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

    Fingerprint

    rye
    enzymes
    gels
    isoelectric focusing
    ion exchange chromatography
    bovine serum albumin
    chlorides
    cellulose
    buffers
    proteins

    Keywords

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

    Cite this

    Ballance, G Murray ; Manners, David J. / Partial purification and properties of an endo-1,3-β-d-glucanase from germinated rye. In: Phytochemistry. 1978 ; Vol. 17, No. 9. pp. 1539-1543.
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    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. {\circledC} 1978.",
    keywords = "cereal β-d-glucans., endo-1,3-/gb-d-glucanase, germinated rye, Gramineae, Secale cereale",
    author = "Ballance, {G Murray} and Manners, {David J}",
    year = "1978",
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    Ballance, GM & Manners, DJ 1978, 'Partial purification and properties of an endo-1,3-β-d-glucanase from germinated rye', Phytochemistry, vol. 17, no. 9, pp. 1539-1543.

    Partial purification and properties of an endo-1,3-β-d-glucanase from germinated rye. / Ballance, G Murray; Manners, David J.

    In: Phytochemistry, Vol. 17, No. 9, 1978, p. 1539-1543.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Partial purification and properties of an endo-1,3-β-d-glucanase from germinated rye

    AU - Ballance, G Murray

    AU - Manners, David J

    PY - 1978

    Y1 - 1978

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    AB - 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.

    KW - cereal β-d-glucans.

    KW - endo-1,3-/gb-d-glucanase

    KW - germinated rye

    KW - Gramineae

    KW - Secale cereale

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    JO - Phytochemistry

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