Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

David J Manners, Glynn Wilson

    Research output: Contribution to journalArticlepeer-review

    27 Citations (Scopus)

    Abstract

    An endo-(1?3)-ß-d-glucanase has been isolated from malted barley and purified 92-fold. The enzyme preparation appeared to be physically homogeneous and had a molecular weight of about 12,800 daltons. The enzyme is highly specific for (1?3)-ß-d-glucosidic linkages, and has an endo action on laminaran. The effect of certain group-specific reagents on the enzyme has been examined. © 1974.

    Original languageEnglish
    Pages (from-to)9-22
    Number of pages14
    JournalCarbohydrate Research
    Volume37
    Issue number1
    Publication statusPublished - Oct 1974

    Fingerprint

    Dive into the research topics of 'Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley'. Together they form a unique fingerprint.

    Cite this