Color removal ability of Phanerochaete chrysosporium in relation to lignin peroxidase and manganese peroxidase produced in molasses wastewater

2004 ◽  
Vol 20 (8) ◽  
pp. 859-864 ◽  
Author(s):  
F. Vahabzadeh ◽  
M. Mehranian ◽  
A.R. Saatari
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Color Removal ◽  
Molasses Wastewater

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.

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.

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

scholarly journals Erratum to: High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium

2014 ◽  
Vol 98 (22) ◽  
pp. 9519-9519
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

scholarly journals Lignolytic Enzymes of a Mushroom Stereum ostrea Isolated from Wood Logs

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
K. Praveen ◽  
B. Viswanath ◽  
K. Y. Usha ◽  
H. Pallavi ◽  
G. Venkata Subba Reddy ◽  
...  
Keyword(s):  
Liquid Medium ◽  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Vegetative Growth ◽  
Manganese Peroxidase ◽  
Time Interval ◽  
Production Time ◽  
Lignolytic Enzymes ◽  
Culture Growth ◽  
Laccase Enzyme

Production of lignolytic enzymes by the mushroom fungus Stereum ostrea in liquid medium under conditions of vegetative growth was examined for 10 days in comparison to the reference culture Phanerochaete chrysosporium. Though growth and secretion of extracellular protein by S. ostrea were comparable to those of P. chrysosporium, yields of laccase enzyme by S. ostrea were higher than laccase titres of P. chrysosporium by more than 2 folds on the peak production time interval (IVth day of incubation). S. ostrea yielded titres of 25 units of laccase/ml as against 8.9 units of laccase/ml on the IVth day of incubation. Stereum ostrea also exhibited activities of other lignolytic enzymes, lignin peroxidase (LiP) and manganese peroxidase (MnP), higher than the reference culture. Growth of S. ostrea on the medium in the presence of Remazol orange 16 resulted in the decolourisation of dye, confirming the presence of lignolytic enzymes. S. ostrea appears to be a promising culture with complete lignolytic system.

Synchronous extraction of lignin peroxidase and manganese peroxidase from Phanerochaete chrysosporium fermentation broth

2014 ◽  
Vol 123 ◽  
pp. 164-170 ◽  
Author(s):  
Xin Peng ◽  
Xing-zhong Yuan ◽  
Guang-ming Zeng ◽  
Hua-jun Huang ◽  
Hou Wang ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Fermentation Broth
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