The main objective of this study was find the oxidizing lignin peroxidase from Basidiomycota. Thereafter, study on biosynthesis, purification and determination of physico-chemical properties as substrate specificity of the enzyme protein LiP from selected fungal strains. The next objective, using purified Lip enzyme combined with laccase to evaluate the ability to remove dyes belonging to Azo group and textile dyeing wastewater.

Theoretical results:
- From fungal strains (39 strains) were screened for LiP activity and selected Lentinus squarrosulus MPN12 and Pleurotus pulmonarius CPG6 strains with the highest enzyme biosynthesis ability, respectively 108.5 U/mL and 102.6 U/mL.
- The studied strains (L. squarrosulus MPN12) were fermented for 9 days on liquid medium supplemented with the inducer veratryl alcohol (0.3 g/L) carbon source from sucrose (10g/L), nitrogen source from urea (5 g/L) in 28oC, pH 5.0 under the condition of stirring at 200 rpm, LiP enzyme activity was 896 U/mL.
- LiP enzyme purified from P. pulmonarius CPG6 through 3 chromatographic columns has total enzyme protein 32 mg, specific activity 6.59 U/mg and efficiency 59% with purity 17.8 times, optimum pH was 3.0, optimum temperature was 30°C.
- Purified enzyme has substrate specificity and catalytic constant with veratryl alcohol: Km of LiP was 25 μM, catalytic rate (Kcat) of the reaction was 3.4 s-1, catalytic efficiency