Protein Variants | Comment | Organism |
---|---|---|
additional information | improving the thermostability of LiP in acidic environments is required for effective lignin depolymerization in practical applications | Phanerodontia chrysosporium |
S49C/A67C/H239E | site-directed mutagenesis, improved thermostability of the synthetic LiPH8 variant (PDB ID 6ISS) capable of strengthening the helix-loop interactions under acidic conditions. The mutant retains excellent thermostability at pH 2.5 with a 10fold increase in t1/2 (2.52 h at 25°C) compared with that of the wild-type enzyme. The recombinant LiPH8 variant is the only unique lignin peroxidase containing five disulfide bridges, and the helix-loop interactions of the synthetic disulfide bridge and ionic salt bridge in its structure are responsible for stabilizing the Ca2+-binding region and heme environment, resulting in an increase in overall structural resistance against acidic conditions | Phanerodontia chrysosporium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | P06181 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
lignin peroxidase | - |
Phanerodontia chrysosporium |
lignin peroxidase H8 | - |
Phanerodontia chrysosporium |
LIP | - |
Phanerodontia chrysosporium |
LiPH8 | - |
Phanerodontia chrysosporium |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
an extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition. Native LiP under mild conditions with half-life (t1/2) of 8.2 days at pH 6.0 exhibits a marked decline in thermostability under acidic conditions with t1/2 of only 14 min at pH 2.5 | Phanerodontia chrysosporium |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Phanerodontia chrysosporium |