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1963•Canadian Journal of ChemistryOpen access

THE USE OF ENZYMES IN STRUCTURAL STUDIES ON POLYSACCHARIDES: I. THE MODE OF ATTACK OF A β- D -(l → 3)-GLUCANASE ON LAMINARIN

T. E. Nelson, Joseph V. Scaletti, F. Smith, S. Kirkwood

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Abstract

A β-D-(1 → 3)-glucanase from the Basidiomycete sp. QM 806 of Reese and Mandels has been purified and shown to hydrolyze insoluble laminarin by removing glucose residues one at a time from the non-reducing end of the polysaccharide. The enzyme will also hydrolyze simple oligosaccharides and its mode of attack on these is similar to its action on laminarin. The products produced by the action of this preparation on laminarin are consistent with recent information on the structure of this polysaccharide.

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A β-D-(1 → 3)-glucanase from the Basidiomycete sp. QM 806 of Reese and Mandels has been purified and shown to hydrolyze insoluble laminarin by removing glucose residues one at a time from the non-reducing end of the polysaccharide. The enzyme will also hydrolyze simple oligosaccharides and its mode of attack on these is similar to its action on laminarin. The products produced by the action of this preparation on laminarin are consistent with recent information on the structure of this polysaccharide.

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Available abstract

A β-D-(1 → 3)-glucanase from the Basidiomycete sp. QM 806 of Reese and Mandels has been purified and shown to hydrolyze insoluble laminarin by removing glucose residues one at a time from the non-reducing end of the polysaccharide. The enzyme will also hydrolyze simple oligosaccharides and its mode of attack on these is similar to its action on laminarin. The products produced by the action of this preparation on laminarin are consistent with recent information on the structure of this polysaccharide.

Key concepts: Laminarin, Polysaccharide, Chemistry, Glucanase, Hydrolysis, Enzyme, Biochemistry, Mode of action

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