Abstract
Dextransucrase an enzyme from a new strain of Leuconostoc mesenteroides LM1 cells has been extracted by 10% sucrose acetate buffer solution and purified by ammonium sulphate fractionation. Immobilization of the enzyme on hydroxyapatite changed the temperature optima of the free(soluble) form of dextransucrase from 30 to 50°C. The hydroxyapatite-immobilized dextransucrase could be stored in a refrigerator for 6-8 months and showed activity in 4-5 cycles of repeated use. Similar results were obtained using calcium alginate beads immobilized dextransucrase system. Some of the chemicals which inhibited free dextransucrase had no effect on the immobilized enzyme on hydroxyapatite.
