Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete

Abstract

Irpex lacteus F17 is well-known for its ability to degrade recalcitrant aromatic pollutants, which mainly results from the action of the manganese peroxidase (MnP) that it is able to produce. Recently, the genome sequencing and annotation of this strain provided comprehensive picture of the ligninolytic peroxidase gene family. In addition to revealing the presence of 13 MnPs, genes for five dye-decolorizing peroxidases (DyPs) were also discovered in the I. lacteus F17 genome, which are unrelated to the fungal class II peroxidases. In the present study, amino acid sequences of five DyPs and 13 MnPs, representing two different families of heme peroxidases, were analyzed. Of these, two enzymes, a DyP (Il-DyP4) and a MnP (Il-MnP6) were expressed respectively in Escherichia coli, and were characterized by comparing their molecular models, substrate specificities, and catalytic features. The results showed that Il-DyP4 possessed a higher catalytic efficiency for some representative substrates, and a stronger decolorizing ability to a wide range of synthetic dyes in acidic conditions. Based on electrochemical measurements, Il-DyP4 was found to have a high redox potential of 27 mV at pH 3.5, which was superior to that of Il-MnP6 (− 75 mV), thereby contributing to its ability to oxidize high redox potential substrates, such as veratryl alcohol and polymeric dye Poly R-478. The results highlighted the potential of Il-DyP4 for use in industrial and environmental applications.Electronic supplementary materialThe online version of this article (10.1186/s13568-018-0648-6) contains supplementary material, which is available to authorized users.

A DyP-Type Peroxidase of Pleurotus sapidus with Alkene Cleaving Activity

“…This result fits the prediction of a Mn 2+ oxidation site. Only a few fungal DyPs are known to catalyze the oxidation of Mn 2+ [24,27,30,31]. Calculation of kinetic constants (Table 1) showed that the catalytic efficiency of PsaPOX towards Mn 2+ was similar to the one of Pleos-DyP1 from P. ostreatus and Ftr-DyP from Funalia trogii [24,27].…”

“…Furthermore, Trp-405 was identified as a homolog to the surface exposed Trp-377 of AauDyP of Auricularia auricula-judae, which serves as an oxidation site for bulky substrates such as Reactive blue 19 (RBB19) using a long-range electron transfer [29]. Comparison of the PsaPOX and Pleos-DyP4 sequence indicated that PsaPOX exhibited a non-canonical Mn 2+ -oxidation site on its surface (Asp-215, Glu-345, Asp-352 and Asp-354; Trp-339 participates in the electron transport from the oxidation site to the heme) like Pleos-DyP4 [28] and can oxidize Mn 2+ to Mn 3+ , which is known for a few fungal DyPs only [24,27,30,31].…”

Biochemical features of dye‐decolorizing peroxidases: Current impact on lignin degradation

“…Substrates tested include a variety of aromatic compounds classified as dyes [50,[53][54][55][56], beta-carotene [57], and aromatic sulfides [48]; some of which are poorly metabolized by other heme peroxidases. Numerous studies have shown that DyPs play a key role in the degradation of lignin [54,55,[58][59][60][61][62][63][64][65]. Their catalytic properties make them very interesting because the bacterial enzymes can be easily engineered, heterologously expressed in E. coli and purified [65] avoiding the issues of using a eukaryotic hosts.…”

Decolorization and Detoxification of Triphenylmethane Dyes by isolated endophytic fungus, Bjerkandera adusta SWUSI4 under non-nutritive conditions

“…Generally, the relative contributions of LiP, MnP and Lac to the decolorization of dyes may be different for each fungus (Srinivasan and Viraraghavan 2010;Wang et al 2017). Previously, Phanerochaete chrysosporium have been reported as Lip producers able to decolorize CV (Bumpus and Brock 1988), Irpex lacteus as Mnp producers able to decolorize MG (Yang et al 2016;Duan et al 2018), Pleurotus ostreatus as Lac producers able to decolorize MG and CV (Morales-Álvarez et al 2018) and Coriolopsis sp. as Lip and NADH-DCIP reductase producers able to decolorize CV, MV and CB, MG, respectively (Chen and Ting 2015b).…”