EC Number   |
Protein Variants |
Reference |
|---|
   1.11.1.14 | A140G/A243R/A317P |
kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value |
687879 |
| 1.11.1.14 | A140G/S190P/P193A/S196F/E208Q |
the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value |
687889 |
| 1.11.1.14 | A55R/N156E/H239E |
site-directed mutagenesis the triple mutant of LiPH8 with 2 additional saltbridges on the solvent-exposed regions shows excellent stability and oxidation activity under extremely acidic conditions down to pH 2.6. The stabilized mutant shows higher activity levels at all three pH levels tested, as compared to wild-type, with the highest activity at pH 2.6. Increased conversion of lignin dimer, convertion of 96.1% and 45.3% of the dimer at pH 2.6 and pH 5.0, respectively |
764353 |
| 1.11.1.14 | A55R/N156E/H239E |
site-directed mutagenesis, a rationally designed variant, that demonstrates a 12.5fold increased half-life under extremely acidic conditions, 9.9fold increased catalytic efficiency toward veratryl alcohol, and a 7.8fold enhanced lignin model dimer conversion efficiency compared to those of native LiPH8. The mutant has two constructed salt bridges. See for structure: PDB ID 6A6Q. Introduction of strong ionic salt bridges based on computational design results in a LiPH8 variant with markedly improved stability, as well as higher activity under acidic pH conditions |
764351 |
| 1.11.1.14 | H102T/S119R/N120T/Q126K/A243R/A315G |
kcat/Km for 2,4-dichlorophenol is fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value |
687879 |
| 1.11.1.14 | more |
design of active LiPH8 variants for increased stability in intensively acidic environments. Introduction of new strong salt bridges at effective locations and optimized interactions between charged residues and their environments are vital for active and stable LiP at acidic pH. Molecular dynamics (MD) simulation of the solvated structure under the desired conditions and calculating the Gibbs free energy of the variant are used for creating an acid-stable LiP variant, followed by protein X-ray crystallography |
764351 |
| 1.11.1.14 | more |
engineering of lignin peroxidase isozyme H8 and other enzymes involved in lignin depolymerization including targeting stability at low pH. Catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product |
764353 |
| 1.11.1.14 | more |
enzyme LiP obtained from a wild isolate of Phanerochaete chrysosporium immobilized on polyurethane foam cubes is purified 21fold using ammonium sulfate precipitation and size exclusion chromatography. The enzyme with a molecular mass of 55 kDa exhibited a considerably higher pH tolerance and thermostability compared with the native enzyme. It shows a strong affinity for the substrate veratryl alcohol and has kinetic constant values of 142.86 micromol and 0.065 mM. inhibited the activity, while ethanol, EDTA, Cu2+, Mn+, Na+, and Fe2+ exhibited induction. Purified LiP completely decolorizes (100%) bromophenyl blue, bromothymol blue, and bromocresol green. The 96% and 72% degradation obtained with phenol and Congo red is also higher compared to crude LiP. Treatment with LiP shows reduction in acid detergent lignin (ADL) as compared to untreated straws, with a maximum of 2.87 units obtained in jowar followed by 2.66 units in paddy straw. The digestibility of all straws increased, the response varying from a maximum of 21.27 units in proso millet to a minimum of 12.32 units obtained in little millet. The enzyme from immobilized organism exhibits an enhanced pH stability compared with the native enzyme obtained in the submerged cultures. It retains over 75% of activity at pH 6.5 for over 15 min |
764314 |
| 1.11.1.14 | more |
fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview |
-, 764590 |
| 1.11.1.14 | more |
improving the thermostability of LiP in acidic environments is required for effective lignin depolymerization in practical applications |
764611 |
