Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology
A Box-Wilson central composite design was applied to optimize copper, veratryl alcohol and L-asparagine concentrations for Trametes trogii (BAFC 212) ligninolytic enzyme production in submerged fermentation. Decolorization of different dyes (xylidine, malachite green, and anthraquinone blue) by the...
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todo:paper_13675435_v30_n12_p682_Trupkin2023-10-03T16:11:34Z Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology Trupkin, S. Levin, L. Forchiassin, F. Viale, A. Dye decolorization Ligninolytic enzymes Response surface methodology Trametes trogii White-rot fungi anthraquinone dye glyoxal indigo carmine laccase lignin malachite green manganese peroxidase article bacterium culture cell free system chemical structure decolorization enzyme active site enzyme degradation enzyme synthesis fungal sclerotium fungal strain intermethod comparison intracellular membrane microbial biomass nonhuman response surface method supernatant Alcohol Oxidoreductases Coloring Agents Culture Media Fermentation Fungal Proteins Industrial Microbiology Laccase Lignin Polyporaceae Bacteria (microorganisms) Funalia trogii Fungi Indigofera Siproeta stelenes Trametes A Box-Wilson central composite design was applied to optimize copper, veratryl alcohol and L-asparagine concentrations for Trametes trogii (BAFC 212) ligninolytic enzyme production in submerged fermentation. Decolorization of different dyes (xylidine, malachite green, and anthraquinone blue) by the ligninolytic fluids from the cultures was compared. The addition of copper stimulated laccase and glyoxal oxidase production, but this response was influenced by the medium N-concentration, with improvement higher at low N-levels. The medium that supported the highest ligninolytic production (22.75 U/ml laccase, 0.34 U/ml manganese peroxidase, and 0.20 U/ml glyoxal oxidase) also showed the greatest ability to decolorize the dyes. Only glyoxal oxidase activity limited biodecoloration efficiency, suggesting the involvement of peroxidases in the process. The addition of 1-hydroxybenzotriazole (a known laccase mediator) to the ligninolytic fluids increased both their range and rate of decolorization. The cell-free supernatant did not decolorize xylidine, poly R-478, azure B, and malachite green as efficiently as the whole broth, but results were similar in the case of indigo carmine and remazol brilliant blue R. This indicates that the mycelial biomass may supply other intracellular or mycelial-bound enzymes, or factors necessary for the catalytic cycle of the enzymes. It also implies that this fungus implements different strategies to degrade dyes with diverse chemical structures. Fil:Trupkin, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Levin, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Forchiassin, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Viale, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13675435_v30_n12_p682_Trupkin |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Dye decolorization Ligninolytic enzymes Response surface methodology Trametes trogii White-rot fungi anthraquinone dye glyoxal indigo carmine laccase lignin malachite green manganese peroxidase article bacterium culture cell free system chemical structure decolorization enzyme active site enzyme degradation enzyme synthesis fungal sclerotium fungal strain intermethod comparison intracellular membrane microbial biomass nonhuman response surface method supernatant Alcohol Oxidoreductases Coloring Agents Culture Media Fermentation Fungal Proteins Industrial Microbiology Laccase Lignin Polyporaceae Bacteria (microorganisms) Funalia trogii Fungi Indigofera Siproeta stelenes Trametes |
| spellingShingle |
Dye decolorization Ligninolytic enzymes Response surface methodology Trametes trogii White-rot fungi anthraquinone dye glyoxal indigo carmine laccase lignin malachite green manganese peroxidase article bacterium culture cell free system chemical structure decolorization enzyme active site enzyme degradation enzyme synthesis fungal sclerotium fungal strain intermethod comparison intracellular membrane microbial biomass nonhuman response surface method supernatant Alcohol Oxidoreductases Coloring Agents Culture Media Fermentation Fungal Proteins Industrial Microbiology Laccase Lignin Polyporaceae Bacteria (microorganisms) Funalia trogii Fungi Indigofera Siproeta stelenes Trametes Trupkin, S. Levin, L. Forchiassin, F. Viale, A. Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| topic_facet |
Dye decolorization Ligninolytic enzymes Response surface methodology Trametes trogii White-rot fungi anthraquinone dye glyoxal indigo carmine laccase lignin malachite green manganese peroxidase article bacterium culture cell free system chemical structure decolorization enzyme active site enzyme degradation enzyme synthesis fungal sclerotium fungal strain intermethod comparison intracellular membrane microbial biomass nonhuman response surface method supernatant Alcohol Oxidoreductases Coloring Agents Culture Media Fermentation Fungal Proteins Industrial Microbiology Laccase Lignin Polyporaceae Bacteria (microorganisms) Funalia trogii Fungi Indigofera Siproeta stelenes Trametes |
| description |
A Box-Wilson central composite design was applied to optimize copper, veratryl alcohol and L-asparagine concentrations for Trametes trogii (BAFC 212) ligninolytic enzyme production in submerged fermentation. Decolorization of different dyes (xylidine, malachite green, and anthraquinone blue) by the ligninolytic fluids from the cultures was compared. The addition of copper stimulated laccase and glyoxal oxidase production, but this response was influenced by the medium N-concentration, with improvement higher at low N-levels. The medium that supported the highest ligninolytic production (22.75 U/ml laccase, 0.34 U/ml manganese peroxidase, and 0.20 U/ml glyoxal oxidase) also showed the greatest ability to decolorize the dyes. Only glyoxal oxidase activity limited biodecoloration efficiency, suggesting the involvement of peroxidases in the process. The addition of 1-hydroxybenzotriazole (a known laccase mediator) to the ligninolytic fluids increased both their range and rate of decolorization. The cell-free supernatant did not decolorize xylidine, poly R-478, azure B, and malachite green as efficiently as the whole broth, but results were similar in the case of indigo carmine and remazol brilliant blue R. This indicates that the mycelial biomass may supply other intracellular or mycelial-bound enzymes, or factors necessary for the catalytic cycle of the enzymes. It also implies that this fungus implements different strategies to degrade dyes with diverse chemical structures. |
| format |
JOUR |
| author |
Trupkin, S. Levin, L. Forchiassin, F. Viale, A. |
| author_facet |
Trupkin, S. Levin, L. Forchiassin, F. Viale, A. |
| author_sort |
Trupkin, S. |
| title |
Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| title_short |
Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| title_full |
Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| title_fullStr |
Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| title_full_unstemmed |
Optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| title_sort |
optimization of a culture medium for ligninolytic enzyme production and synthetic dye decolorization using response surface methodology |
| url |
http://hdl.handle.net/20.500.12110/paper_13675435_v30_n12_p682_Trupkin |
| work_keys_str_mv |
AT trupkins optimizationofaculturemediumforligninolyticenzymeproductionandsyntheticdyedecolorizationusingresponsesurfacemethodology AT levinl optimizationofaculturemediumforligninolyticenzymeproductionandsyntheticdyedecolorizationusingresponsesurfacemethodology AT forchiassinf optimizationofaculturemediumforligninolyticenzymeproductionandsyntheticdyedecolorizationusingresponsesurfacemethodology AT vialea optimizationofaculturemediumforligninolyticenzymeproductionandsyntheticdyedecolorizationusingresponsesurfacemethodology |
| _version_ |
1807319876081025024 |