Purification and Substrate Specificity of endo-Type Inulinase from Penicillium purpurogenum(Biological Chemistry)
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概要
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An inulinase was highly purified from the culture broth of Penicillium purpurogenum by chromatographies on DEAE-Sepharose CL-6B, Toyopearl HW-65, and Bio-Gel P-100. The enzyme was homogeneous by disc electrophoretic analysis. The molecular weight was 6.4×10^4 by SDS-disc electrophoresis and gel filtration on Bio-Gel P-150. The isoelectric point was pH 3.6 by isoelectric focusing. The enzyme hydrolyzed inulin rapidly, but did not affect sucrose. By paper chromatography analysis, the major products from inulin were tri-, tetra-, penta-, and hexa-saccharides. The substrate specificity of the enzyme on hydrolyses of fructo-oligosaccharides[1^F(1-β-D-fructofuranosyl)_nsucrose (n=1 to 6 and n^^- (average of polymerization degree)=8)] were examined. The Km values and relative maximum velocities for the hydrolyses of inulin and fructo-oligosaccharides (GF_n, n=2 to and n^^n=9) were as follows: inulin, (D^^-P^^-=35) 0.21 mM and 100; GF_9, 0.24 mM and 86.5; GF_7, 0.33 mM and 132; GF_6, 0.85 mM and 71.2; GF_5, 3.8 mM and 25.4; GF_4, 2.8 mM and 28.8; GF_3, (nystose) 16 mM and 0.8; GF_2 (1-kestose), 8.4 mM and 0.2. The molecular activities for the hydrolyses of fructo-oligosaccarides (GF_n, n=2 to 6) were increased depending on the degree of polymerization of fructosyl residues, and were nearly constant if the polymerization degree over seven. These results strongly suggested that the endo-type inulinase from Penicillium purpurogenum had a subsite structure consisting of at least seven subsites.
- 社団法人日本農芸化学会の論文
- 1988-10-23
著者
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Shiomi Norio
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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Onodera Shuichi
Department Of Cardiology Shizuoka City Shizuoka Hospital
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Onodera S
Rakuno Gakuen Univ. Hokkaido Jpn
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