Purification and Characterization of β-1,6-Glucanase ofStreptomyces rocheiApplication in the Study of Yeast Cell Wall Proteins
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A beta-1,6-glucanase was purified to apparent homogeneity from a commercial yeast digestive enzyme prepared from Streptomyces rochei by a series of column chromatographies. The molecular mass of the purified enzyme was 60 kDa by SDS-PAGE. The purified enzyme had an optimum pH range from 4.0 to 6.0 and was stable in the same pH range. The enzyme was stable under 50 degrees C but lost almost all activity at 60 degrees C. The enzyme was specific to beta-1,6-glucan and had little activity towards beta-1,3-glucan and beta-1,4-glucan. When the beta-1,6-glucan was hydrolyzed with the purified enzyme for 5 h, the reaction products contained 20% glucose, 36% gentiobiose, and 44% other oligosaccharides, suggesting that the enzyme is an endo-type glucanase. When the purified enzyme was used for the digestion of the cell wall of Saccharomyces cerevisiae, cell-wall proteins covalently bound to the cell-wall glucan were recovered as soluble forms, suggesting that this enzyme is useful for analysis of yeast-cell wall proteins.Keywords:
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An alkali-insoluble glucan synthesized from UDP-d-glucose by the particulate enzyme system from Phaseolus aureus is hydrolyzed by a highly purified exo-beta-(1 --> 3)-d-glucanase to d-glucose, to the extent of 91% in 24 hr. The alkali-insoluble glucan from GDP-d-glucose formed by the particulate enzyme system from the same plant which is known to be (from chemical data) a beta-(1 --> 4)-d-glucan (cellulose) is not acted upon by this glucanase.
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A procedure recently described for the assay of malt p-glucanase, which employs a dye-labelled and chemically-modified barley p-glucan substrate, has been improved by changing the precipitant solution used to terminate the reaction.The new precipitant solution contains 0-4% (w/v) zinc acetate and 4% (w/v) sodium acetate dissolved in 80% (v/v) aqueous methyl cellosolve.With this precipitant the procedure can be directly applied to the assay of cellulase activity, and with minor modification, to the assay of lichenase activity.
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Abstract Apricot gummosis pathogens — the fungi Hendersonula toruloidea , a Cytosporina sp. and a Cytospora sp., produce cellulase (endo‐1,4‐β‐glucanase, carboxymethylcellulase, CMCase) in culture. Cytospora sp. produced significantly lower amounts of cellulase than H. toruloidea and Cytosporina sp. The tendency of cellulase accumulation inside apricot stems infected with either H. toruloidea or Cytosporina sp. is similar: most of the cellulase was found in the necrotic area, whereas comparatively small amounts accumulated at the advancing edge of the disease symptom. H. toruloidea produces cellulase with a molecular mass of 76 kDa.
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