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Separation and characterization of the endo beta 1 3 d glucanase from rhizoctonia solani


Separation and characterization of the endo beta 1 3 d glucanase from rhizoctonia solani



Agricultural and Biological Chemistry 50(3): 543-550



ISSN/ISBN: 0002-1369

The endo-.beta.-(1 .dag.AR 3)-D-glucanase from extracts of Rhizoctonia solani has been purified to homogeneity by chromatographies on CM Bio-Gel A and Bio-Gel P-60 and finally by affinity chromatography on short-chain pachyman-AH-Sepharose. In the ability chromatography, the adsorption of the enzyme seemed to be brought into close with the large spacer arm by prior biospecific adsorption on an attached ligand. The isoelectric point was pH 9.8 and the molecular weight was 29,000. The optimum pH for short-chain pachyman was 5.5. The enzyme was fairly stable at pH 5 to 8.5 and at temperatures below 50.degree. C. The enzyme favors stretches of .beta.-D-(1 .fwdarw. 3)-linkages and also depolymerize .beta.-(1 .fwdarw. 3)-.beta.-(1 .fwdarw. 4) mixed-linked glucan. It has transglycosylase activity.

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Accession: 006390752

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