Purification and Characterization of β-Fructofuranosidase from Bifidobacterium infantis

概要

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β-Fructofuranosidase activities of eight strains of Bifidobacteria, intestinal bacteria, were assayed and Bifidobacterium infantis was selected for purification of the enzyme. β-Fructofuranosidase activity was recovered in the supernatant fraction after disruption of B. infantis cells with sonication and was purified to homogeneity by ammonium sulfate fractionation, and DEAE-cellulose, butyl-Toyopearl and Sephacryl S-300 column chromatographies. The enzyme (molecular weight (M.W.) 232000) was composed of three identical subunits (M.W.75000) whose NH_2-terminal amino acids were threonine. The enzyme was stable at pH 6-8,having the optimum activity at pH 6.0-6.2. The enzyme activity was stable under 40℃ and the optimal temperature was 55℃. This enzyme catalyzed the hydrolysis of sucrose, 1-kestose, nystose, inulin and raffinose at the relative velocities of 100,297,365,140 and 3.8,respectively, but did not catalyze the hydrolysis of maltose or cellobiose. These results indicated that this fructooligosaccharide hydrolyzing enzyme is a novel type of β-fructofuranosidase.
社団法人日本薬学会の論文
1994-05-15