Extracellular partially purified endo (1 -> 4) beta-d-glucanase belong to CAZy Family GH12 produced by Bacillus licheniformis KIBGE-IB2 was immobilized within the microenvironment of calcium alginate beads using entrapment technique. Immobilization technology is one of the supporting technique for obtaining purified product with cost effectiveness. The activities of soluble and immobilized endo (1 -> 4) beta-d-glucanase were compared using carboxymethyl cellulose (CMC) as a substrate. The results showed that the maximum immobilization of enzyme was achieved when calcium chloride (0.2 M) and sodium alginate (2.0%) were used. The pH optima of soluble and immobilized enzyme remain same, but temperature optima (60 A degrees C) of entrapped enzyme shifted to a higher level (70 A degrees C) as compared to soluble enzyme. The scanning electron microscopy analysis reveals the changes in morphology and size of micro pores on the surface of calcium alginate before and after immobilization. The immobilized enzyme showed its reusability up to five cycles. The stability against various inhibitors was also improved after immobilization.