Decolorization of Azo, Triphenyl Methane, Heterocyclic, and Polymeric Dyes by Lignin Peroxidase Isoenzymes from Phanerochaete chrysosporium

Abstract

The ligninolytic enzyme system of Phanerochaete chrysosporium decolorizes several recalcitrant dyes. Three isolated lignin peroxidase isoenzymes (LiP 4.65, LiP 4.15, and LiP 3.85) were compared as decolorizers with the crude enzyme system from the culture medium. LiP 4.65 (H2), LiP 4.15 (H7), and LiP 3.85 (118) were purified by chromatofocusing, and their kinetic parameters were found to be similar. Ten different types of dyes, including azo, triphenyl methane, heterocyclic, and polymeric dyes, were treated by the crude enzyme preparation. Most of the dyes lost over 75% of their color, only Congo red, Poly R-478, and Poly T-128 were decolorized less than the others, 54, 46, and 48%, respectively. Five different dyes were tested for decolorization by the three purified isoenzymes. The ability of the isoenzymes to decolorize the dyes in the presence of veratryl alcohol was generally comparable to that of the crude enzyme preparation, suggesting that lignin peroxidase plays a major role in the decolorization and that manganese peroxidase is not required to start the degradation of these dyes. In the absence of veratryl alcohol, the decolorization activity of the isoenzymes was in most cases dramatically reduced. However, LiP 3.85 was still able to decolorize 20%o of methylene blue and methyl orange and as much as 60% of toluidine blue 0, suggesting that at least some dyes can function as substrates for isoenzyme LiP 3.85 but not to the same extent for LiP 4.15 or LiP 4.65. Thus, the isoenzymes have different specificities towards dyes as substrates.

Lignin peroxidase functionalities and prospective applications

“…Studies on the applications of fungi and bacteria in dye abasement abound (Kumar & Sumangala, 2011;Shah, Patel, Nair, & Darji, 2013;Singh & Pakshirajan, 2010;Singh, Singh, & Singh, 2014), however, little attention has been given to the oxidative extracellular enzymes as an independent acting entity, thus, against this backdrop Ollikka et al (1993) investigated the ability of some lignin peroxidase isozymes, isolated from P. chrysosporium, to decolourize azo, triphenyl methane, heterocyclic, and polymeric dyes in comparison with crude enzyme.…”

Removal of estrogenic activity of 4‐tert‐octylphenol by ligninolytic enzymes from white rot fungi

“…Great interest has been currently expressed in lignindegrading white rot fungi and their ligninolytic enzymes due to the recognized potential for degrading and detoxifying recalcitrant environmental pollutants such as dioxins (Bumpus et al, 1985), chlorophenols (Joshi and Gold, 1993), polycyclic aromatic hydrocarbons (Bezale et al, 1996;Collins et al, 1996), and dyes (Ollikka et al, 1993). Manganese peroxidase (MnP), laccase, and lignin peroxidase (LiP) produced extracellularly by white rot fungi are involved in the degradation of lignin, and have been shown to degrade these pollutants.…”

Potential for Bioremediation of Xenobiotic Compounds by the White‐Rot Fungus Phanerochaete chrysosporium

“…Lignin peroxidase compound I oxidized azo dyes and was converted to compound 11, which was then reduced by veratryl alcohol to help complete the catalytic cycle of the enzyme. Ollikka et al (1993) found that dyes belonging to four different groups-polymeric, azo, heterocyclic, and triphenylmethane-were decolorized by three major lignin peroxidase isoenzymes (H2, H7, and H8). Although purified enzymes decolorized all dyes investigated, with isoenzymes veratryl alcohol was required for decolorization in some cases, but not in others (Ollikka et al, 1993).…”

“…Ollikka et al (1993) found that dyes belonging to four different groups-polymeric, azo, heterocyclic, and triphenylmethane-were decolorized by three major lignin peroxidase isoenzymes (H2, H7, and H8). Although purified enzymes decolorized all dyes investigated, with isoenzymes veratryl alcohol was required for decolorization in some cases, but not in others (Ollikka et al, 1993). We have now elucidated some of the major chemical steps involved in the degradation of azo dyes by lignin peroxidases and manganese peroxidases (Goszczynski et al, 1994;Pasti-Grigsby et al, 1994a), as shown in Figure 4.…”