Large-scale applicable purification and characterization of a membrane-bound PQQ-dependent aldose dehydrogenase

Maria Smolander (Corresponding Author), Johanna Buchert, Liisa Viikari

    Research output: Contribution to journalArticleScientificpeer-review

    19 Citations (Scopus)

    Abstract

    A membrane-bound xylose oxidizing PQQ-dependent dehydrogenase from Gluconobacter oxydans was purified with a simple large-scale applicable purification procedure. The activity recovery from membrane extract was 33% with 130-fold purification. Important characteristics with respect to the application of the dehydrogenase in biosensor technology were studied. The purified enzyme was most stable in the pH range 3.5–6.5. The pH optimum for xylose oxidation was in the range 7.5–8 for the solubilized enzyme. Optimal pH for the electrochemical detection of xylose oxidation was 6.5. Dimethyl and carboxylic acid derivatives of ferrocene were able to mediate electrons transferred in xylose oxidation from the enzyme immobilized on graphite electrode to the electrode. Hence the purified enzyme appeared to be suitable for biosensor applications.

    Original languageEnglish
    Pages (from-to)287 - 297
    Number of pages11
    JournalJournal of Biotechnology
    Volume29
    Issue number3
    DOIs
    Publication statusPublished - 1993
    MoE publication typeA1 Journal article-refereed

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