USE OF IMMOBILIZED L-ARABINOSE ISOMERASE FOR PRODDUCTION OF TAGATOSE

Abstract

L-arabinose isomerase from Escherichia coli O157:H7 Was immobilized with activated Bentonite from local markets of Baghdad, Iraq by 10% 3-APTES and treated with 10% aqueous glutaraldehyde, the results refer that the yield of immobilization was 89%, and pH profile of free and immobilized L-arabinose isomerase was 7 and 7.5 and it is stable at 6-8 for 60 min respectively, while, the optimum temperature was 30 and 35°C and it was stable at 35 and 40°C for 60 min but it loses more than 60 and 30% from its original activity at 50°C for free and immobilized L-arabinose isomerase respectively. Immobilized enzyme retained its full activity for 32 day, but it retained 73.58% of its original activity after storage for 60 day at 4°C, and its retained a full activity for 36 continue usage; while it retained 84.63% of its original activity after 50 continue usage. Immobilized enzyme could to get about 85% of D-tagatose from 100 gm\L of D-galactose as a substrate with at 80 rpm of reaction speed for 24 hr.