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- W2019864956 abstract "1. Arthrobacter ureafaciens inulinase II which converts inulin to di-d-fructofuranose 1,2′ : 2,3′ dianhydride (difructose anhydride III) leaving a small amount of oligosaccharides, was investigated in order to characterize its mode of action. 2. After the enzymatic reaction on the glucose-terminated inulin molecules had been completed, the oligosaccharides left in the enzyme digest were isolated, and identified to be the fructose-glucose oligosaccharides; O-β-d-fructofuranosyl-(2 → 1)-O-β-d-fructofuranosyl α-d-glucopyranoside (1-kestose), O-β-d-fructofuranosyl-[(2 → 1)-O-β-d-fructofuranosyl]2 α-d-glucopyranoside and O-β-d-fructofuranosyl-[(2 → 1)-O-β-d-fructofuranosyl]3 α-d-glucopyranoside. The difructose anhydride formation from the three fructose-glucose oligosaccharides in the separate reaction system with an increased substrate concentration was observed only with the latter two substrates, but not with the first one. 3. The difructose anhydride formation with several (2 → 1)-β-linked fructose oligosaccharides and bacterial (2 → 6)-β-fructans was examined. The (2 → 1)-β-linked fructose oligosaccharides were effective as substrates for the enzyme with the exception of inulobiose, but the (2 → 6)-β-fructans remained unaffected. 4. It was concluded that the enzyme attacks (2 → 1)-β-linked fructan molecules from the nonreducing fructose ends and requires the presence of at least two adjacent (2 → 1)-β-fructofuranosyl linkages." @default.
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- W2019864956 date "1975-07-01" @default.
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- W2019864956 title "Action of Arthrobacter ureafaciens inulinase II on several oligofructans and bacterial levans" @default.
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- W2019864956 doi "https://doi.org/10.1016/0005-2744(75)90189-8" @default.
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