Activity Test, Selectivity, Stability of Chitinase on Amobil Chitosan Membranes

Abstract

The use of enzymes for industrial functions needs enzymes that are stable, selective and might be used repeatedly. The aim of the study was to determine the chitinase enzyme's function, selectivity, and stability in amobil chitosan membranes. The research method consisted of stages: production of the chitinase enzyme which included the manufacture of chitin colloidal substrate, rejuvenation of thermophilic bacteria, preparation of the inoculum and determining the optimum time of production, fractionation of ammonium sulfate, chitinase enzyme immobilization technique and activity, stability and selectivity test of amobil enzyme. The results demonstrated that chitinase activity, which incorporates the optimum temperature and thus the optimum concentration of production within the immobilization technique, had an optimum temperature of 65oC on day 4 of production time with an OD value of 0.9876. The selectivity of amobil chitinase with metal ions Cd (II), Pb (II), Zn (II), and Hg (II) demonstrated that amobil chitinase was selective for these ions. Eamobil chitinase was heat stable at 55-75oC and resistant to organic solvents, suggesting that it could be used repeatedly.