scholarly journals Isolation and cloning of an aryl-aldehyde dehydrogenase gene from the white-rot fungus Pycnoporus cinnabarinus strain MUCL 39533

2015 ◽  
Author(s):  
Ong, K. L. ◽  
Liew, S. L. ◽  
Mutalib, S. A. ◽  
Murad, A. M. A. ◽  
Abu Bakar, F. D.
Keyword(s):  
Aldehyde Dehydrogenase ◽  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus ◽  
Dehydrogenase Gene ◽  
Aryl Aldehyde

Investigation of the role of 3-hydroxyanthranilic acid in the degradation of lignin by white-rot fungus Pycnoporus cinnabarinus

2001 ◽  
Vol 28 (4-5) ◽  
pp. 301-307 ◽  
Author(s):  
Kaichang Li ◽  
Peter S Horanyi ◽  
Robert Collins ◽  
Robert S Phillips ◽  
Karl-Erik L Eriksson
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus ◽  
Hydroxyanthranilic Acid

Bioremediation of a wine distillery wastewater using white rot fungi and the subsequent production of laccase

2007 ◽  
Vol 56 (2) ◽  
pp. 179-186 ◽  
Author(s):  
P.J. Strong ◽  
J.E. Burgess
Keyword(s):  
Biological Treatment ◽  
Oxygen Demand ◽  
White Rot Fungi ◽  
White Rot ◽  
White Rot Fungus ◽  
Laccase Production ◽  
Total Phenolic ◽  
Pycnoporus Cinnabarinus ◽  
Distillery Wastewater

The aim of this work was to ascertain whether a submerged culture of a white rot fungus could be used to treat distillery wastewater, and whether the compounds present in the wastewater would stimulate laccase production. Trametes pubescens MB 89, Ceriporiopsissubvermispora, Pycnoporus cinnabarinus and UD4 were screened for their ability for the bioremediation of a raw, untreated distillery wastewater as well as distillery wastewater that had been pretreated by polyvinylpolypyrrolidone. Suitability of each strain was measured as a function of decreasing the chemical oxygen demand (COD) and total phenolic compounds concentration and the colour of the wastewater, while simultaneously producing laccase in high titres. After screening, T. pubescens MB 89 was used further in flask cultures and attained 79±1.1% COD removal, 80±4.6% total phenols removal, 71±1.6% decrease in colour at an absorbance of 500 nm and increased the pH from 5.3 to near-neutral. Laccase activity in flask cultures peaked at 4,644±228 units/l, while the activity in a 50 l bubble lift reactor peaked at 12,966±71 units/l. Trametes pubescens MB 89 greatly improved the quality of a wastewater known for toxicity towards biological treatment systems, while simultaneously producing an industrially relevant enzyme.

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%).

Laccase-less mutants of the white-rot fungus Pycnoporus cinnabarinus cannot delignify kraft pulp

1998 ◽  
Vol 66 (2-3) ◽  
pp. 117-124 ◽  
Author(s):  
Hakan Bermek ◽  
Kaichang Li ◽  
Karl Erik-L Eriksson
Keyword(s):  
Kraft Pulp ◽  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus

Vanillin as a product of ferulic acid biotransformation by the white-rot fungus Pycnoporus cinnabarinus I-937: Identification of metabolic pathways

1994 ◽  
Vol 37 (2) ◽  
pp. 123-132 ◽  
Author(s):  
B. Falconnier ◽  
C. Lapierre ◽  
L. Lesage-Meessen ◽  
G. Yonnet ◽  
P. Brunerie ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Metabolic Pathways ◽  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus

Isolation of a new laccase isoform from the white-rot fungiPycnoporus cinnabarinusstrain ss3

2000 ◽  
Vol 46 (8) ◽  
pp. 759-763 ◽  
Author(s):  
Ludovic Otterbein ◽  
Eric Record ◽  
David Chereau ◽  
Isabelle Herpoël ◽  
Marcel Asther ◽  
...  
Keyword(s):  
First Generation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus ◽  
Ammonium Sulphate Precipitation ◽  
Liquid Culture Medium

Two extracellular laccase isoforms (Lac I and Lac II) produced by the white-rot fungus Pycnoporus cinnabarinus from the monokaryotic strain ss3 were purified from ferulic-acid-induced liquid culture medium using ammonium sulphate precipitation, followed by anion-exchange chromatography on a Mono Q column. Strain ss3 is the first generation of the parental strain P. cinnabarinus I-937. The new isolated isoform, Lac II, consists of an 86 000 molecular weight protein as determined by SDS polyacrylamide gel electrophoresis. The N-terminal amino acid sequences of both isoforms were determined, and compared to known laccase protein sequences of other organisms.Key words: oxydo-reductase, filamentous fungi, purification.

scholarly journals Heterologous Production and Characterization of Two Glyoxal Oxidases from Pycnoporus cinnabarinus

2016 ◽  
Vol 82 (16) ◽  
pp. 4867-4875 ◽  
Author(s):  
Marianne Daou ◽  
François Piumi ◽  
Daniel Cullen ◽  
Eric Record ◽  
Craig B. Faulds
Keyword(s):  
Substrate Specificity ◽  
Metal Ion ◽  
Inorganic Compounds ◽  
Glyoxylic Acid ◽  
Catalytic Efficiency ◽  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus ◽  
Content Type ◽  
Glyoxal Oxidase

ABSTRACTThe genome of the white rot fungusPycnoporus cinnabarinusincludes a large number of genes encoding enzymes implicated in lignin degradation. Among these, three genes are predicted to encode glyoxal oxidase, an enzyme previously isolated fromPhanerochaete chrysosporium. The glyoxal oxidase ofP. chrysosporiumis physiologically coupled to lignin-oxidizing peroxidases via generation of extracellular H2O2and utilizes an array of aldehydes and α-hydroxycarbonyls as the substrates. Two of the predicted glyoxal oxidases ofP. cinnabarinus, GLOX1 (PciGLOX1) and GLOX2 (PciGLOX2), were heterologously produced inAspergillus nigerstrain D15#26 (pyrGnegative) and purified using immobilized metal ion affinity chromatography, yielding 59 and 5 mg of protein forPciGLOX1 andPciGLOX2, respectively. Both proteins were approximately 60 kDa in size and N-glycosylated. The optimum temperature for the activity of these enzymes was 50°C, and the optimum pH was 6. The enzymes retained most of their activity after incubation at 50°C for 4 h. The highest relative activity and the highest catalytic efficiency of both enzymes occurred with glyoxylic acid as the substrate. The twoP. cinnabarinusenzymes generally exhibited similar substrate preferences, butPciGLOX2 showed a broader substrate specificity and was significantly more active on 3-phenylpropionaldehyde.IMPORTANCEThis study addresses the poorly understood role of how fungal peroxidases obtain anin situsupply of hydrogen peroxide to enable them to oxidize a variety of organic and inorganic compounds. This cooperative activity is intrinsic in the living organism to control the amount of toxic H2O2in its environment, thus providing a feed-on-demand scenario, and can be used biotechnologically to supply a cheap source of peroxide for the peroxidase reaction. The secretion of multiple glyoxal oxidases by filamentous fungi as part of a lignocellulolytic mechanism suggests a controlled system, especially as these enzymes utilize fungal metabolites as the substrates. Two glyoxal oxidases have been isolated and characterized to date, and the differentiation of the substrate specificity of the two enzymes produced byPycnoporus cinnabarinusillustrates the alternative mechanisms existing in a single fungus, together with the utilization of these enzymes to prepare platform chemicals for industry.

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