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. 2007 Jul 27;73(19):6098–6105. doi: 10.1128/AEM.01037-07

TABLE 3.

Catalytic propertiesa and other characteristics of EG1, rcCel9B, rcCel9BΔBTD, ClCBase, rcCel8B, and rcCel5H

Enzyme (reference) Km Vmax (U/mg) kcat (s−1) kcat/Km (ml/s · mg) Binding to cellulose Temp optimum (oC) pH optimum Divalent cation requirement
EG1 (28) 3.6 mg/ml 84 91 25.3 No 39 6.5 Yes
rcCel9B 9.20 ± 0.83 mg/ml 36.9 ± 1.46 39.79 ± 1.57 4.24 No 37 6.5 Yes
rcCel9BΔBTD 5.93 ± 0.78 mg/ml 47.8 ± 3.00 46.29 ± 2.91 7.80 No 37 6.5 Yes
rcCel5H 16.2 ± 1.91 mg/ml 0.31 ± 0.02 0.51 ± 0.03 0.031 Yes 37 6.5 No
rcCel8B 10.9 ± 1.25 mg/ml 1.08 ± 0.06 1.47 ± 0.08 0.14 No 42 7.0 No
ClCBase (14) 0.1 mM 14.2 15.9 159 Yes 45/37b 6.5 No
rcCel10A 0.36 ± 0.02 mM 11.6 ± 1.02 12.1 ± 1.06 33.6 Yes 37/37b 6.5 No
a

Substrates used: p-nitrophenyl cellobioside for native ClCBase and rcCel10A and CMC for the enzymes EG1, rcCel9B, rcCel9BΔBTD, rcCel5H, and rcCel8B.

b

With/without 0.2 M NaCl.