USE OF IMMOBILIZED L-ARABINOSE ISOMERASE FOR PRODDUCTION OF TAGATOSE

USE OF IMMOBILIZED L-ARABINOSE ISOMERASE FOR PRODDUCTION OF TAGATOSE

  • محمد عبد الرزاق الصوفي
Keywords: immobilized enzyme, L-arabinose isomerase, bentonite, D-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.

Author Biography

محمد عبد الرزاق الصوفي

Professor PhD., Market Research and Consumer Protection Center, University of Baghdad, Baghdad, Iraq

Published
2019-04-07