Purification, Characterization, and Gene Analysis of Cellulase (Cel8A) from Lysobacter sp. IB-9374
Access this Article
Search this Article
An enzyme that has both β-1,4-glucanase and chitosanase activities was found in the culture medium of the soil bacterium <I>Lysobacter</I> sp. IB-9374, a high lysyl endopeptidase-producing strain. The enzyme was purified to homogeneity from the culture filtrate using five purification steps and designated Cel8A. The purified Cel8A had a molecular mass of 41 kDa, as estimated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. A pH optimum of 5.0 was found for the β-1,4-glucanase activity, and pH optima of 5.0 and 7.0 were found for the chitosanase activity. Nucleotide sequencing of the Cel8A gene yielded a deduced amino acid sequence that comprises a 33-amino acid, N-terminal signal peptide and a mature enzyme consisting of a 381-residue polypeptide with a predicted molecular mass of 41,241 Da. The amino acid sequence of the Cel8A, which contains the catalytic module of glycosyl hydrolase family 8, is homologous to β-1,3-1,4-<small>D</small>-glucanase from <I>Bacillus circulans</I> WL-12 and endoglucanase N-257 from <I>B. circulans</I> KSM-N257.
- Agricultural and Biological Chemistry
Agricultural and Biological Chemistry 70(10), 2420-2428, 2006-10-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry