Partial purification and properties of an endo-1,3-β-d-glucanase from germinated rye

G Murray Ballance, David J Manners

    Research output: Contribution to journalArticle

    Abstract

    An endo-1,3-ß-d-glucanase from germinated rye was purified 58-fold by ion exchange chromatography on DEAE- and CM-cellulose, and by gel filtration on Bio Gel P-60. The enzyme had pH optima of 5.0 with laminarin and 5.7 with carboxymethyl pachyman and was stable up to 45°. Bovine serum albumin and certain chlorides increased the activity at low concentrations of buffer. With laminarin, the enzyme had a Km of 0.25 mg/ml and the MW was estimated to be 24 300. Isoelectric focusing indicated that the endo-1,3-/gb-d-glucanase was a basic protein. The properties of the enzyme are compared with those from other higher plants. © 1978.

    Original languageEnglish
    Pages (from-to)1539-1543
    Number of pages5
    JournalPhytochemistry
    Volume17
    Issue number9
    Publication statusPublished - 1978

    Keywords

    • cereal β-d-glucans.
    • endo-1,3-/gb-d-glucanase
    • germinated rye
    • Gramineae
    • Secale cereale

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