Cloning and Sequence Analysis of the Cycloisomaltooligosaccharide Glucanotransferase Gene from Bacillus ciyculans T-3040 and Expression in Escherichia coli Cells

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The gene for cycloisomaltooligosaccharide glucanotransferase from Bacillus circulars T-3040 was cloned and expressed in the recombinant plasmid pCI429 in Escherichia coli. The enzyme gene consisted of a unique open reading frame of 2916 bp. Comparison of the DNA sequence data with the N-terminal, C-terminal and 12 internal amino acid sequences of the purified enzyme secreted from B. circulars T-3040 suggested the enzyme was translated from mRNA as a secretory precursor with a signal peptide of 38 amino acid residues. The deduced amino acid sequence of the mature enzyme contained 934 residues, resulting in a polypeptide with a molecular mass of 103, 103 Da. It had no common consensus region which is characteristic of the α-amylase family. The cycloisomaltooligosaccharide glucanotransferase activity, cyclization activity in transformant was about 3.0 mU/ml which was the same as that from B. circulars T-3040.
日本応用糖質科学会の論文