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