International Journal of Biotechnology Applications

130-133

Authors: KO YOUNG HWAN, KIM YU-KYOUNG, OH HYUN-JEONG

Three Bacillus subtilis strains were isolated from soil, compost and animal waste slurry in Jeju Island, Korea and their endo-β-1,4-glucanase genes cloned. Cellulase genes from B. subtilis SL9-9, C5-16 and S52-2 encoded proteins of 480, 470 and 499 amino acid residues, respectively. DNA sequences of the genes were compared with those of other known cellulase genes. The deduced amino acid sequences of the cellulase genes from the isolates matched quite well the modern concepts of multidomain cellulolytic enzymes. The enzymes were composed of three discrete domains: catalytic domains (CD) of glucosyl hydrolase family 5/A2 and interdomain linker and cellulosebinding domains (CBD) of family IIIa. Similar to the modular organization of many Bacillus endoglucanases, the CDs of these enzymes were located in the N-terminal region and CBDs in the C-terminal region.