The ability to decolorize four synthetic dyes (Phenol Red, Evans Blue, Eosin Yellowish and Poly B411) in five Pleurotus ostreatus strains (a parental strain and four isolates derived from it) was determined. Two of the isolates had markedly higher and other two substantially lower production of ligninolytic enzymes and hydrogen peroxide than the parental strain. Like the parental strain, the higher-producing isolates were able to decolorize all the tested dyes, but not to a higher extent than the parental strain. In contrast, two lower-producing isolates exhibited slow decolorization, which was incomplete even at the end of cultivation. Evans Blue and Eosin Yellowish strongly suppressed the growth of the strains, while Phenol Red and Poly B411 induced none or only a very slight growth reduction.

• MeSH
• Color MeSH
• Coloring Agents metabolism   MeSH
• Laccase MeSH
• Oxidoreductases metabolism   MeSH
• Hydrogen Peroxide metabolism   MeSH
• Peroxidases metabolism   MeSH
• Pleurotus chemistry   enzymology   metabolism   MeSH
• Textile Industry MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Coloring Agents MeSH
• Laccase MeSH
• manganese peroxidase MeSH Browser
• Oxidoreductases MeSH
• Hydrogen Peroxide MeSH
• Peroxidases MeSH

Neem hull waste (containing a high amount of lignin and other phenolic compounds) was used for lignin peroxidase production by Phanerochaete chrysosporum under solid-state fermentation conditions. Maximum decolorization achieved by partially purified lignin peroxidase was 80% for Porocion Brilliant Blue HGR, 83 for Ranocid Fast Blue, 70 for Acid Red 119 and 61 for Navidol Fast Black MSRL. The effects of different concentrations of veratryl alcohol, hydrogen peroxide, enzyme and dye on the efficiency of decolorization have been investigated. Maximum decolorization efficiency was observed at 0.2 and 0.4 mmol/L hydrogen peroxide, 2.5 mmol/L veratryl alcohol and pH 5.0 after a 1-h reaction, using 50 ppm of dyes and 9.96 mkat/L of enzyme.

• MeSH
• Azadirachta MeSH
• Color MeSH
• Coloring Agents metabolism   MeSH
• Benzyl Alcohols metabolism   MeSH
• Biodegradation, Environmental MeSH
• Bioreactors MeSH
• Hydrogen-Ion Concentration MeSH
• Culture Media MeSH
• Lignin metabolism   MeSH
• Peroxidases metabolism   MeSH
• Phanerochaete enzymology   MeSH
• Substrate Specificity MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Coloring Agents MeSH
• Benzyl Alcohols MeSH
• Culture Media MeSH
• lignin peroxidase MeSH Browser
• Lignin MeSH
• manganese peroxidase MeSH Browser
• Peroxidases MeSH
• veratryl alcohol MeSH Browser

The ability of a Brazilian strain of Pleurotus pulmonarius to decolorize structurally different synthetic dyes (including azo, triphenylmethane, heterocyclic and polymeric dyes) was investigated in solid and submerged cultures. Both were able to decolorize completely or partially 8 of 10 dyes (Amido Black, Congo Red, Trypan Blue, Methyl Green, Remazol Brilliant Blue R, Methyl Violet, Ethyl Violet, Brilliant Cresyl Blue). No decolorization of Methylene Blue and Poly R 478 was observed. Of the four phenol-oxidizing enzymes tested in culture filtrates (lignin peroxidase, manganese peroxidase, aryl alcohol oxidase, laccase), P. pulmonarius produced only laccase. Both laccase activity and dye decolorization were related to glucose and ammonium starvation or to induction by ferulic acid. The decolorization in vivo was tested using three dyes--Remazol Brilliant Blue R, Trypan Blue and Methyl Green. All of them were completely decolorized by crude extracellular extracts. Decolorization and laccase activity were equally affected by pH and temperature. Laccase can thus be considered to be the major enzyme involved in the ability of P. pulmonarius to decolorize industrial dyes.

• MeSH
• Coloring Agents metabolism   MeSH
• Fermentation MeSH
• Laccase MeSH
• Oxidoreductases biosynthesis   metabolism   MeSH
• Pleurotus enzymology   metabolism   MeSH
• Industrial Microbiology * MeSH
• Monophenol Monooxygenase biosynthesis   metabolism   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Geographicals
• Brazil MeSH
• Names of Substances
• Coloring Agents MeSH
• Laccase MeSH
• Oxidoreductases MeSH
• Monophenol Monooxygenase MeSH

Laccase activity in Trichoderma harzianum and in our own isolate Trichoderma atroviride was correlated with the production of the green pigment in conidial spores. The laccases of the two fungal species exhibit comparable kinetic parameters, pH optima and thermal sensitivity but differed in physiological properties, such as their catalytic activity during growth.

• MeSH
• Kinetics MeSH
• Hydrogen-Ion Concentration MeSH
• Laccase MeSH
• Oxidoreductases chemistry   metabolism   MeSH
• Spores, Fungal enzymology   growth & development   MeSH
• Temperature MeSH
• Trichoderma enzymology   growth & development   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Laccase MeSH
• Oxidoreductases MeSH

White-rot fungi, Coriolus versicolor and Funalia trogii, produced laccase on media with diluted olive-oil mill wastewater and vinasse. Addition of spent cotton stalks enhanced the laccase activity with a maximum after 12 d of cultivation.

• MeSH
• Gossypium MeSH
• Culture Media MeSH
• Laccase MeSH
• Waste Products * MeSH
• Plant Oils MeSH
• Olive Oil MeSH
• Oxidoreductases metabolism   MeSH
• Polyporales metabolism   MeSH
• Industrial Waste * MeSH
• Agriculture * MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Culture Media MeSH
• Laccase MeSH
• Waste Products * MeSH
• Plant Oils MeSH
• Olive Oil MeSH
• Oxidoreductases MeSH
• Industrial Waste * MeSH

The relationship between production of 3-indoleacetic acid (IAA) and peroxidase and laccase activity was investigated in white-rot fungus Funalia trogii (Trametes trogii). F. trogii produced IAA and peroxidase and laccase as both primary metabolite and secondary metabolite; the levels of IAA may be influenced by peroxidase and laccase. A correlation exists between the levels of IAA and peroxidase-laccase activity.

• MeSH
• Indoleacetic Acids metabolism   MeSH
• Laccase MeSH
• Oxidoreductases metabolism   MeSH
• Peroxidase metabolism   MeSH
• Polyporales enzymology   metabolism   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• indoleacetic acid MeSH Browser
• Indoleacetic Acids MeSH
• Laccase MeSH
• Oxidoreductases MeSH
• Peroxidase MeSH