Anaerobic bacteria producing cellulases have not been extensively studied though they are the efficient producers of cellulase. Clostridium papyrosolvens CFR-1010, an anaerobic cellulolytic bacterial strain was identified as a potent cellulase producer and selected for the purification and kinetic studies of Exo-b-1,4-glucanase and Endo-b-1,4-glucanase. The molecular masses of the enzymes were 65 and 60 kDa, respectively. The enzymes showed maximum activities at pH 5.0 and at the temperature of 50 ^oC. The activities increased  in the presence of MnCl₂, whereas, N-bromosuccinimide decreased enzyme activities by 68 and 75% respectively, thus suggesting the presence of tryptophan residues at the active sites of enzymes. Exoglucanase had a K_m of 20 mg/ml and V_max of 22 units/min/mg of protein whereas the endoglucanase exhibited a K_m of 6.66mg/ml and V_max of 11.76 units/min/mg of protein. Results of the present studies suggest the use of C. papyrosolvens for cellulase production in shorter periods of time and they also add significance for the exploration of this organism for industrial applications.