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
Hauptverfasser: MARCINKEVICIENE, L, BACHMATOVA, I, SEMENAITE, R, RUDOMANSKIS, R, BRAZENAS, G, MESKIENE, R, MESKYS, R
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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]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005499709935