Peroxidase of Trametes hirsuta LE-BIN 072: Purification, Characteristics, and Application for Dye Decolorization

Abstract Lignin peroxidase ( LiP9 ) from the basidiomycete Trametes hirsuta LE-BIN 072, an effective lignin destructor, was purified to a homogeneous state (with an RZ purity index of 1.8) and characterized for the first time. The molecular weight of LiP9 was 43 kDa and its pI was 3.2. The enzyme showed the highest activity at pH 2.5 and 35°C when veratryl alcohol was used as a substrate. The analysis of the substrate specificity showed that LiP9 oxidized phenol derivatives much faster than those of benzoic and cinnamic acids with the same substituents in the benzene ring. The highest specific activity of the enzyme was observed for catechol oxidation. The ability of LiP9 to decolorize recalcitrant dyes (reactive black 5, congo red, remazol brilliant blue R, phenol red, indigo carmine, and bromocresol green) was assessed. The highest decolorization efficiency was shown for indigo carmine (in the presence of veratryl alcohol) and bromocresol green (directly) up to 80 and 60%, respectively, in 1 hour.