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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Xylose
Purification
Enzymes
Membranes
Biosensing Techniques
Biosensors
Oxidation
Oxidoreductases
Electrodes
Gluconobacter oxydans
Immobilized Enzymes
Graphite electrodes
Graphite
Carboxylic Acids
Carboxylic acids
Electrons
Technology
Derivatives
Recovery
aldose dehydrogenase (pyrroloquinoline-quinone)

Cite this

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title = "Large-scale applicable purification and characterization of a membrane-bound PQQ-dependent aldose dehydrogenase",
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.",
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Large-scale applicable purification and characterization of a membrane-bound PQQ-dependent aldose dehydrogenase. / Smolander, Maria (Corresponding Author); Buchert, Johanna; Viikari, Liisa.

In: Journal of Biotechnology, Vol. 29, No. 3, 1993, p. 287 - 297.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Large-scale applicable purification and characterization of a membrane-bound PQQ-dependent aldose dehydrogenase

AU - Smolander, Maria

AU - Buchert, Johanna

AU - Viikari, Liisa

PY - 1993

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AB - 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.

U2 - 10.1016/0168-1656(93)90060-Z

DO - 10.1016/0168-1656(93)90060-Z

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