The interaction of collagenase with hydroxyapatite and related materials and enzymatic properties of the adsorbed enzyme.

The commercial collagenase from Clostridium histolyticum was adsorbed on hydroxyapatite, on bovine femur shaft and on enamel and dentin powders. The substrate specificity of the adsorbed enzyme tested, with chromophore substrate, azocoll and native collagen, differed from that obtained with the soluble enzyme. The adsorption and the substrate specificity was also dependent on the adsorbent used. A pretreatment of hydroxyapatite with chondroitin sulphate, hyaluronate and DNA lowered the adsorption of collagenase. Phosphate ion caused desorption of the enzyme from hydroxyapatite. Sodium fluoride caused partial desorption of the enzyme from hydroxyapatite and enamel and dentin powders. Colangenase adsorbed on root surfaces of teeth liberated hydroxyproline containing material.