Studies on Dextranase. VII. The Kinetic Parameters of Brevibacterium fuscum Dextranase and Molecular Properties of the Digestion Products
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概要
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Hydrolysis actions of dextranase (EC 3. 2. 1. 11) from Brevibacterium fuscum var. dex-tranlyticum on dextrans with various molecular weights (5.0×10^3-approx. 1.0×10^7) were investigated comparing with those of Penicillium funiculosum IAM 7013 dextranase. The specific activities were measured as an increase of reducing sugar per min per mg protein at the substrate concentration 1.34%. The activities of B. fuscum dextranase were 110-190 μmoles as glucose for various dextrans. Those of P. funiculosum dextranase were, however, almost constant and approximately 400 μmoles for dextrans examined. The K_m values (%) and V_<max> values (μmoles/min per mg protein) of B. fuscum dex-tranase decreased with an increase in molecular weight of dextrans. K_m values were 0.041-0.065 and V_<max> values were 76-128. However, both values of P. funiculosum dextranase were constant, and K_m remained at about 0.2 and V_<max> was approximately 800. Molecular properties of digestion products by B. fuscum dextranase were investigated. The polymerization degree of the products in the oligosaccharide fraction was constantly 3 in spite of an increase of reducing sugar content in the reaction mixture. Molecular size of the products was also investigated by the gel filtration on Bio Gel P-60. The fractionation patterns were markedly different from those of P. funiculosum dextranase as a typical endo-enzyme. These results indicated that the enzyme acted as an exo-dextranase at early reaction stage, and finally the enzyme might be able to hydrolyze the residual part of the substrate ; i. e. core dextran having branching points.
- 公益社団法人日本薬学会の論文
- 1975-07-25
著者
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杉浦 衛
Department of Pharmacy, Tokyo College of Pharmacy
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杉浦 衛
Tokyo College Of Pharmacy
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伊東 晃
Department of Biochemistry, Tokyo College of Pharmacy
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伊東 晃
Department Of Pharmacy Tokyo College Of Pharmacy
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