An endo-β-mannanase (1, 4-β-D-mannan mannanohydrolase, EC 3. 2. 1. 78.) was isolated from the culture fluid of strain no. F-25 of fleromonas hydyophila subspecies anaerogenes, and purified about 440-fold by ammonium sulfate precipitation, and column chromatographies on DEAE-Sephadex A-50, Amberlite CG-SO, Sephadex G-100, and hydroxylapatite. The final enzyme preparation was regarded as being homogeneous on polyacrylamide gel electrophoresis. The enzyme had a molecular weight of 24,000, p1 of 5.6, pH optimum of 5.5, and was stable in a pH region of 5.0 to 9.0 and at temperatures below 45℃. The enzyme hydrolyzed at random the internal β-1, 4-linkages in mannotetraose and larger oligosaccharides, and in codium mannan, coffee mannan, konjac glucomannan and guar gum galactomannan to give various sizes of oligosaccharides. It did not act on mannobiose and mannotriose.
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