Abstract
Abstract Bacillus sp. KC201 was newly isolated from soil as a high cyclodextrin glucanotransferase (CGTase)-producing bacteria. The CGTase from Bacillus sp. KC201 converted 39.5% of soluble starch to cyclodextrins and the ratio of β-: γ-cyclodextrin produced was 6.2: 1. No α-cyclodextrin was produced. A gene coding for the CGTase from Bacillus sp. KC201 was cloned into Escherichia coli, and its nucleotide sequence was determined. Starting at an ATG codon, there was an open reading frame composed of 2175 bp (725 amino acids). The NH2-terminal portion encoded a 51 amino acid-long signal peptide. The deduced amino acid sequence of the extracellular mature enzyme (674 amino acids) was identical with that of the CGTase from alkalophilic Bacillus sp. 1-1. Enzyme preparations purified from the culture supernatant of Bacillus sp. KC201 and from the intracellular fraction of the E. coli transformant had the same molecular weight. Amino acid sequences of both enzymes at the NH2-terminal were consistent with each other. However, the enzymatic properties were slightly different.
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