Purification and characterization of bacillus cereus cellulase using semi-solid state fermentation

ABSTRACT

Cell free extract of Bacillus cereus was fractionated by 50% ammonium sulphate resulting in 22.5% protein reduction, and purified by 133.3 fold using chromatography on DEAE-Sephadex A50 and CM-Sephadex C[50]. The pure enzyme consists of one peptide chain with molecular weight of 58,000 Dalton. The enzyme was found to be rich in glycine, glutamic, serine and alanine. The apparent K[m] and V[max] values of the purified enzyme were 2.56 mg/ml and 91.74U/ml respectively. Maximum cellulase activity was observed when incubated with CMC [carboxymethyl cellulose] at pH 7 for 30 min. at 45°C