The Stability Pattern of the Cellulase Enzyme Produced by Aspergillus flavus

In view of the fact that temperature plays key role in the activity of fungal cellulases, this experiment was designed to assess the stability pattern of the cellulase Enzyme produced by Aspergillus flavus derived from rotten wood. The characterization of the purified cellulase enzyme of Aspergillus flavus was carried out using Carboxymethyl cellulose, Filter paper and Cotton wool assays. The maximum and optimum temperatures were 90°C and 70°C, respectively. The enzyme retained above 50% of its original activity at 100°C for 1h and up to 80% at 80°C for 1h Enzyme decay study showed that Cellulase activity remained 100 % at 0 h for both CMC and filter paper. However, as incubation period increased, the activity decreased, but the enzyme still retained above 50 % activity in both substrates at 1h, over the range of 40-100°C. The study carried out showed that the purified Aspergillus flavus cellulases demonstrated useful properties among which include; high optimum temperature, increased thermal stability. They also offer additional advantage as they are more rigid than meso enzymes and moreover, are more resistant to thermal and chemical denaturation. Hence are remarkable tools for developing commercial biotechnologies and for studying protein stability.