Purification and Properties of Cycloinulooligosaccharide Fructanotransferase from Paenibacillus polymyxa MG-CF6

概要

論文の詳細を見る
A bacterial strain which produced a cycloinulooligosaccharide fructanotransferase was isolated from soil and was identified as Paenibacillus polymyxa MG-CF6. The enzyme was then purified to apparent homogeneity from culture supernatant of the bacterium. The molecular mass of the enzyme was estimated to be 128 kDa by SDS-PAGE. Maximal activity was found to be at pH 7.0 and 45°C. The enzyme was stable from pH 6.0 to 9.0 and at temperature up to 40°C. Molar ratio of cycloinulohexaose: cycloinuloheptaose formed by this enzyme was found to be about 2.5:1. N-Terminal amino acid sequence of the enzyme was identical with a part of amino acid sequence of the same enzymes from Bacillus macerans CFC1 and Bacillus polymyxa MGL21. The gene of the enzyme was cloned from P. polymyxa MG-CF6. It consisted of 3999 nucleotides, which encodes a protein of 1333 amino acids. The deduced amino acid sequence showed 83, 95 and 98% similarity to that of Bacillus circulans MCI-2554, Bacillus macerans CFC1 and Bacillus polymyxa MGL21, respectively.
日本応用糖質科学会の論文