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- W1505332022 abstract "Several concentrations of periodate were used to oxidize barley beta-d-glucan. Measurement of the periodate consumed and Chromatographic examination of the products indicated that the beta-d-glucan was linked by 70% (1 → 4)-bonds and 30% (1 → 3)-bonds. There were no adjacent (1 → 3)-bonds in the beta-d-glucan. The action of A11-endo-beta-glucanase, a germinated barley enzyme which hydrolyzes beta-d-glucan, was tested on compounds containing a variety of beta-glucosidic linkages. The enzyme was unable to hydrolyze laminarin, carboxymethyl cellulose, oligosaccharides containing consecutive (1 → 3)-bonds, consecutive (1 → 4)-bonds, 4-0-beta-d-laminaribiosyl-d-glucose, 4-0-beta-d-laminaribiosyl-d-cellobiose, 3-0-beta-d-cellobiosyl-d-glucose, 3-0-beta-d-cellotriosyl-d-glucose, or two other more complex beta-linked glucose oligosaccharides whose structures are not completely established." @default.
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- W1505332022 date "1965-12-01" @default.
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- W1505332022 title "Mechanism of action of malt beta-glucanases" @default.
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- W1505332022 doi "https://doi.org/10.1016/0003-9861(65)90091-3" @default.
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