Molecular docking of oxidases from Pleurotus ostreatus and the activity of those produced by ARS 3526 strain grown in both, submerged and solid-state fermentations

Abstract

Pleurotus ostreatus is a basidiomycete fungus capable of producing oxidases involved in the degradation of lignin, such as laccase (Lac), manganese peroxidase (MnP), versatile peroxidase (VP), veratryl alcohol oxidase (VAO) and dye-decolorizing peroxidase (DyP). In this research, the molecular docking showed that the interaction between Mn-ion, ABTS or DMP ligand with the respective oxidases studied were strongly supported by exposed GLU and ASP charged residues H-bonded or hydrophobic-bonded, in most of the complexes, mainly GLU and ASP played a very important role in the union, especially in the presence of the Mn-ion. On the other hand, the growth and activity of such enzymes of Pleurotus ostreatus ARS 3526 grown in both, submerged fermentation (SmF) and solid-state fermentation (SSF) were evaluated. The specific growth rate in SSF was 2.5 times higher than in SmF. The values of activity of Lac, VP and DyP were higher in the SSF, of the VAO activity was similar in both fermentation systems and SmF had the higher MnP activity value in comparison with SSF. This study provides evidence of the enzymatic potential of this fungus and shows the similarities in charged amino acids when used in their catalytic interactions, and the intimate relationship between the enzyme and its substrate.