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 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. 

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 Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi

2014 ◽  
Vol 70 (12) ◽  
pp. 3253-3265 ◽  
Author(s):  
Elena Fernández-Fueyo ◽  
Sandra Acebes ◽  
Francisco J. Ruiz-Dueñas ◽  
María Jesús Martínez ◽  
Antonio Romero ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electron Transfer ◽  
Manganese Peroxidase ◽  
Catalytic Properties ◽  
Substrate Oxidation ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ceriporiopsis Subvermispora ◽  
Ligninolytic Fungi ◽  
Access Channel

The genome ofCeriporiopsis subvermisporaincludes 13 manganese peroxidase (MnP) genes representative of the three subfamilies described in ligninolytic fungi, which share an Mn2+-oxidation site and have varying lengths of the C-terminal tail. Short, long and extralong MnPs were heterologously expressed and biochemically characterized, and the first structure of an extralong MnP was solved. Its C-terminal tail surrounds the haem-propionate access channel, contributing to Mn2+oxidation by the internal propionate, but prevents the oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), which is only oxidized by short MnPs and by shortened-tail variants from site-directed mutagenesis. The tail, which is anchored by numerous contacts, not only affects the catalytic properties of long/extralong MnPs but is also associated with their high acidic stability. Cd2+binds at the Mn2+-oxidation site and competitively inhibits oxidation of both Mn2+and ABTS. Moreover, mutations blocking the haem-propionate channel prevent substrate oxidation. This agrees with molecular simulations that position ABTS at an electron-transfer distance from the haem propionates of anin silicoshortened-tail form, while it cannot reach this position in the extralong MnP crystal structure. Only small differences exist between the long and the extralong MnPs, which do not justify their classification as two different subfamilies, but they significantly differ from the short MnPs, with the presence/absence of the C-terminal tail extension being implicated in these differences.

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