EC Number   |
Organic Solvent |
Reference |
|---|
   1.10.3.2 | 1,4-dioxan |
complete inhibition at 50% or above |
726355 |
| 1.10.3.2 | 1-propanol |
9% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain |
-, 742374 |
| 1.10.3.2 | Acetone |
10% (v/v), the enzyme retains more than 89.68% activity |
-, 764373 |
| 1.10.3.2 | Acetone |
10% v/v, 10°C, 1 h, 100% of activity remains |
743577 |
| 1.10.3.2 | Acetone |
20%, 75.9% residual activity after 16 h of preincubation |
764368 |
| 1.10.3.2 | Acetone |
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 27% loss of activity |
-, 742691 |
| 1.10.3.2 | Acetone |
complete inhibition at 50% or above |
726355 |
| 1.10.3.2 | Acetone |
retains high degree of activity |
655898 |
| 1.10.3.2 | Acetone |
rLac1 retains less than 20% activity in 50% v/v acetone after a 3 h incubation at 25°C |
-, 726411 |
| 1.10.3.2 | Acetone |
slight loss of activity at 10% v/v |
726416 |
