Isolation and Characterization of the Second Extracellular Peroxidase of the White-Rot Fungus Coriolus hirsutus

Mycologia ◽  
2000 ◽  
Vol 92 (6) ◽  
pp. 1057 ◽  
Author(s):  
Yeo Jin Lee ◽  
Kwang Soo Shin
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Extracellular Peroxidase ◽  
Isolation And Characterization ◽  
Coriolus Hirsutus

Isolation and characterization of novel pI 4.8 MnP isoenzyme from white-rot fungus Irpex lacteus

2010 ◽  
Vol 46 (7) ◽  
pp. 550-556 ◽  
Author(s):  
J. Sklenar ◽  
M.-L. Niku-Paavola ◽  
S. Santos ◽  
P. Man ◽  
K. Kruus ◽  
...  
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Irpex Lacteus ◽  
Isolation And Characterization

Isolation and characterization of a white rot fungus Bjerkandera sp. strain capable of oxidizing phenanthrene

2005 ◽  
Vol 27 (12) ◽  
pp. 845-851 ◽  
Author(s):  
Enrique Terrazas-Siles ◽  
Teresa Alvarez ◽  
Benoit Guieysse ◽  
Bo Mattiasson
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Isolation And Characterization

scholarly journals Induction, Isolation, and Characterization of Two Laccases from the White Rot Basidiomycete Coriolopsis rigida

2002 ◽  
Vol 68 (4) ◽  
pp. 1534-1540 ◽  
Author(s):  
Mario C. N. Saparrat ◽  
Francisco Guillén ◽  
Angélica M. Arambarri ◽  
Angel T. Martínez ◽  
María Jesús Martínez
Keyword(s):  
Phenolic Compounds ◽  
Contaminated Soils ◽  
Ligninolytic Enzyme ◽  
White Rot ◽  
White Rot Fungus ◽  
Phenol Red ◽  
Isolation And Characterization ◽  
Terminal Amino ◽  
Monomeric Proteins

ABSTRACT Previous work has shown that the white rot fungus Coriolopsis rigida degraded wheat straw lignin and both the aliphatic and aromatic fractions of crude oil from contaminated soils. To better understand these processes, we studied the enzymatic composition of the ligninolytic system of this fungus. Since laccase was the sole ligninolytic enzyme found, we paid attention to the oxidative capabilities of this enzyme that would allow its participation in the mentioned degradative processes. We purified two laccase isoenzymes to electrophoretic homogeneity from copper-induced cultures. Both enzymes are monomeric proteins, with the same molecular mass (66 kDa), isoelectric point (3.9), N-linked carbohydrate content (9%), pH optima of 3.0 on 2,6-dimethoxyphenol (DMP) and 2.5 on 2,2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), absorption spectrum, and N-terminal amino acid sequence. They oxidized 4-anisidine and numerous phenolic compounds, including methoxyphenols, hydroquinones, and lignin-derived aldehydes and acids. Phenol red, an unusual substrate of laccase due to its high redox potential, was also oxidized. The highest enzyme affinity and efficiency were obtained with ABTS and, among phenolic compounds, with 2,6-dimethoxyhydroquinone (DBQH2). The presence of ABTS in the laccase reaction expanded the substrate range of C. rigida laccases to nonphenolic compounds and that of MBQH2 extended the reactions catalyzed by these enzymes to the production of H2O2, the oxidation of Mn2+, the reduction of Fe3+, and the generation of hydroxyl radicals. These results confirm the participation of laccase in the production of oxygen free radicals, suggesting novel uses of this enzyme in degradative processes.

Characterization of ��-Glucosidase Produced by the White Rot Fungus Flammulina velutipes

2015 ◽  
Vol 25 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Julieta Mallerman ◽  
Leandro Papinutti ◽  
Laura Levin
Keyword(s):  
White Rot ◽  
Flammulina Velutipes ◽  
White Rot Fungus

scholarly journals Cloning and Characterization of a cDNA Encoding a Novel Extracellular Peroxidase from Trametes versicolor

1999 ◽  
Vol 65 (3) ◽  
pp. 1343-1347 ◽  
Author(s):  
Patrick J. Collins ◽  
Margaret M. O’Brien ◽  
Alan D. W. Dobson
Keyword(s):  
Trametes Versicolor ◽  
Cdna Sequence ◽  
White Rot ◽  
Transcript Levels ◽  
Extracellular Peroxidase ◽  
Low Concentrations ◽  
Lignin Peroxidases

ABSTRACT The white rot basidiomycete Trametes versicolorsecretes a large number of peroxidases which are believed to be involved in the degradation of polymeric lignin. These peroxidases have been classified previously as lignin peroxidases or manganese peroxidases (MnP). We have isolated a novel extracellular peroxidase-encoding cDNA sequence from T. versicolor CU1, the transcript levels of which are repressed by low concentrations of Mn2+ and induced by nitrogen and carbon but not induced in response to a range of stresses which have been reported to induce MnP expression.

scholarly journals Characterization of Acetylxylan Esterase from White-Rot Fungus Irpex lacteus

2019 ◽  
Vol 66 (4) ◽  
pp. 131-137
Author(s):  
Sangho Koh ◽  
Seika Imamura ◽  
Naoto Fujino ◽  
Masahiro Mizuno ◽  
Nobuaki Sato ◽  
...  
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Irpex Lacteus ◽  
Acetylxylan Esterase
Sign in / Sign up

Export Citation Format

Share Document