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Isolation and partial characterization of an 87-kilodalton beta-1,3- glucanase from Bacillus circulans IAM1165

Article Abstract:

Bacillus circulans IAM1165 is a fungus that produces cellulytic enzymes. These extracellular enzymes, beta-1,3-glucanases, produce two enzymes that have different chromatographic behaviors and molecular masses.One of these enzymes was isolated from the culture supernatant and partially characterized in this study. It was detected by immunoblotting method and purified by hydrophobic chromatography which showed that the enzyme was an anionic protein. This 87-kilodalton endo-beta-1,3-glucanase randomly cleaved with laminarin as a substrate at an optimum temperature of 70 degrees Centigrade.

Enzymes, Lyases

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Isolation of extracellular 28- and 42-kilodalton beta-1,3-glucanases and comparison of three beta-1,3-glucanases produced by Bacillus circulans IAM1165

Article Abstract:

Standard techniques help purify the extracellular 28- and 42-kDa beta-1,3-glucanases produced by Bacillus circulans IAM1165. A comparative study of the characteristics of these enzymes with previously isolated 91-kDa enzymes reveals that the 42-kDa enzyme is the most effective in lysing fungal cell walls. The 28- and 42-kDa beta-1, 3-glucanases exhibit similar enzymatic characteristics and are the members of endo type 1,3-beta-D-glucan glucanohydrolases. At 60 degrees Celsius these enzymes exhibit optimum activity.

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Characterization and substrate specificity of an endo-beta-1,4-D-glucanase I (Avicelase I) from an extracellular multienzyme complex of Bacillus circulans

Article Abstract:

Chromatographic techniques help purify an endo-1,4-beta-D-glucanase I from an extracellular celluloxylanosome of Bacillus circulans F-2. Gel filtration and gel electrophoresis help determine the molecular weight of the enzyme. Activity of the enzyme is optimum at 50 degrees Celsius. The enzyme exhibits significant substrate specificity toward carboxymethyl cellulose.

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