Summary: Hyaluronidase from has been purified 13000-fold from the culture supernatant to homogeneity (as determined by polyacrylamide disc gel electrophoresis). The molecular weight of the purified enzyme was 85110 as determined by gel filtration. The purified enzyme had a pH optimum at 6.4, was stable between pH 5 and 5.8 and was completely inactivated after 15 min at 50°C. Preliminary studies suggested that the enzyme is active against chondroitin 4- and 6-sulphates, but not against dermatan sulphate. Analysis by paper chromatography of the reaction products from the degradation of hyaluronic acid by bacterial, testicular and enzymes suggested that the enzyme is similar in its mode of action to other bacterial hyaluronate lyases. The enzyme from may thus be tentatively classified as a hyaluronate lyase.


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