Abstract
Clones of a gene encoding an endo-1, 4-β-glucanase (EC 3.2.1.4) were obtained from Bacillus sp. 22-28, and the nucleotides were sequenced. A recombinant plasmid, pMK5, included a complete ORF of 2352bp that encoded 783 amino acid residues. Another plasmid, pM3, which showed enzymatic activity in E. coli JM109, was also obtained, and it included an incomplete ORF of 1873bp, which lacked the original stop codon and 479 bp of the C-terminal region. The enzymes purified from both of the two types of transformants have shown almost the same properties in comparison with that of the wild type Bacillus sp. 22-28.
