Date Received: 20-06-2018 / Date Accepted: 28-11-2018
The objective of the present study was to purify and determine the properties (optimal temperature, heat stability, optimal pH, pH stability, effects of metal ions) of cellulase derived from Bacillussp. M5strain. The crude enzyme produced from the culture of cellulase-producing bacillus M5 strain was collected by centrifugationand precipitated for purification andcharacterization. To investigate the enzyme's characteristics onoptimal temperature, pH as well as heat stability, pH stability and the effect of certain metal ions, the enzyme fluid was treated under different conditions. The enzymewas disolvedin acetate buffer pH 5.50 mM to determine enzyme activity. Results showed that the cellulase from Bacillus M5 strain was active at an optimaltemperature of 65C; optimalpH of 5.5; heat stability at about 50C (activity remains53% after 120 minutes); pH of 6.0 to 6.5.Ca2+and Mg2+metal ions increasedenzyme activity and Zn2+ion decreasedenzyme activity. The enzyme hadthemolecular weight of 45 kDa.