular weight and the isoelectric point of the enzyme were determined to be 42,000 and a pH of 4.6, respectively. The enzyme showed high activity against human glycoprotein substrates, especially the salivary bacterial agglutinating factor.