In order to investigate the functions of the C-terminal region of chitinase ChiCW of Bacillus cereus 28-9, a C-terminal truncated enzyme, ChiCW$Delta$FC, was expressed in Escherichia coli and purified to homogeneity for biochemical characterization. Compared with ChiCW, ChiCW$Delta$FC exhibited higher chitinase activity at high temperature and pH, but expressed lower hydrolytic and binding activities toward insoluble substrates. In addition, kinetic properties indicated that ChiCW$Delta$MC hydrolyzed oligomeric and polymeric substrates less efficiently than ChiCW. These results suggest that the C-terminal region of ChiCW plays important roles in substrate binding and hydrolysis of chitin. In addition, the biological meaning of C-terminal proteolytic modification of ChiCW is discussed.