10.22376/ijpbs.2019.10.1.p1-12 Volume 4 Issue 4 2013 (October - December) Studies were conducted on the lessThan i greaterThan Bacillus lessThan /i greaterThan sp. neutral protease immobilization on different matrices. The immobilized protease was prepared by three methods, such as entrapment on calcium alginate and gelatin; physical adsorption by celite and alumina; ionic binding by amberlite IR-120 and DEAE-cellulose. The maximum immobilization yield was obtained with celite adsorbed protease. The immobilized enzyme was characterized in comparison with free enzyme. The optimal pH of the immobilized protease was shifted to lower values; and exhibited good thermal stability. The reusability and storage stability of the immobilized enzyme on different carriers was analysed. The ability of lessThan i greaterThan Bacillus lessThan /i greaterThan sp. protease activity even on immobilization and its characteristics could collectively be useful for commercial production. ROOPA PRASAD AND A. JAYAKUMARAN NAIR Bacillus sp., protease, matrices, celite and characterization. 155-161