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Table 3 Apparent kinetic constants of recombinant and wild-type Glomerella cingulata GDH for either D-glucose or D-xylose as substrate, with the concentration of the electron acceptor ferrocenium ion held constant at 20 μM.

From: Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris

Substrate and pH

enzyme

Km

(mM)

kcat

(s-1)

kcat/Km

(M-1 s-1)

Glucose, pH = 5.5

wt

10.2 ± 0.2

180 ± 3

17.6 × 103

 

rec

10.1 ± 0.4

179 ± 4

17.7 × 103

Glucose, pH = 7.5

wt

19.0 ± 0.3

380 ± 6

20.0 × 103

 

rec

17.1 ± 0.7

418 ± 4

24.5 × 103

Xylose, pH = 5.5

wt

21 ± 0.6

40 ± 1.5

1.90 × 103

 

rec

26 ± 2.7

53 ± 1.9

2 × 103

Xylose, pH = 7.5

wt

24 ± 1.5

60 ± 2

2.5 × 103

 

rec

23 ± 0.7

61 ± 1

2.7 × 103

  1. Kinetic data were determined at 30°C, the data for wild-type Gc GDH are from [10].