Kinetics of the Growth of White-Rot Fungus Coriolus hirsutus in Soil for Bioremediation

2008 ◽  
Vol 41 (2) ◽  
pp. 100-107 ◽  
Author(s):  
Katsuhiro Ueshima ◽  
Kazuhiro Asami ◽  
Kazuhisa Ohtaguchi
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Coriolus Hirsutus ◽  
Kinetics Of

Biotreatment of persistent substances using effective microorganisms

2000 ◽  
Vol 42 (12) ◽  
pp. 93-106 ◽  
Author(s):  
M. Fujita ◽  
M. Ike ◽  
Y. Kawagoshi ◽  
N. Miyata
Keyword(s):  
Polyvinyl Alcohol ◽  
Oxidative Degradation ◽  
White Rot ◽  
White Rot Fungus ◽  
Enzymatic Reactions ◽  
Degradation Mechanisms ◽  
Effective Microorganisms ◽  
Degradation Reactions ◽  
Coriolus Hirsutus ◽  
Degrading Bacteria

To efficiently biotreat the persistent substances contained in wastewater, it is necessary to fully elucidate the degradation mechanisms of the substances by specific degrading microorganisms. Especially clarifying the enzymatic reactions responsible for the degradation of persistent substances is very important. Here three different kinds of aerobic or oxidative degradation reactions of persistent substances are introduced. Polyvinyl alcohol (PVA) degradation by Pseudomonas vesicularis var. povalolyticus strain PH, co-oxidative degradation of trichloroethylene (TCE) by a variety of phenol degrading bacteria, and decolorization of melanoidin by a white rot fungus Coriolus hirsutus were shown.

scholarly journals Molecular Analysis of a Laccase Gene from the White Rot Fungus Pycnoporus cinnabarinus

1998 ◽  
Vol 64 (5) ◽  
pp. 1766-1772 ◽  
Author(s):  
Claudia Eggert ◽  
Peter R. LaFayette ◽  
Ulrike Temp ◽  
Karl-Erik L. Eriksson ◽  
Jeffrey F. D. Dean
Keyword(s):  
Genomic Sequence ◽  
Oxidation Potential ◽  
White Rot ◽  
White Rot Fungus ◽  
Coding Region ◽  
Pycnoporus Cinnabarinus ◽  
Eukaryotic Promoter ◽  
Coriolus Hirsutus ◽  
Type 1 Copper ◽  
Copper Center

ABSTRACT It was recently shown that the white rot basidiomycetePycnoporus cinnabarinus secretes an unusual set of phenoloxidases when it is grown under conditions that stimulate ligninolysis (C. Eggert, U. Temp, and K.-E. L. Eriksson, Appl. Environ. Microbiol. 62:1151–1158, 1996). In this report we describe the results of a cloning and structural analysis of the laccase-encoding gene (lcc3-1) expressed by P. cinnabarinus during growth under xylidine-induced conditions. The coding region of the genomic laccase sequence, which is preceded by the eukaryotic promoter elements TATA and CAATA, spans more than 2,390 bp. The corresponding laccase cDNA was identical to the genomic sequence except for 10 introns that were 50 to 60 bp long. A sequence analysis indicated that the P. cinnabarinus lcc3-1 product has a Phe residue at a position likely to influence the reduction-oxidation potential of the enzyme’s type 1 copper center. The P. cinnabarinus lcc3-1 sequence was most similar to the sequence encoding a laccase from Coriolus hirsutus (level of similarity, 84%).

scholarly journals Potential Degradation and Kinetics of Melanoidin by Using Laccase from White Rot Fungus

2020 ◽  
pp. 1-10
Author(s):  
Wittawat Toomsan ◽  
Pinthita Mungkarndee ◽  
Sophon Boonlue ◽  
Nguyen Thanh Giao ◽  
Sumana Siripattanakul-Ratpukdi
Keyword(s):  
Maximum Rate ◽  
Degradation Kinetics ◽  
Catalytic Efficiency ◽  
White Rot ◽  
White Rot Fungus ◽  
Carbonyl Groups ◽  
Michaelis Constant ◽  
Turnover Number ◽  
Rate Of Reaction ◽  
Kinetics Of

This study was attempted to use laccase extracted from white rot fungus to remove melanoidin in the ethanol production wastewater. The isolated fungus producing the highest laccase was identified as Megaspororia sp. The highest degradation efficiencies of the purified and crude laccases were 48.00% and 44.60%, respectively. Both degradation kinetics well fit Michaelis-Menten model. The Michaelis constant (Km) and maximum rate of reaction (Vmax) were 0.82% melanoidin and 0.0045% melanoidin h-1 for the degradation by the purified laccase and 0.71% melanoidin and 0.0037% melanoidin h-1 for the degradation by the crude laccase. Turnover number (Kcat) of purified and crude laccases were 0.00023 and 0.00019% melanoidin U-1 h-1, respectively. Catalytic efficiency (Kcat/Km) of purified and crude laccases were 0.00028 and 0.00027 U-1 h-1, respectively. The affinity of the crude laccase was slightly higher because of its non-specificity. Kcat and Kcat/Km of the purified laccase were higher than the crude laccase. Proposed potential degradation result showed that laccase could oxidize CH3, carbonyl groups, haloalkanes (C–H), C–O and C–N bondings which probably caused decolorization of melanoidin in wastewater. Thus, the purified and crude laccases can be used to decolorize melanoidin-containing wastewater from ethanol industries. As the attempt to use purified laccase consumed times and costs especially in purification steps, the crude laccase can be used to degrade color of melanoidin in wastewater with only 3.4% lower than the purified laccase.

Metabolization and degradation kinetics of the urban-use pesticide fipronil by white rot fungus Trametes versicolor

2016 ◽  
Vol 18 (10) ◽  
pp. 1256-1265 ◽  
Author(s):  
Jordyn M. Wolfand ◽  
Gregory H. LeFevre ◽  
Richard G. Luthy
Keyword(s):  
Trametes Versicolor ◽  
Degradation Kinetics ◽  
Transformation Products ◽  
White Rot ◽  
White Rot Fungus ◽  
Kinetics Of

The urban-use pesticide, fipronil, is metabolized to novel transformation products by white rot fungusT. versicolor.

scholarly journals Kinetics of inter-domain electron transfer in flavocytochrome cellobiose dehydrogenase from the white-rot fungus Phanerochaete chrysosporium

2002 ◽  
Vol 365 (2) ◽  
pp. 521-526 ◽  
Author(s):  
Kiyohiko IGARASHI ◽  
Ikuo MOMOHARA ◽  
Takeshi NISHINO ◽  
Masahiro SAMEJIMA
Keyword(s):  
Electron Transfer ◽  
Phanerochaete Chrysosporium ◽  
Substrate Concentration ◽  
Substrate Inhibition ◽  
Cellobiose Dehydrogenase ◽  
White Rot ◽  
White Rot Fungus ◽  
Isosbestic Point ◽  
Second Phase ◽  
Kinetics Of

The pre-steady-state kinetics of inter-domain electron transfer in the extracellular flavocytochrome cellobiose dehydrogenase from Phanerochaete chrysosporium was studied using various values of pH and substrate concentration. Monitoring at the isosbestic point of each prosthetic group indicated that the reductive half-reactions of flavin and haem were biphasic and monophasic respectively. When the observed rates of the flavin and haem reactions were plotted against substrate concentration, the behaviour of the second phase of the flavin reduction was almost identical with that of haem reduction at all substrate concentrations and pH values tested, suggesting that the formation of flavin semiquinone and haem reduction involve the same electron transfer reaction. Although flavin reduction by cellobiose was observed in the range of pH3.0–7.0, the velocity of the next electron transfer step decreased with increase of pH and was almost zero above pH6.0. The second phase of flavin reduction and the haem reduction were inhibited similarly by high concentrations of the substrate, whereas the first phase of flavin reduction showed a hyperbolic relation to the cellobiose concentration. Increase in pH enhanced the substrate inhibition of haem reduction but not the initial flavin reduction. Moreover, the dissociation constant Kd of flavin reduction and the substrate inhibition constant Ki of haem reduction decreased similarly with an increase of pH. From these results, it is evident that binding of cellobiose to the active site inhibits electron transfer from flavin to haem.

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