Abstract
An endoglucanase gene from glycoside hydrolase family 5, had been isolated from Bacillus sp. RP1 and cloned into Escherichia coli . The cloned gene comprised the promoter, coding sequence and terminator of the gene. This gene encoded a protein with 499 amino acid residues (Mr=55.2 kDa) with a typical Bacillus signal peptide. The recombinant endoglucanase (EG) had optimum activity at pH 5.0 and 50 °C. The recombinant EG was expressed in the extracellular, intracellular, and periplasmic fractions with the highest total activity (60.15%) in the intracellular fraction, measured at three hours after isopropyl-β-Dthiogalactopyranoside (IPTG) induction. Three hours after the addition of 1% carboxymethyl cellulose (CMC), there was a two-fold increase in intracellular EG specific activity compared to the uninduced cells. Three hours after the addition of 1 mM IPTG, 1% glucose, 1% galactose or 1% cellobiose the intracellular EG specific activity decreased compared to the uninduced cells.
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