Chitin is a linear polysaccharide that consists of β-1,4-linked N-acetyl-glucosamine (GlcNAc) and it forms the carbohydrate backbone of crustacean and insect exoskeletons. Chitinase has the ability to degrade these chitins to its product chitin oligosaccharides which are used in potential applications of biomedicine, nutrition and bio-technology. Bacillus thuringiensis is one of the well-known bacteria producing chitinase. In present study, we identified and purified the chitinase from B. thuringiensis PRCII. Chitinase activity assay using crap shell chitin and T. molitor chitin indicates that three chitinases approximately 37, 42, and 71 kDa were detected from B. thuringiensis PRCII. In addition, we cloned and expressed the 71 kDa chitinase from B. thuringiensis PRCII. These chitinases exhibited two chitinase protein activity 71 and 50 kDa in both native and rBtchitinase using crap shell and T. molitor chitin. On the basis of the in silco analysis of Btchitinase, Btchitinase lacks chitin binding domain. However, it exhibited the active chitinase activity, suggesting that chitin binding domain is not necessary for chitin hydrolysis.