Table 1 Kinetic parameters of the wild-type PUL and the truncated mutants.

From: Disorder prediction-based construct optimization improves activity and catalytic efficiency of Bacillus naganoensis pullulanase

Enzyme

Km(mg·mL−1)

kcat (s−1)

Vmax (μmol·mg−1min−1)

kcat/Km(mL·mg−1s−1)

PUL

6.07 ± 0.92

792.79 ± 43.50

468.13 ± 27.43

130.61 ± 24.31

PULΔN5

2.88 ± 0.61

854.09 ± 42.59

507.60 ± 25.29

296.56 ± 21.45

PULΔN22

1.46 ± 0.14

243.77 ± 4.18

147.90 ± 2.53

166.96 ± 7.94

PULΔN45

0.42 ± 0.03

202.70 ± 15.85

126.40 ± 10.72

482.61 ± 25.52

PULΔN64

3.71 ± 0.43

328.26 ± 23.74

208.90 ± 19.03

88.48 ± 10.22

PULΔN78

0.70 ± 0.01

230.47 ± 13.45

149.30 ± 8.78

329.24 ± 13.98

PULΔN106

4.33 ± 0.38

757.36 ± 38.13

507.80 ± 30.87

174.91 ± 21.39

PULΔC9

3.14 ± 0.32

598.07 ± 33.25

357.00 ± 10.09

190.47 ± 25.51

PULΔC36

2.20 ± 0.01

183.42 ± 2.27

112.50 ± 1.39

83.37 ± 0.77

  1. The values were obtained by fitting the initial rate data to the Michaelis-Menten equation using nonlinear regression with GraphPad Prism software. Values are means ± standard deviations.
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