Table 2.
Enzyme kinetic parameters of AmyK and oligopeptide fusion proteins
| Enzyme kinetic parametera | Value ± SD |
||||||
|---|---|---|---|---|---|---|---|
| AmyK | AmyK-p1 | AmyK-p2 | AmyK-p3 | AmyK-p4 | AmyK-p5 | AmyK-p6 | |
| Km (g/liter) | 9.2 ± 0.2 | 6.0 ± 0.2 | 5.9 ± 0.1 | 5.5 ± 0.4 | 6.2 ± 0.2 | 8.9 ± 0.3 | 6.1 ± 0.5 |
| Vmax (μmol/[ml·min]) | 37.8 ± 2.1 | 59.5 ± 1.1 | 26.3 ± 1.2 | 19.1 ± 0.9 | 27.6 ± 1.5 | 33.7 ± 2.2 | 23.9 ± 1.8 |
| kcat (·103 min−1) | 166.7 ± 2.3 | 582.8 ± 2.9 | 62.9 ± 1.7 | 33.8 ± 2.0 | 10.6 ± 1.5 | 24.1 ± 1.9 | 6.8 ± 1.1 |
| kcat/Km (·103 liter/[g·min]) | 18.1 ± 0.7 | 97.1 ± 3.9 | 10.7 ± 0.5 | 6.2 ± 0.8 | 1.7 ± 0.3 | 2.7 ± 0.3 | 1.1 ± 0.3 |
| Specific activity (·106 U/μmol) | 6.2 ± 0.8 | 25.5 ± 1.1 | 4.0 ± 0.5 | 2.1 ± 0.3 | 0.6 ± 0.1 | 1.3 ± 0.2 | 0.4 ± 0.1 |
a
Km, substrate dissociation constant; kcat, μmol dextrose equivalents per minute per μmol protein.