scholarly journals Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators

2005 ◽  
Vol 386 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Hisatoshi KAMITSUJI ◽  
Takashi WATANABE ◽  
Yoichi HONDA ◽  
Masaaki KUWAHARA
Keyword(s):  
Pleurotus Ostreatus ◽  
Manganese Peroxidase ◽  
Polymer Degradation ◽  
Veratryl Alcohol ◽  
Redox Mediators ◽  
Direct Oxidation ◽  
Peroxidase Isoenzyme ◽  
Pancreatic Rnase ◽  
Polymeric Substrates ◽  
Polymer Oxidation

VPs (versatile peroxidases) sharing the functions of LiP (lignin peroxidase) and MnP (manganese peroxidase) have been described in basidiomycetous fungi Pleurotus and Bjerkandera. Despite the importance of this enzyme in polymer degradation, its reactivity with polymeric substrates remains poorly understood. In the present study, we first report that, unlike LiP, VP from Pleurotus ostreatus directly oxidized two polymeric substrates, bovine pancreatic RNase and Poly R-478, through a long-range electron pathway without redox mediators. P. ostreatus produces several MnP isoenzymes, including the multifunctional enzyme MnP2 (VP) and a typical MnP isoenzyme MnP3. MnP2 (VP) depolymerized a polymeric azo dye, Poly R-478, to complete its catalytic cycle. Reduction of the oxidized intermediates of MnP2 (VP) to its resting state was also observed for RNase. RNase inhibited the oxidation of VA (veratryl alcohol) in a competitive manner. Blocking of the exposed tryptophan by N-bromosuccinimide inhibited the oxidation of RNase and VA by MnP2 (VP), but its Mn2+-oxidizing activity was retained, suggesting that Trp-170 exposed on an enzyme surface is a substrate-binding site both for VA and the polymeric substrates. The direct oxidation of RNase and Poly R by MnP2 (VP) is in sharp contrast with redox mediator-dependent oxidation of these polymers by LiP from Phanerochaete chrysosporium. Molecular modelling of MnP2 (VP) revealed that the differences in the dependence on redox mediators in polymer oxidation by MnP2 (VP) and LiP were explained by the anionic microenvironment surrounding the exposed tryptophan.

scholarly journals Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79

2009 ◽  
Vol 14 (8) ◽  
pp. 1153-1163 ◽  
Author(s):  
Maurizio Petruccioli ◽  
Marco Frasconi ◽  
Daniele Quaratino ◽  
Stefano Covino ◽  
Gabriele Favero ◽  
...  
Keyword(s):  
Manganese Peroxidase ◽  
Redox Properties ◽  
Peroxidase Isoenzyme ◽  
Panus Tigrinus

scholarly journals The Influence of Inducers on the Coltricia cinnamomea Laccase Activity and its Ability to Degrade POME

2021 ◽  
Vol 13 (2) ◽  
pp. 243-249
Author(s):  
Yohanes Bernard Subowo ◽  
Arwan Sugiharto
Keyword(s):  
Palm Oil ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Laccase Activity ◽  
Ligninolytic Enzymes ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Growth Media ◽  
Palm Oil Mill ◽  
Low Activity

Some species of Basidiomycetes, specifically white rot groups, produce three ligninolytic enzymes, namely, Lignin Peroxidase (LiP), Manganese Peroxidase (MnP) and Laccase (Lac), which have low activity in degrading Palm Oil Mill Effluent (POME). The research objective was to obtain the data on the ability of the Coltricia cinnamomea to produce LiP, MnP, and Lac enzymes to degrade POME. This research also studied the effect of sucrose, alcohol, veratryl alcohol, CuSO4 and ZnSO4,as inducers. Isolates of Coltricia cinnamomea, which were stored in a PDA media at -20℃ were obtained from the Microbiology section of the Research Center for Biology (LIPI). Furthermore, the growth media used were DM, Bean sprout Extract (TE) and PDB. The result indicated that PDB is the most suitable growth media for the production of ligninolytic enzymes, because in this medium these enzymes showed the highest activity. It was also observed that sucrose increased the laccase activity by 40.80%. Furthermore, Coltricia cinnamomea was able to reduce the concentration of Poly R-478 by 60.74%, after the addition of ZnSO4. In addition, it degraded and decreased the color and COD of POME, by 72.63% and 91.19% respectively, after the addition of veratryl alcohol, and incubation for 10 days. Therefore, this fungus can be used to degrade POME in order to prevent environmental pollution. Coltricia cinnamomea has not been used for POME degradation. By using Coltricia cinnamomea, we  obtained new data regarding the activity of laccase and its ability to degrade POME. 

A new versatile peroxidase from Pleurotus

2001 ◽  
Vol 29 (2) ◽  
pp. 116-122 ◽  
Author(s):  
F. J. Ruiz-Dueñas ◽  
S. Camarero ◽  
M. Pérez-Boada ◽  
M. J. Martínez ◽  
A. T. Martínez
Keyword(s):  
Electron Transfer ◽  
Chemical Modification ◽  
Binding Site ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Veratryl Alcohol ◽  
Substrate Oxidation ◽  
Molecular Models ◽  
Electron Transfer Pathway ◽  
High Affinity

Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanero-chaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn2+, hydro-quinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn2+-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn2+-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.

scholarly journals Influence of cellobiose oxidase on peroxidases from Phanerochaete chrysosporium

1993 ◽  
Vol 293 (2) ◽  
pp. 431-435 ◽  
Author(s):  
P Ander ◽  
G Sena-Martins ◽  
J C Duarte
Keyword(s):  
Cytochrome C ◽  
Horseradish Peroxidase ◽  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Veratryl Alcohol ◽  
Lag Phase ◽  
And Function ◽  
Compound Ii ◽  
Catalytic Cycles

Reduction of H2O2-oxidized manganese peroxidase (MnP), lignin peroxidase and, to some extent, horseradish peroxidase, was studied in the presence of cellobiose oxidase (CbO) and cellobiose. It was found that the reversion rates for MnP compound II and lignin peroxidase compound II back to native enzymes increased significantly in the presence of CbO and cellobiose. However, the reduction of cytochrome c by CbO plus cellobiose was 40 times faster than the reduction of MnP compound II. Also, the lag phase before reversion to the native states decreased for all three peroxidases in the presence of CbO and cellobiose. Active CbO did not repress formation of compounds I or II of the peroxidases, and Mn2+/veratryl alcohol reduced compound II of the peroxidases much more rapidly than did active CbO. This indicates that, in the presence of Mn2+ or veratryl alcohol, MnP and lignin peroxidase can complete their catalytic cycles and function normally without interference from CbO. Without the presence of peroxidase substrates, active CbO reduced compound II of the above peroxidases.

scholarly journals Screening of cellulose- and lignin-degrading fungi for improving nutritive quality of ruminant feed

2018 ◽  
Vol 197 ◽  
pp. 06001
Author(s):  
Muhammad Fauzi ◽  
Nisa Rachmania Mubarik ◽  
Anuraga Jayanegara
Keyword(s):  
Rice Straw ◽  
Phanerochaete Chrysosporium ◽  
Pleurotus Ostreatus ◽  
Manganese Peroxidase ◽  
Ganoderma Lucidum ◽  
Fungal Species ◽  
Potato Dextrose Broth ◽  
Nutritive Quality ◽  
Ruminant Feed

This experiment aimed to screen some cellulose- and lignin-degrading fungal species for improving nutritive quality of ruminant feed. Fungal species used were Ganoderma lucidum, Pleurotus ostreatus, Phanerochaete chrysosporium, and Trametes visicolor. These fungal species were grown on Potato Dextrose Broth (PDB) medium that added with 0.5 g substrate, i.e. either rice straw, rice bran or carboxymethyl cellulose for 12 days at room temperature. Harvesting was performed in order to separate fungal mycelium and supernatant that contained crude cellulase enzyme. Among the fungi observed, Ganoderma lucidum had the highest cellulase activity, i.e. 4.02 U/mg. Cellulase activities of Pleurotus ostreatus, Phanerochaete chrysosporium, and Trametes visicolor were 1.53, 1.08, and 0.13 U/mg, respectively. Ganoderma lucidum was further investigated for its ligninolytic enzyme activity, i.e. laccase and manganese peroxidase. It was observed that the fungi had laccase and manganese peroxidase activities of 368.95 and 33.89 U/mL, respectively. Crude enzymes of Ganoderma lucidum that contain cellulase, laccase and manganese peroxidase were further used to increase nutritive quality of rice straw and subjected to in vitro incubation with rumen fluid of cattle.

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