Partial Purification and Properties of a Bacterial Isoamylase

Richard M Evans, David J Manners, J Roger Stark

    Research output: Contribution to journalArticle

    Abstract

    Isoamylase has been prepared by affinity chromatography of a commercial enzyme-preparation from a strain of Cytophaga (also known as a Flavobacterium] or Polyangium). The enzyme was not very stable, but the stability could be improved by calcium ions. The enzyme had a very low but significant activity on pullulan and on alpha-dextrins having maltosyl side-chains. This observation, which is contrary to previous reports, has been related to the specificity of isoamylase and other barterial debranching-enzymes. © 1979.

    Original languageEnglish
    Pages (from-to)203-213
    Number of pages11
    JournalCarbohydrate Research
    Volume76
    Issue number1
    Publication statusPublished - Nov 1979

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    Isoamylase
    Purification
    Enzymes
    Dextrins
    Affinity chromatography
    Ions
    Calcium

    Cite this

    Evans, R. M., Manners, D. J., & Stark, J. R. (1979). Partial Purification and Properties of a Bacterial Isoamylase. Carbohydrate Research, 76(1), 203-213.
    Evans, Richard M ; Manners, David J ; Stark, J Roger. / Partial Purification and Properties of a Bacterial Isoamylase. In: Carbohydrate Research. 1979 ; Vol. 76, No. 1. pp. 203-213.
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    Evans, RM, Manners, DJ & Stark, JR 1979, 'Partial Purification and Properties of a Bacterial Isoamylase', Carbohydrate Research, vol. 76, no. 1, pp. 203-213.

    Partial Purification and Properties of a Bacterial Isoamylase. / Evans, Richard M; Manners, David J; Stark, J Roger.

    In: Carbohydrate Research, Vol. 76, No. 1, 11.1979, p. 203-213.

    Research output: Contribution to journalArticle

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    Evans RM, Manners DJ, Stark JR. Partial Purification and Properties of a Bacterial Isoamylase. Carbohydrate Research. 1979 Nov;76(1):203-213.