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标题：Purification and Characterization of β-Fructofuranosidase from Bifidobacterium infantis
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作者：Lisa IMAMURA ; Kenichi HISAMITSU ; Kyoichi KOBASHI 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：1994
卷号：17
期号：5
页码：596-602
DOI：10.1248/bpb.17.596
出版社：The Pharmaceutical Society of Japan
摘要：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 NH₂-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°C and the optimal temperature was 55°C. 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.
关键词：β-fructofuranosidase;fructooligosaccharide;Bifidobacterium infantis;Bifidobacteria;intestinal bacteria