Peroxidase production by carbon and nitrogen sources fed-batch culture of Arthromyces ramosus

Tsujimura, Hideo; Takaya, Masamitsu; Katano, Kenji; Matsumoto, Nobuya; Park, Yong Soo; Okabe, Mitsuyasu

doi:10.1007/bf00128603

Cited by 4 publications

(3 citation statements)

References 5 publications

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“…Most white rot fungi, including Phanerochaete chrysosporium, start lignin degradation when nitrogen, carbon, or sulfur becomes limiting (12). Peroxidase production from Arthromyces ramosus is greatest when glucose and yeast extract or polypeptone are added at a ratio of 3:5 (41). The production of manganese peroxidase by the white rot fungus Lentinus edodes is suppressed by a high nitrogen concentration in the medium, whereas under these conditions laccase production reached its maximum level (3).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Laccases and Peroxidases from Wood-Rotting Fungi (FamilyCoprinaceae)

Heinzkill

Bech

Halkier

et al. 1998

Appl Environ Microbiol

259

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Panaeolus sphinctrinus, Panaeolus papilionaceus, and Coprinus friesii are described as producers of ligninolytic enzymes. P. papilionaceus andP. sphinctrinus both produced a laccase. In addition,P. sphinctrinus produced a manganese peroxidase. C. friesii secreted a laccase and two peroxidases similar to the peroxidase of Coprinus cinereus. The purified laccases and peroxidases were characterized by broad substrate specificities, significant enzyme activities at alkaline pH values, and remarkably high pH optima. The two peroxidases of C. friesii remained active at pH 7.0 and 60°C for up to 60 min of incubation. The peroxidases were inhibited by sodium azide and ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA), whereas the laccases were inhibited by sodium azide andN,N-diethyldithiocarbamic acid. As determined by native polyacrylamide gel electrophoresis and isoelectric focusing, all three fungi produced laccase isoenzymes.

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Section: Discussionmentioning

confidence: 99%

Characterization of Laccases and Peroxidases from Wood-Rotting Fungi (FamilyCoprinaceae)

Heinzkill

Bech

Halkier

et al. 1998

Appl Environ Microbiol

259

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“…Nidadavolu et al, (2010) were found that the best extraction ratio for peroxidase from discarded mushroom beds was 1:1 and 1:2. While (Tsujimura et al, 1994), shown the best ratio was 1:5 for peroxidase extraction from Arthromyces ramosus.s…”

Section: The Optimum Ratio Of Peroxidase Extractionmentioning

confidence: 96%

Characterization and Immobilization of Peroxidase Extracted from Horse Radish and Decolorization of Some Dyes

Sa'ady¹,

Bahrani²,

Aziz³

2018

Int.J.Curr.Microbiol.App.Sci

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“…Nidadavolu et al, (2010) 23 were found that the best extraction ratio for peroxidase purified from discarded mushroom beds was 1:1 and 1:2. While Tsujimura et al,(1994) 24 extracted peroxidase from Arthromycesramosus with 1:5 ratio.…”

Section: The Optimum Ratio Of Peroxidase Extractionmentioning

confidence: 99%

Extraction, and Purification of Peroxidase Enzyme from Peganum harmala Seeds

Al-Mentafji¹,

Al-Fahdawi²,

Al-farras³

2019

ijddt

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The aim of this study was to extract peroxides enzyme from Peganum harmala seeds; peroxides was extracted by using different extraction buffer solutions, then it was purified by three steps of purification includes precipitation with ammonium sulfate in a saturation ratio of 70 %, ion exchange chromatography through DEAE-Cellulose, and gel filtration chromatography throughout Sephadex G-100, and determine the optimum condition for extraction. This was performed by controlling the type and concentration of buffer, pH of the buffer used, and the ratio of extraction. The Sodium acetate buffer with 0.2mM and pH 5.0 was found to be the best buffer for the extraction of peroxidase. By using the extraction ratio for a plant of 1:3 (W/V), the specific activity was 195 U/mg protein. These three purification steps raised the specific activity to 235U/mg protein in the precipitation step with purification fold 2.3 and enzyme recovery 69%; the specific activity was increased to 243U/mg protein in Ion exchange step with purification fold 2.4 and enzyme recovery 23%, also the specific activity doubled after gel filtration step to 447U/mg protein with purification fold 4.4 and enzyme recovery 15%.

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Peroxidase production by carbon and nitrogen sources fed-batch culture of Arthromyces ramosus

Cited by 4 publications

References 5 publications

Characterization of Laccases and Peroxidases from Wood-Rotting Fungi (FamilyCoprinaceae)

Characterization of Laccases and Peroxidases from Wood-Rotting Fungi (FamilyCoprinaceae)

Characterization and Immobilization of Peroxidase Extracted from Horse Radish and Decolorization of Some Dyes

Extraction, and Purification of Peroxidase Enzyme from Peganum harmala Seeds

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