Lignin is an abundant aromatic biopolymer found in the lignocellulos component of the plant cell wall. The lignin peroxidase isozyme H8 from white-rot fungus Phanerochaete chrysosporium (PcLiP01) is one of the most widely studied isozymes which can degrade lignin via oxidative mechanisms. Denaturation caused by heat and pH is still a great issue in enzyme studies. Recently, it was observed that the melting temperatures rose in several single mutants of PcLiP01, especially in the V181A mutant model. A triple mutant (E40S/G86I/V181A) showed significant improvement in Tm in pH 3.0. It was conjectured that this effect would be attributed to the newly formed interactions between the heme and the mutated residues. In this study, we performed Molecular Dynamics (MD) simulations with both wild type (WT) and triple mutant (MT) PcLiP01. The stabilities of secondary structures which are related to the mutated residues were investigated during the simulation. Interactions around residue 181 indicated notable differences between WT and MT, which is consistent with experimental observation. These results demonstrate that the structural stability of lignin peroxidase is affected by the mutation of residues in secondary structures.

Molecular dynamics simulation studies of secondary structure stability in mutated lignin peroxidase

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