Ligninases fromChrysonilia sitophila (TFB-27441 strain)

Durán, Nélson; Ferrer, Irene; Rodrı́guez, Jaime

doi:10.1007/bf02798364

Cited by 27 publications

(4 citation statements)

References 26 publications

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“…In nature, lignin physically encrusts cellulose and is resistant to biodegradation (Kirk & Farrell 1987). Most active lignin degraders such as Phanerochaete chrysosporium, Phlebia radiata, Trametes versicolor, Bjerkandera adusta, Chrysonilia sitophila, Streptomyces badius and Streptomyces flavovirens belong to the basidiomycetes (Kirk & Farrell 1987;Blanchette 1991), though some of them are ascomycetes (Duran et al 1987) or actinomycetes (Crawford et al 1983;Ramachandra et al 1988). In fungi, the biodegradation of lignin is an enzymatic procedure.…”

Section: Introductionmentioning

confidence: 97%

Purification and characterization of lignin peroxidases from Penicillium decumbens P6

Yang

Yuan

Wang

et al. 2005

World J Microbiol Biotechnol

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Peroxidases are essential enzymes in biodegradation of lignin and lignite which have been investigated intensively in the white-rot fungi. This is the first report of purification and characterization of lignin peroxidase from Penicillium sp. P6 as lignite degradation fungus. The results indicated that the lignin peroxidase of Penicillium decumbens P6 had physical and chemical properties and a N-terminal amino acid sequence different from the lignin peroxidases of white-rot fungi. The lignin peroxidase was isolated from a liquid culture of P. decumbens P6. This enzyme had a molecular weight of 46.3 KDa in SDS-PAGE and exhibited greater activity, temperature stability and wider pH range than those previously reported. The isolation procedure involved (NH 4 ) 2 SO 4 precipitation, ion-exchange chromatography on DEAE-cellulose and CM-cellulose, gel filtration on Sephadex G-100, and non-denaturing, discontinuous polyacrylamide gel electrophoresis. The K m and V max values of this enzyme using veratryl alcohol as substrate were 0.565 mmol L )1 and 0.088 mmol (mg protein) )1 min )1 respectively. The optimum pH of P6 lignin peroxidase was 4.0, and 70.6% of the relative activity was remained at pH 9.0. The optimum temperature of the enzyme was 45°C.

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Section: Introductionmentioning

confidence: 97%

Purification and characterization of lignin peroxidases from Penicillium decumbens P6

Yang

Yuan

Wang

et al. 2005

World J Microbiol Biotechnol

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“…But traces of the typical structure of lignin can be found in certain coals. Lignin peroxidase is one of the lignolytic enzymes that was first found in the white rot fungus Phanerochaete chrysosporium (Glenn et al 1983;Tien and Kirk 1983) and later also isolated from other basidiomycete fungi like Phlebia radiata (Hatakka et al 1987), Trametes versicolor (Dodson et al 1987), Bjerkandera adusta (Kimura et al 1991), and Nematoloma frowardii and an ascomycete Chrysonilia sitophila (Duran et al 1987). Lignin peroxidase has broad substrate specificity and can act on both phenolic and nonphenolic compounds (Odier et al 1988;Schoemaker et al 1985).…”

Section: Lignin Peroxidasesmentioning

confidence: 99%

Microbe–Mineral Interactions: Exploring Avenues Towards Development of a Sustainable Microbial Technology for Coal Beneficiation

et al. 2015

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“…These oxidizing agents degrade the lignite by breaking the bonds between sub-units causing depolymerization of lignin (Tien and Kirk, 1983). Lignin peroxidase (Lip) is an important lignolytic enzyme which is found in Basidiomycetes fungi like Phanerochaete chrysosporium (Tien and Kirk, 1983), Phlebia radiate (Hatakka et al, 1987), Phlebia versicolor (Dodson et al, 1987) and one ascomycete Chrysosporium sitophila (Duran et al, 1987). Lip has an affinity for aromatic compounds and is oxidized to phenolic radicals (Odier et al, 1988), the latter is oxidized to aryl radicals (Schoemaker et al, 1985).…”

Section: Degradation Of Organic Compounds Of Coalmentioning

confidence: 99%

Biomethanization of Coal to Obtain Clean Coal Energy: A Review

Singh

2012

Energy Exploration & Exploitation

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This paper entails a review on the possibility of methanization of coal using microbial tool. Biomethanization process of coal begins with biodegradation of coal by specific bacteria and fungi. As a result of this, major polymers present in coal like proteins, polysaccharides, nucleic acids and lipids are hydrolyzed to monomers like aminoacids, sugars, purines, pyrimidines and long chain fatty acids. Their subsequent fermentation forms hydrogen, CO 2 and a number of reduced compounds like alcohols, short chain fatty acids, organic acids and certain aromatics. The oxidation of these reduced compounds further leads to the formation of acetate, hydrogen and CO 2 , methylated compounds and several intermediate compounds. Syntrophic relationship exists between fermenting bacteria and methanogens. The resultant oxidized compounds of fermenting bacteria are gradually utilized by specific methanogens to form methane. Hydrogenotrophic methanogens utilize H 2 and convert CO 2 into methane. Whereas acetate is utilized by acetoclastic methanogens to generate methane. The methylated compounds are utilized for methane formation by methylotrophic methanogens.

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Ligninases fromChrysonilia sitophila (TFB-27441 strain)

Cited by 27 publications

References 26 publications

Purification and characterization of lignin peroxidases from Penicillium decumbens P6

Purification and characterization of lignin peroxidases from Penicillium decumbens P6

Microbe–Mineral Interactions: Exploring Avenues Towards Development of a Sustainable Microbial Technology for Coal Beneficiation

Biomethanization of Coal to Obtain Clean Coal Energy: A Review

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