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Table 2 Kinetic parameters derived from progress curves of initial BMCC hydrolysis: association (kon), catalytic (kcat), and dissociation (koff) rate constants, and apparent processivity number (n)

From: Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Enzyme

kon (g−1 L s−1)

kcat (s−1)

koff (s−1)

n

TreCel7A

0.0055 ± 0.0002

4 ± 0.2

0.0066 ± 0.0005

89 ± 5

TreCel7A_CD

0.0034 ± 0.0005

4.9 ± 0.7

0.0049 ± 0.0012

88 ± 5

ThaCel7A

0.0056 ± 0.0002

4.8 ± 0.4

0.0061 ± 0.0002

74 ± 1

TatCel7A

0.0071 ± 0.0001

8.3 ± 0.3

0.0071 ± 0.0001

97 ± 1

TatCel7A_CD

0.0044 ± 0

6.8 ± 0.3

0.0066 ± 0.0002

87 ± 3

  1. These parameters were derived for the 0–200 s pre-steady-state time interval. The substrate load was 3.3 g/L, and the enzyme concentration was 50 nM
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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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