Purification and characterisation of PQQ-dependent glucose dehydrogenase from Erwinia sp. 34-1
A pyrroloquinoline quinone-dependent glucose dehydrogenase from an isolate of Erwinia sp. has been purified to homogeneity and characterised. SDS-PAGE showed a single band of 88.4 kDa. The enzyme activity was optimal at 47°C and pH 7.5-8.5. The Michaelis constants for d-glucose and PMS were 3.2 mM a...
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Veröffentlicht in: | Biotechnology letters 1999-03, Vol.21 (3), p.187-192 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A pyrroloquinoline quinone-dependent glucose dehydrogenase from an isolate of Erwinia sp. has been purified to homogeneity and characterised. SDS-PAGE showed a single band of 88.4 kDa. The enzyme activity was optimal at 47°C and pH 7.5-8.5. The Michaelis constants for d-glucose and PMS were 3.2 mM and 132 μM, respectively (50 mM glycine-NaOH, at pH 8.0).[PUBLICATION ABSTRACT] |
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ISSN: | 0141-5492 1573-6776 |
DOI: | 10.1023/A:1005499709935 |