• Journal of Mushroom
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• v.20 no.2
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• pp.86-91
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• 2022

Pleurotus eryngii, a white rot fungus, produces two extracellular lignin-degrading enzymes, laccase and manganese peroxidase (MnP). Owing to these enzymes, P. eryngii efficiently degrades synthetic chemicals such as azo, phthalocyanine, and triphenyl methane dyes. In this study, we investigated the degradation processes of four aromatic dyes, congo red (CR), methylene blue (MB), crystal violet (CV), and malachite green (MG), by P. eryngii under solid and liquid culture conditions. CR and MG were the most quickly degraded under solid and liquid culture conditions, respectively. However, compared to CR, CV, and MG, MB was not degraded well under both culture conditions. The activities of ligninolytic enzymes (laccase and MnP) were also investigated. Laccase was identified to be the major enzyme for dye degradation. A positive relationship between decolorization and enzyme activity was observed for CR, MB, and CV degradation. In contrast, decolorization of MG ensued after high enzyme activity. These results indicate that the degradation process differs between MG and the other aromatic dyes. Therefore, P. eryngii could be a potential tool for the bioremediation of synthetic aromatic dye effluent.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1977.10a
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• pp.191-192
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• 1977

Microbial degradation of unnatural synthetic substances are interesting from hypothesis that a new metabolic pathway should be established from the unnatural compound to a common metabolic intermediate fro such an ability. The establishment of a new pathway essentially require a creature of new enzyme active on the unnatural synthetic compound which have never existed on the each.(중략)

• Journal of Applied Biological Chemistry
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• v.50 no.4
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• pp.221-226
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• 2007

The high molecular-weight mucilage extracted and purified from cactus fruit of Opuntia ficus-indica var. Saboten was degraded by the cell-free culture filtrate of a fungus isolated from soil. TLC analysis of the polymeric mucilage after incubation with the fungal culture filtrate confirmed its degradation. When the degradation products were tested for their qualitative reactions with ninhydrin and phenol-sulfuric acid, only phenol-sulfuric acid gave positive development, and ninhydrin did not show any observable color reaction. This coloring reaction suggested the presence of a carbohydrate without an amino group within the mucilage. Analyses by HPLC and liquid gel permeation chromatography on sephadex G-100 also provided additional information on degradation of the mucilage by the fungal culture filtrate. The sequences of ITS-5.8S rDNA from the fungal isolate that was cultivated for the preparation of mucilage-degrading enzyme showed 99% similarity to those of Pestalotiopsis aquatica.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.41 no.2
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• pp.102-106
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• 2008

Formaldehyde, an indoor volatile organic compound, is considered toxic due to its carcinogenic risk. Recently, we isolated a formaldehyde-degrading bacterium Pseudomonas sp. YK-32. A crude enzyme prepared from YK-32 also degraded formaldehyde, suggesting that YK-32 cells have formaldehyde hydrogenase activity which is one of the important factors in formaldehyde degradation. The formaldehyde hydrogenase activity was increased 1.25 fold by adding 0.1 % glucose and formaldehyde to the culture medium. In addition, treatment with 1 mM EDTA as a permeabilizer promoted the degradation of formaldehyde and increased the enzymatic activity.

• Journal of Environmental Health Sciences
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• v.30 no.2
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• pp.161-166
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• 2004

The impact of dissolved wastewater constituents on the treatment of synthetic bisphenol A (BPA) solutions was investigated under a variety of reaction conditions. The laccase enzyme from Trametes vesicolor was used for the BPA treatment. The constituents studied included various inorganic salts, organic compounds and heavy metal ions. BPA degradation was inhibited by sulfate, thiosulfate, sulfide, nitrite, and cyanide ions at 25 mg/$\ell$, 100mg/$\ell$, 25 mg/$\ell$ 150 mg/$\ell$, and 2.5 mg/$\ell$, respectively. However, the inhibitive effects of sulfide and sulfite on BPA degradation were diminished by additional aeration to oxidize them. Formaldehyde significantly reduced the rate of BPA degradation at 1.0% among organic compounds studied. Among heavy metal ions tested, Fe(II) substantially suppressed BPA removal at 1 mM. MgCl$_2$ and CaCl$_2$ exhibited great inhibition of BPA degradation at 25mM.

• Journal of the Korean Wood Science and Technology
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• v.32 no.3
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• pp.79-87
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• 2004

The objectives of this study were to select superior fungus for lignin degradation and to decolor dyes by selected fungus. Ligninolytic fungi were screened and isolated from decayed woods. Ten ligninolytic fungi were selected by ligninolytic enzyme activity on the PDA media containing rhemazol brilliant blue R, guaiacol and gallic acid. Their lignin degradation abilities were tested on the extractive-free wood powder of Quercus acutissima and Pinus densiflora. As a result, 8J-28 was selected as superior fungus for lignin degradation. Also, decolorization abilities of dyes were examined by shaking and static culture. And congo red, crystal violet, poly R-478, methylene blue used to investigate decolorization abilities of dyes. As a result, 8J-28 showed over 90% in decolorization of congo red, crystal violet, poly R-478.

• Journal of Microbiology and Biotechnology
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• v.10 no.4
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• pp.462-469
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• 2000

Sixty-one strains representing the main genera of wood-decaying xylariaceous fungi (mainly in Daldinia, Hypoxylon, Kretzschmaria, Rosellinia, Penzigia, and Xylaria) were tested for their ability to produce ligninolytic enzymes. The phenol oxidase activity and fungal growth of the xylariaceous fungi on gallic aicid and tannic acid media showed a variation in their ability to degrade lignocellulose. A number of species showed equal 개 betterligninolytic enzyme activities than Coriolus versicolor, a known basidiomycete wood-degrader. A large variation of the enzyme activity was observed by individual strains as well as a substantial variation between the isolates of the same species. The most frequent ligninolytic enzymes were peroxidase and general oxidase. With 19% of the strains tested, peroxidase showed the strongest ligninolytic enzyme activity, while tyrosinase activity was detected only in 7% of the strains. All strains of Kretzschmaria and Rosellinia tested was positive for laccase. Xylariaceous fungi were able to degrade the macromolecule, lignin, using each specific ligninolytic enzyme in the specfic lignin degradation pathway.

• Microbiology and Biotechnology Letters
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• v.23 no.2
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• pp.203-208
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• 1995

The Polyvinyl alcohol (PVA) oxidase is a key enzyme involved in degradation of PVA with PVA hydrolase. The PVA oxidase has been purified to homogeneity from the culture broth of PVA grown Pseudomonas cepacia G5Y strain by ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-150 gel filtration. The molecular weight of the purified enzyme was estimated about 60, 000 daltons by SDS-polyacrylamid gel electrophoresis. The enzyme is most active at 45$\circ$C and at pH 8.5, and is stable below 55$\circ$C and between pH 6 and 9. The enzyme activity was strongly inhibited by Ag$^{2+}$ and Hg$^{2+}$.

• Microbiology and Biotechnology Letters
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• v.21 no.3
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• pp.276-280
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• 1993

Cell lytic enzyme, 5'-phosphodiesterase, and AMP-deaminase were used to produce yeast extract as a natural seasoning from beer yeast cells. Prior to the addition of cell lytic enzyme, heat treatment was performed to increase the cell wall degradation` the optimum condition of the cell lytic enzyme was 50C at pH 7.0. The production yields by the enzymatic method and conventional autolysis method were 42% and 35%, respectively. The total quantity of 5'-nucleotides, GMP and IMP, produced by enzymatic method was increased by 45% than that by the conventional method. Futhermore, the operation time of enzymatic method was only 6.5 hrs, significantly reduced from 24 hrs of the conventional method.

• Journal of Plant Biology
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• v.27 no.4
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• pp.241-251
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• 1984

The present study investigated the effects of triacontanol (TRIA) on plant growth and peroxisomal enzyme activities in radish seedlings. The optimum concentration of TRIA with respect to radish seedling bioassay was decided to 1.0mg $1^{-1}$. In comparison to untreated controls (including Tween 20 treatment), 1.0mg $1^{-1}$ TRIA treatment caused an increase in seed germination rate and root growth, but no stimulation in hypocotyl growth. Chlorophyll accumulation in cotyledon during carly development stage increased rapidly, and degradation of chlorophyll in later stage due to the cotyledon senesence was noticeably retarded. Increase of soluble protein content in cotyledon at early period of development was observed. Isocitrate lyase and catalase activity was not significantly different in both the treated and the untreated plants. But, glycolate oxidase activity was inhibited by TRIA down to 20% against controls. Also, the increase of the activity of peroxidase, a leaf-senescence marker enzyme, was continuously retarded over control for 8 days of development. Based on above results, TRIA was found to be active in both the growth and the peroxisomal enzyme activities of radish seedlings.