Purification and Characterization of Pectinase from Bacillus licheniformis obtained from a Cassava Waste Dump

This study investigated the properties of pectinase from Bacillus licheniformis. The pectinase secreted by the microorganism was purified using ion exchange and gel filtration chromatography on DEAE-Sephadex and Sephadex G-200 respectively. A purification fold of 10.5, yield of 23.9% and specific activity of 9.47 U/mg was obtained. The characteristics of the enzyme included a native molecular weight of 38 kDa, pH optimum 9.0, temperature stability between 35 and 45ºC; temperature optimum 50°C. Inhibition of the enzyme was observed with metal and chemicals, such as Ba2+, Al3+, Mg2+, EDTA, benzoic acid, tannic acid, citric acid and sodium oxalate, however the enzyme activity was enhanced in the presence of K+ and Na+. Other enzymatic properties was Km values of 1.37, 1.62, and 9.09 mg/ml for polygalacturonic acid, 7.8% methylated pectin and 67% methylated pectin respectively The pectinase produced have some desirable characteristics that could be utilised in many industrial processes.