Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate

Leonowicz, Andrzej; Grzywnowicz, Krzysztof

doi:10.1016/0141-0229(81)90036-3

Cited by 363 publications

(164 citation statements)

References 11 publications

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“…The kinetic parameters for purified laccase were also measured with syringaldazine (525 nm; e 65 000 M 21 cm 21 ; Leonowicz & Grzywnowicz, 1981), 2,6-dimethoxyphenol (469 nm; e 49 600 M 21 cm 21 ; Wariishi et al, 1992), and guaiacol (465 nm; e 12 100 M 21 cm 21 ; Paszczynski et al, 1985) in 40 mM MES/NaOH buffer (pH 6). The Michaelis-Menten curves for determining K m and V max were obtained with the GraphPad Prism 3.02 program (GraphPad Software).…”

Section: Methodsmentioning

confidence: 99%

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

et al. 2004

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Previous studies on Melanocarpus albomyces laccase have shown that this enzyme is very interesting for both basic research purposes and industrial applications. In order to obtain a reliable and efficient source for this laccase, it was produced in the filamentous fungus Trichoderma reesei. Two approaches were used: production of a non-fused laccase and a hydrophobin-laccase fusion protein. Both proteins were expressed in T. reesei under the cbh1 promoter, and significantly higher activities were obtained with the non-fused laccase in shake-flask cultures (corresponding to about 230 mg l "1 ). Northern blot analyses showed rather similar mRNA levels from both expression constructs. Western analysis indicated intracellular accumulation and degradation of the hydrophobin-laccase fusion protein, showing that production of the fusion was limited at the post-transcriptional level. No induction of the unfolded protein response pathway by laccase production was detected in the transformants by Northern hybridization. The most promising transformant was grown in a fermenter in batch and fed-batch modes. The highest production level obtained in the fed-batch culture was 920 mg l "1 . The recombinant laccase was purified from the culture supernatant after cleaving the major contaminating protein, cellobiohydrolase I, by papain. The recombinant and wild-type laccases were compared with regard to substrate kinetics, molecular mass, pH optimum, thermostability, and processing of the N-and C-termini, and they showed very similar properties.

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Section: Methodsmentioning

confidence: 99%

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

et al. 2004

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“…A mistura reativa consistiu de 1,5 mL de tampão fosfato (100 mM, pH 6,5), 0,2 mL de siringaldazina (0,5 mM em solução etanólica) e 0,1 mL de filtrado da cultura. A oxidação do substrato após 5 minutos e a 30 °C foi estimada em 525 nm 17 .…”

Section: Determinação Das Atividades Enzimáticasunclassified

Aproveitamento do resíduo de laranja para a produção de enzimas lignocelulolíticas por Pleurotus ostreatus (Jack:Fr)

Alexandrino

Faria

Souza

et al. 2007

Ciênc. Tecnol. Aliment.

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“…Laccase activity was determined by the increase in the absorbance at λ = 525. This was due to the production of tetramethoxy-azo-bis-methylenequinone resulting from the reaction of laccase with syringaldazine [12], [13]. Protease activity was determined by mixing 0.5 ml of enzyme with 0.5 ml of 0.5% azocasein as the substrate.…”

Section: Enzymes Assaysmentioning

confidence: 99%

Treatment of Landfill Leachate Using Ganoderma Australe Mycelia Immobilized on Ecomat

Abdullah¹,

Razarinah²,

Mahmood³

et al. 2013

IJESD

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Abstract-Biological processes have been proven to be efficient in treating landfill leachates. In this study, treatment of landfill leachate by Ecomat-immobilized mycelia of Ganoderma australe packed in a column was investigated. Continuous recycling of leachate at a constant flow (20 ml/min) was operated for 10 cycles to facilitate biological reactions. Diluted leachate (50%) and raw leachate (100%) were tested for comparison of efficiency of treatment. The results showed that biological oxygen demand (BOD 5 ) was not removed for diluted leachate and a slight removal of 0.14 and 1.72% for raw leachate after cycles 4 and 10, respectively. Chemical oxygen demand (COD) removal occurred after each cycle with diluted leachate demonstrating higher removal compared to raw leachate. The highest percentage of COD removal of 51.62% for diluted leachate and 22.79% for raw leachate were achieved after the tenth cycle. Ecomat-immobilized mycelium of Ganoderma australe could also reduce ammoniacal nitrogen (NH 3 -N) exhibiting highest reduction of 45.95% and 30.90% after cycle 8 for diluted and raw leachate, respectively. These findings suggested that a white rot fungus, G. australe has the ability to be considered as potential candidate in landfill leachate treatment.Index Terms-Fungal enzymes, ammoniacal nitrogen, chemical oxygen demand, biological treatment, white-rot fungi.

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Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate

Cited by 363 publications

References 11 publications

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

Aproveitamento do resíduo de laranja para a produção de enzimas lignocelulolíticas por Pleurotus ostreatus (Jack:Fr)

Treatment of Landfill Leachate Using Ganoderma Australe Mycelia Immobilized on Ecomat

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