Observations on the Salivary Mucolytic Enzymes

Abstract

The mucinase activity of saliva was measured by 3 methods, viz., decrease in mucoid precipitable by an acid-alcohol mixture (ACRA method), decrease in carbohydrate precipitable by trichloracetic acid, and decrease in viscosity. A relationship between the 3 methods was shown. The enzyme titer varies during the day and from day to day in the one person, and there is some variation from person to person. Salivary mucinase has been partly purified by precipitation with acetone alcohol and ammonium sulphate, and adsorption onto kaolin or alumina C 7 followed by elution with [image]/15 (NH4)2HPO4. Salivary mucinase prepared by the last method is inactivated below pH 4.5 and above pH 11.0; also heating to 55[degree]C for 2 min. destroys the enzyme. Studies of possible activators and inhibitors suggest that the enzyme system does not require the presence of sulfhydryl groups but is activated by Mg. Several microorganisms with mucolytic activity have been isolated from saliva and the production of an exocellular mucolytic enzyme has been demonstrated.