New approach to improve degradation of recalcitrant azo dyes by Streptomyces spp. and Phanerochaete chrysosporium

  title={New approach to improve degradation of recalcitrant azo dyes by Streptomyces spp. and Phanerochaete chrysosporium},
  author={Andrzej J. Paszczynski and Maria B. Pasti and Stefan Goszczyński and Don L. Crawford and Ronald L. Crawford},
  journal={Enzyme and Microbial Technology},
Mineralization of sulfonated azo dyes and sulfanilic acid by Phanerochaete chrysosporium and Streptomyces chromofuscus
This work showed that lignocellulolytic fungi and bacteria can be used for the biodegradation of anionic azo dyes, which thus far have been considered among the xenobiotic compounds most resistant to biodegradability.
Degradation of azo dyes by the lignin-degrading fungus Phanerochaete chrysosporium
The results suggest that P. chrysosporium has potential applications for the cleanup of textile mill effluents and for the bioremediation of dye-contaminated soil.
New pathway for degradation of sulfonated azo dyes by microbial peroxidases of Phanerochaete chrysosporium and Streptomyces chromofuscus
Pathways for the degradation of 3,5-dimethyl-4-hydroxy-azobenzene-4'-sulfonic acid (I) and 3-methoxy-4-hydroxyazobenzene-4'-sulfonamide (II) by the manganese peroxidase and ligninase of Phanerochaete
Transformation of Azo Dye Isomers by Streptomyces chromofuscus A11
Replacement of the sulfonic group with a carboxylic group enhanced overall dye degradability by S. chromofuscus A11.
Decolorization of Azo, Triphenyl Methane, Heterocyclic, and Polymeric Dyes by Lignin Peroxidase Isoenzymes from Phanerochaete chrysosporium
The ligninolytic enzyme system of Phanerochaete chrysosporium decolorizes several recalcitrant dyes and the ability of the isoenzymes to decolorize the dyes in the presence of veratryl alcohol was generally comparable to that of the crude enzyme preparation, suggesting that lignin peroxidase plays a major role in the decolorization.
Azo dye transformation by enzymatic and chemical systems
An investigation of azo dye decolorization by peroxidases, hydroxyl radicals, zero-valent iron, and NADH is described, suggesting that the initial attack of .
Relationships between the abilities of streptomycetes to decolorize three anthron-type dyes and to degrade lignocellulose
Fourteen Streptomyces strains known to degrade lignocellulose were screened for their ability to decolorize three anthron-type dyes: Remazol Brilliant Blue R (RBBR), blue poly(vinylamine) sulfonate –
Basic and applied aspects in the microbial degradation of azo dyes
  • A. Stolz
  • Biology, Engineering
    Applied Microbiology and Biotechnology
  • 2001
Several (laboratory-scale) continuous anaerobic/aerobic processes for the treatment of wastewaters containing azo dyes have recently been described.


Novel extracellular enzymes (ligninases) of Phanerochaete chrysosporium
3 new spectrophotometric enzyme assays were developed for the study of microbial lignin-degrading enzymes and led to the discovery of an extracellular, aromatic methyl ether demethylase produced by the white-rot fungus Phanerochaete chrysosporium.
Properties of purified Orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46.
A survey of the efficiency of various Orange dyes as substrates for Orange II azoreductase showed that a hydroxy group in the 2-position of the naphthol ring is required and charged groups in proximity to the azo group hinder the reaction.
Metabolism of cinnamic, p-coumaric, and ferulic acids by Streptomyces setonii.
Streptomyces setonii strain 75Vi2 was grown at 45 degrees C in liquid media containing yeast extract and trans-cinnamic acid, p-coumaric acid, ferulic acid, or vanillin. Gas chromatography,
Catabolism of Substituted Benzoic Acids by Streptomyces Species
Four thermotolerant actinomycetes from soil, identified as Streptomyces albulus 321, Streptomyces sioyaensis P5, Streptomyces viridosporus T7A, and Streptomyces sp. V7, were grown at 45°C in media
The oxidative 4-dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases
The results indicate a mechanism whereby lignin peroxidase oxidizes a 4- chlorinated phenol to an electrophilic intermediate, perhaps the 4-chlorocyclohexadienone cation, which produces the quinone.
Streptomyces setonii: catabolism of vanillic acid via guaiacol and catechol.
A unique feature of this strain was its catabolism of vanillic acid by of guaiacol and catechol, using a pathway that had not been confirmed previously.
Characterization of an extracellular lignin peroxidase of the lignocellulolytic actinomycete Streptomyces viridosporus
This is the first report of a lignin peroxidase in a bacterium designated as ALiP-P3 and characterizations showed that this enzyme is a heme protein (Soret band, 408 nm) and a major component of the ligninolytic system of S. viridosporus T7A.
Biodegradation of azo and heterocyclic dyes by Phanerochaete chrysosporium
Biodegradation of Orange II, Tropaeolin O, Congo Red, and Azure B in cultures of the white rot fungus, Phanerochaete chrysosporium, was demonstrated by decolarization of the culture medium, the
Biodegradation of TNT (2,4,6-trinitrotoluene) by Phanerochaete chrysosporium
Results suggest that the white rot fungus Phanerochaete chrysosporium may be useful for the decontamination of sites in the environment contaminated with TNT.