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Table 1 Activity value of wild type rCelStrep and mutants, nucleotide and aminoacid substitutions in rCelStrep variants

From: Directed evolution of the bacterial endo-β-1,4-glucanase from Streptomyces sp. G12 towards improved catalysts for lignocellulose conversion

  mU/mL mU/OD600 Nucleotide substitution Aminoacid substitution
CelStrep wild type 70.4 ± 10.8 984.6 ± 52.3
epCelStrep_1 (epCS_1) 103.8 ± 0.3 1222.2 ± 94.2 G898T, G1031A G263C; R307H
epCelStrep_2 (epCS_2) 88.6 ± 8.5 1711.9 ± 456.4 G49A, G545A, T732A, G858A, C986A, C1131A G145D; N207K
epCelStrep_3 (epCS_3) 112.6 ± 6.7 3295.2 ± 202.1 C411T, T687C, C794G, G857A, G954T, G1060A, C1130T P228R
epCelStrep_4 (epCS_4) 89.1 ± 6.6 1095.1 ± 44.9 C311A, T537G, G808A, A828G, T836A, T1101A T67N; D142E; S218N; V242D; D330E
epCelStrep_5 (epCS_5) 102.9 ± 0.2 2073.3 ± 689.1 C363T, C581T, G863A, T887A T157I; G251D; V259D
  1. AZO-CMCase activity levels of the CelStrep wild type and of the five evolved enzymes expressed as mU/mL and normalized to OD600nm. The enzymes were assessed for the endoglucanase activity in liquid medium in the presence of 1% CMC at 50 °C. Experiments were performed in triplicate. Nucleotide and aminoacid substitutions in the selected rCelStrep variants