Substrate Specificity and Subsite Affinities of β-Fructofuranosidase from Bifidobacterium adolescentis G1

概要

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The substrate specificity of β-fructofuranosidase from Bifidobacterium adolescentis G1 for fructooligosaccharides [1^F (1-β-D-fructofuranosyl)_<n-1> sucrose, GF_n , (n=3-8)] andinulooligosaccharides [1^F (1-β-D-fructofuranosyl)_<n-1> fructose, F_n, (n=2-7)] were investigated. The K_m (mM) and k_0 (s^<-1>) values were : GF_3, 1.1 and 155 ; GF_4, 1.6 and 154 ; GF_5, 3.2 and 252 ; GF_6, 4.2 and 186 ; GF_7, 7.1 and 260 ; GF_8, 7.0 and 180 ; F_2, 4.9 and 213 ; F_3, 1.5 and 423 ; F_4, 2.4 and 311 ; F_5, 1.9 and 458 ; F_6, 8.7 and 369 ; F_7, 8.1 and 323, respectively. The enzyme preferred oligosaccharides to inulin and sucrose as the substrate. The enzyme hardly catalyzed transfructosylation from GF_2. The dependence of rate parameters on the degree of polymerization differed from that of Penicillium trzebinskii exo-inulinase. The subsite atfinities in the active site were 0.93, 4.33, 1.15, -0.48, 0.38, -1.07, and -0.04 kcal/mol for subsites 1,2,3,4,5,6, and 7, respectively.
社団法人日本農芸化学会の論文
1994-09-23