scholarly journals Glutathione S-transferases from the white-rot fungus, Phanerochaete chrysosporium

1997 ◽  
Vol 324 (1) ◽  
pp. 243-248 ◽  
Author(s):  
Caitriona A. DOWD ◽  
Catherine M. BUCKLEY ◽  
David SHEEHAN
Keyword(s):  
Molecular Mass ◽  
Phanerochaete Chrysosporium ◽  
Sequence Similarity ◽  
Gel Filtration ◽  
Preliminary Evidence ◽  
White Rot ◽  
White Rot Fungus ◽  
Glutathione S Transferase ◽  
Glutathione S Transferases ◽  
A Subunit

A glutathione S-transferase (GST) was purified to homogeneity from the white-rot fungus, Phanerochaete chrysosporium, by affinity chromatography on glutathione–agarose followed by Mono-Q ion-exchange FPLC. This protein immunoblotted with antisera to rat Theta class GST 5-5 and also showed N-terminal sequence similarity to the Theta class, including the presence of a conserved serine residue that has been specifically implicated in catalysis in this class [Wilce, Board, Feil and Parker (1995) EMBO J. 14, 2133–2143] and other residues conserved in plant sequences. Catalytic activity was found to be highly labile in the purified protein, although preliminary evidence for activity (approx. 120 m-units/mg) with 1,2-epoxy-3-(p-nitrophenoxy)propane was obtained in some preparations. The enzyme seems to be a dimer with a subunit molecular mass of 25 kDa by SDS/PAGE. The native molecular masses estimated by non-denaturing electrophoresis and by Superose-12 gel filtration were 58 and 45 kDa respectively. A second protein purified in this study also gave low level of activity with 1,2-epoxy-3-(p-nitrophenoxy)propane and had a subunit molecular mass of 28 kDa (native size 62–63 kDa), but did not immunoblot with any GST class and seemed to be N-terminally blocked.

scholarly journals Cloning and expression of a chick liver glutathione S-transferase CL 3 subunit with the use of a baculovirus expression system

1992 ◽  
Vol 281 (2) ◽  
pp. 545-551 ◽  
Author(s):  
L H Chang ◽  
J Y Fan ◽  
L F Liu ◽  
S P Tsai ◽  
M F Tam
Keyword(s):  
Specific Activity ◽  
Sequence Similarity ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Relative Activity ◽  
Cloning And Expression ◽  
Glutathione S Transferase ◽  
Sds Page ◽  
Glutathione S Transferases ◽  
A Subunit

Glutathione S-transferase CL 3 subunits purified from 1-day-old-chick livers were digested with Achromobacter proteinase I and the resulting fragments were isolated for amino acid sequence analysis. An oligonucleotide probe was constructed accordingly for cDNA library screening. A cDNA clone of 1342 bases, pGCL301, encoding a protein of 26209 Da was isolated and sequenced. Including conservative substitutions, this protein has 75-79% sequence similarity to other Alpha family glutathione S-transferases. The coding sequence of pGCL301 was inserted into a baculovirus vector for infection of Spodoptera frugiperda (SF9) cells. The expressed protein has a high relative activity with ethacrynic acid (47% of the specific activity with 1-chloro-2,4-dinitrobenzene). The enzyme has a subunit molecular mass of 25.2 +/- 1.2 kDa (by SDS/PAGE), a pI of 9.45 and an absorption coefficient A1%1cm of 13.0 +/- 0.5 at 280 nm.

The Effect of Heavy Metal-Induced Oxidative Stress on the Enzymes in White Rot Fungus Phanerochaete chrysosporium

2014 ◽  
Vol 175 (3) ◽  
pp. 1281-1293 ◽  
Author(s):  
Qihua Zhang ◽  
Guangming Zeng ◽  
Guiqiu Chen ◽  
Min Yan ◽  
Anwei Chen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heavy Metal ◽  
Phanerochaete Chrysosporium ◽  
White Rot ◽  
White Rot Fungus

Toxicity of carbon nanotubes to white rot fungus Phanerochaete chrysosporium

2018 ◽  
Vol 162 ◽  
pp. 225-234 ◽  
Author(s):  
Zhu Ming ◽  
Shicheng Feng ◽  
Ailimire Yilihamu ◽  
Shengnan Yang ◽  
Qiang Ma ◽  
...  
Keyword(s):  
Carbon Nanotubes ◽  
Phanerochaete Chrysosporium ◽  
White Rot ◽  
White Rot Fungus

scholarly journals Biodegradation of sago effluent by white-rot fungus Phanerochaete chrysosporium

2021 ◽  
Vol 11 (2) ◽  
pp. 91-99
Author(s):  
Vivekanandhan K. ◽  
Dr.M.P. Ayyappadas ◽  
Dr. S. K. Ayyappadas ◽  
R. Renugadevi, ◽  
M. Flory Shobana ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
White Rot ◽  
White Rot Fungus

scholarly journals Biotransformation of Pristine and Oxidized Carbon Nanotubes by the White Rot Fungus Phanerochaete chrysosporium

Nanomaterials ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 1340 ◽  
Author(s):  
Qiang Ma ◽  
Ailimire Yilihamu ◽  
Zhu Ming ◽  
Shengnan Yang ◽  
Mengyao Shi ◽  
...  
Keyword(s):  
Carbon Nanotubes ◽  
Multiwalled Carbon Nanotubes ◽  
Phanerochaete Chrysosporium ◽  
Environmental Remediation ◽  
Carbon Nanomaterials ◽  
Carbon Skeleton ◽  
White Rot ◽  
White Rot Fungus ◽  
Multiwalled Carbon ◽  
Complete Degradation

Carbon nanomaterials are widely studied and applied nowadays, with annual production increasing. After entering the environment, the complete degradation of these carbon nanomaterials by microorganisms is proposed as an effective approach for detoxification and remediation. In this study, we evaluated the degradation of pristine multiwalled carbon nanotubes (p-MWCNTs) and oxidized multiwalled carbon nanotubes (o-MWCNTs) by the white rot fungus Phanerochaete chrysosporium, which is a powerful decomposer in the carbon cycle and environmental remediation. Both p-MWCNTs and o-MWCNTs were partially oxidized by P. chrysosporium as indicated by the addition of oxygen atoms to the carbon skeleton in the forms of C=O and O–H bonds. The fungal oxidation led to the shortening of MWCNTs, where precipitated o-MWCNTs showed more short tubes. During the transformation, the defects on the tubes became detached from the carbon skeleton, resulting in decreases of the ID/IG (intensity of D-band/ intensity of G-band) values in Raman spectra. The transformation mechanism was attributed to the enzymatic degradation by laccase and manganese peroxidase excreted by P. chrysosporium. The results collectively indicated that MWCNTs could be transformed by P. chrysosporium, but complete degradation could not be achieved in a short time period. The implications on the environmental risks of carbon nanomaterials are discussed.

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