Author/Authors :
karam, e. a. national research centre - microbial chemistry dept., Giza, Egypt , hassan, m. e. national research centre - centre of excellence - encapsulation nanobiotechnology group, natural and microbial product chemistry dept., Giza, Egypt , moharam, m. e. national research centre - microbial chemistry dept., Giza, Egypt , kansoh, a. l. national research centre - microbial chemistry dept., Giza, Egypt
Abstract :
Crude inulinase produced by Rhizopus oligosporus NRRL2549 was effectively immobilized on a novel alginate/k-Carrageen beads that were hardened with glutaraldehyde. The pH activities of the free and immobilized enzyme were optimal at pHs of 5.5 and 6.0, respectively. The optimal reaction temperature was shifted from 45°C to 55°C for the immobilized inulinase enzyme. On the other hand, thermal stability investigated that the activity of the free enzyme was reduced to 54% at 80°C after 30 minute while the immobilized form retained 76% of its activity at the same condition. Achieved immobilization yield was 84.6 % and the immobilized enzyme was reused 18 times retaining 90.2% of its activity. continuous production of fructose from inulin by the immobilized inulinase was also investigated.
Keywords :
Inulinase , Enzyme , Stability , Rhizopus oligosporus , Immobilization
