Results 121 to 130 of about 3,868 (158)
Cerrena unicolor (Basidiomycota, polypore), une espèce à morphologie variable
Cerrena unicolor (Basidiomycota, polypore), a species with a variable morphology. The authors describe Cerrena unicolor and its shapes from their own collections. For this taxon, three shapes are retained : irpicoides (Bourdot et Galzin) Domanski, Orlos et Skirgiello, resupinata (Bourdot et Galzin) Bondartzew and a new shape called poroides.
Bernard Rivoire
exaly +4 more sources
The objective of this study was to investigate the hypoglycemic activity of crude exopolysaccharides (EPS) produced by three mushroom isolates in streptozotocin-induced diabetic rats.
Gungor Kanbak +2 more
exaly +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Cerrena unicolor (Bull.) Murrill - CERRENACEAE
2023International ...
Gafforov, Yusufjon +6 more
openaire +2 more sources
In this study, the culture requirements of the Cerrena unicolor OBCC 5005 strain were determined to optimize bioactive exopolysaccharide production in submerged culture.
Bükay Yenice Gürsu, Mustafa Yamaç
exaly +2 more sources
PURIFICATION OF EXTRACELLULAR LACCASE FROMCerrena unicolor
Preparative Biochemistry and Biotechnology, 2010Cerrena unicolor was found to produce large amounts of extracellular laccase when grown aerobically on the optimized Lindenberg and Holm medium in fermenter culture with an automatic pH control. The laccase from this source was purified to homogeneity by a rapid procedure, using ion-exchange chromatography, affinity chromatography, and chromatofocusing.
Jerzy Marian Rogalski, Janusz, G.
openaire +3 more sources
Applied Biochemistry and Microbiology, 2003
Laccases of the basidiomycetes Cerrena unicolor 059, C. unicolor 0784, and Pleurotus oastreatus 0432 were subjected to a comparative study. The enzymes were isolated as homogeneous preparations with molecular weights of 55, 56, and 57 kD, respectively. The three enzymes were found to be glycoproteins.
E. V. Stepanova +4 more
openaire +1 more source
Laccases of the basidiomycetes Cerrena unicolor 059, C. unicolor 0784, and Pleurotus oastreatus 0432 were subjected to a comparative study. The enzymes were isolated as homogeneous preparations with molecular weights of 55, 56, and 57 kD, respectively. The three enzymes were found to be glycoproteins.
E. V. Stepanova +4 more
openaire +1 more source
Proteolytic modifications of laccase from Cerrena unicolor
Journal of Molecular Catalysis B: Enzymatic, 2015Laccase from the wood-degrading Cerrena unicolor FCL139 has been proved many times to be useful as a decolorizing enzyme, antibacterial agent, and important part of biosensors. In recent papers, there have been attempts to modify its structure and thereby alter its features and activity.
Grzegorz Janusz +4 more
openaire +2 more sources
Increased production of laccase by Cerrena unicolor in submerged liquid cultures
World Journal of Microbiology and Biotechnology, 2007The wood-degrading basidiomycete Cerrena unicolor C-139 has been suggested as a potential producer of the industrially important enzyme laccase. Basic culture parameters influencing the enzyme synthesis in shaken-flask and aerated bioreactor cultures were evaluated to improve the yields of the process.
Janusz, G. +2 more
openaire +2 more sources
Effect of Various Pollutants and Soil‐Like Constituents on Laccase from Cerrena unicolor
Journal of Environmental Quality, 1999AbstractLaccase from Cerrena unicolor catalyses the oxidation of a wide range of aromatic compounds, either xenobiotic or naturally occurring phenols, leading to the formation of polymeric products. These are characterized by their low solubility and often may form precipitates or aggregates. The oxidizing efficiency of the enzyme is strictly dependent
M. T. Filazzola +3 more
openaire +3 more sources
Immobilization of laccase from Cerrena unicolor on controlled porosity glass
Journal of Molecular Catalysis B: Enzymatic, 1999White-rot basidiomycete Cerrena unicolor grown in non-induced and induced conditions was tested for production of laccase, lignin peroxidase (LiP) and manganese-dependent peroxidase (MnP). A typical correlation between the concentration of phenolic compounds in the culture fluid and the extracellular laccase activity was observed.
Jerzy Marian Rogalski +3 more
openaire +1 more source

