A novel method for the immobilization of a thermostable fungal chitinase and the properties of the immobilized enzyme

The recombinant thermostable fungal chitinase of T hermomyces lanuginosus was immobilized on the phenyl S epharose matrix, and the properties of the immobilized chitinase were studied. The immobilized enzyme was optimally active at p H 6.0 and 50 °C and showed improved activity in the acidic range of p H values when compared with the soluble enzyme. The recombinant thermostable immobilized enzyme showed remarkable thermostability at 50 °C by retaining about 45% of the activity for more than 6 H. The K M and V max values were 1.3 mM and 4.5 mol/min/mg of protein, respectively. Both the free and immobilized forms of the enzymes were inhibited significantly by A g + but behaved similarly to various other metal ions, detergents, and additives. The immobilized enzyme was stable for at least 1 month at 4 °C.