Purification and Characterization of an Endo-1,4-.BETA.-glucanase from Neisseria sicca SB that Hydrolyzes .BETA.-1,4 Linkages in Cellulose Acetate.

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  • MORIYOSHI Kunihiko
    <i>Department of Biochemistry, Osaka Municipal Technical Research Institute</i>
  • OHMOTO Takashi
    <i>Department of Biochemistry, Osaka Municipal Technical Research Institute</i>
  • OHE Tatsuhiko
    <i>Department of Biochemistry, Osaka Municipal Technical Research Institute</i>
  • SAKAI Kiyofumi
    <i>Department of Biochemistry, Osaka Municipal Technical Research Institute</i>

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  • Purification and Characterization of an Endo-1,4-β-glucanase from Neisseria sicca SB that Hydrolyzes β-1,4 Linkages in Cellulose Acetate
  • Purification and Characterization of an Endo 1 4 ベータ glucanase from Neisseria sicca SB that Hydrolyzes ベータ 1 4 Linkages in Cellulose Acetate
  • Purification and Characterization of an Endo-1,4-β-glucanase from<i>Neisseria sicca</i>SB that Hydrolyzes β-1,4 Linkages in Cellulose Acetate

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  An enzyme catalyzing hydrolysis of β-1,4 bonds in cellulose acetate was purified 18.3-fold to electrophoretic homogeneity from a culture supernatant of Neisseria sicca SB, which can assimilate cellulose acetate as the sole carbon and energy source. The molecular mass of the enzyme was 41 kDa and the isoelectric point was 4.8. The pH and temperature optima of the enzyme were 6.0–7.0 and 60°C. The enzyme catalyzed hydrolysis of water-soluble cellulose acetate (degree of substitution, 0.88) and carboxymethyl cellulose. The Km and Vmax for water-soluble cellulose acetate and carboxymethyl cellulose were 0.242% and 2.24 μmol/min/mg, and 2.28% and 12.8 μmol/min/mg, respectively. It is estimated that the enzyme is a kind of endo-1,4-β-glucanase (EC 3.2.1.4) from the substrate specificity and hydrolysis products of cellooligosaccharides. The enzyme and cellulose acetate esterase from Neisseria sicca SB degraded water-insoluble cellulose acetate by synergistic action.<br>

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