TABLE 1.
Physical characteristics for the set of enzymes selected for in silico structure-based surface analysis and biophysical characterization using QCM-D
Major bands are shown in bold and underlined.
| Protein | Organism | Domain architecture | pI | Molecular mass | SASAHphob | Hydrophobic patch score |
|---|---|---|---|---|---|---|
| kDa | % | |||||
| β-Glucosidase (Bgl1) | A. niger | GH3 | 4.2 | 93.3 (117.5)a | 53.0b | 45.9b |
| Serum albumin | Bovine | BSA | 4.6 | 66.5 | 60.5 | 34.9 |
| Cellobiohydrolase (Cel7A) | T. reesei | GH7-CBM1 | 4.3 | 54.1 | 59.1 | 13.3 |
| Acetyl xylan esterase (Axe1) | T. reesei | Axe1-CBM1 | 6.8, 6.9, 7.1, 7.4 | 30.8 | 70.7 | 9.1 |
| Endocellulase (E1) | A. cellulolyticus | GH5 | 5.2 | 40.1 | 60.1 | 7.7 |
| Endoxylanase (XynA) | T. lanuginosus | GH11 | 3.8, 4.0 | 24.4 | 54.1 | 2.7 |
| Arabinofuranosidase (AbfB) | A. niger | GH54 | 3.6, 3.8 | 52.5 | 57.0 | 1.9 |
| Endoxylanase (XynII) | T. reesei | GH11 | 9 | 24.2 | 54.6 | 0.8 |
a Molecular mass for Bgl1 shown in parentheses was determined by mass spectrometry. Molecular masses for Bgl1 are for the monomeric species.
b SASA calculations and hydrophobic patch score for Bgl1 are for the dimeric species.