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 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.

Comparative production of ligninolytic enzymes by Phanerochaete chrysosporium and Polyporus sanguineus

2009 ◽  
Vol 55 (12) ◽  
pp. 1397-1402 ◽  
Author(s):  
Paramjit Kaur Bajwa ◽  
Daljit Singh Arora
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Ligninolytic Enzymes ◽  
Culture Conditions ◽  
Malt Extract ◽  
Mineral Salts ◽  
Wide Range ◽  
Extract Medium ◽  
Malt Extract Medium

The aim of the present study was to compare the effect of a wide range of culture conditions on production of ligninolytic enzymes by Polyporus sanguineus and Phanerochaete chrysosporium . Lignin peroxidase production by P. sanguineus was comparable with that of P. chrysosporium, although the culture conditions giving the highest yield varied greatly between the two fungi. Highest yield of manganese peroxidase by P. sanguineus obtained in 0.5% malt extract medium and peptone or malt extract supplemented mineral salts broth could not be surpassed by P. chrysosporium in any of the optimization experiments. In addition to lignin peroxidase and manganese peroxidase, P. sanguineus also produced laccase, which was best expressed in malt extract medium supplemented with sugarcane bagasse.

scholarly journals Homologous Expression of Recombinant Lignin Peroxidase in Phanerochaete chrysosporium

1999 ◽  
Vol 65 (4) ◽  
pp. 1670-1674 ◽  
Author(s):  
Maarten D. Sollewijn Gelpke ◽  
Mary Mayfield-Gambill ◽  
Geoffrey P. Lin Cereghino ◽  
Michael H. Gold
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Active Form ◽  
Schizophyllum Commune ◽  
Transient State ◽  
Veratryl Alcohol ◽  
Kinetic Properties ◽  
Gene Encoding ◽  
Homologous Expression ◽  
State Kinetic

ABSTRACT The glyceraldehyde-3-phosphate dehydrogenase (gpd) promoter was used to drive expression of lip2, the gene encoding lignin peroxidase (LiP) isozyme H8, in primary metabolic cultures of Phanerochaete chrysosporium. The expression vector, pUGL, also contained the Schizophyllum commune ura1gene as a selectable marker. pUGL was used to transform a P. chrysosporium Ura11 auxotroph to prototrophy. Ura+transformants were screened for peroxidase activity in liquid cultures containing high-carbon and high-nitrogen medium. Recombinant LiP (rLiP) was secreted in active form by the transformants after 4 days of growth, whereas endogenous lip genes were not expressed under these conditions. Approximately 2 mg of homogeneous rLiP/liter was obtained after purification. The molecular mass, pI, and optical absorption spectrum of rLiPH8 were essentially identical to those of the wild-type LiPh8 (wt LiPH8), indicating that heme insertion, folding, and secretion functioned normally in the transformant. Steady-state and transient-state kinetic properties for the oxidation of veratryl alcohol between wtLiPH8 and rLiPH8 were also identical.

High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium

2014 ◽  
Vol 98 (22) ◽  
pp. 9283-9294 ◽  
Author(s):  
Nancy Coconi-Linares ◽  
Denis Magaña-Ortíz ◽  
Doralinda A. Guzmán-Ortiz ◽  
Francisco Fernández ◽  
Achim M. Loske ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Versatile Peroxidase ◽  
High Yield ◽  
Yield Production ◽  
High Yield Production
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