Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei

Elisabetta Sabini, Keith Wilson, Matti Siika-aho, Claire Boisset, Henri Chanzy (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    7 Citations (Scopus)

    Abstract

    The enzymatic degradation of single crystals of mannan I with the catalytic core domain of a β‐mannanase (EC 3.2.1.78 or Man5A) from Trichoderma reesei was investigated by transmission electron microscopy and electron diffraction. The enzyme attack took place at the edge of the crystals and progressed towards their centres. Quite remarkably the crystalline integrity of the crystals was preserved almost to the end of the digestion process. This behaviour is consistent with an endo‐mechanism, where the enzyme interacts with the accessible mannan chains located at the crystal periphery and cleaves one mannan molecule at a time. The endo mode of digestion of the crystals was confirmed by an analysis of the soluble degradation products.

    Original languageEnglish
    Pages (from-to)2340 - 2344
    Number of pages5
    JournalEuropean Journal of Biochemistry
    Volume267
    Issue number8
    DOIs
    Publication statusPublished - 2000
    MoE publication typeA1 Journal article-refereed

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