Extracellular Enzyme System Utilized by the Fungus<i>Sporotrichum pulverulentum (Chrysosporium lignorum)</i>for the Breakdown of Cellulose

Almin, K. E.; Eriksson, Karl‐Erik; Pettersson, B.

doi:10.1111/j.1432-1033.1975.tb03920.x

Cited by 58 publications

(7 citation statements)

References 14 publications

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“…The turnover numbers of the pea enzyme on barley 13-glucan and CM-cellulose are identical and are an order of magnitude higher than the value obtained for the A. niger enzyme using barley 13-glucan as substrate. The molecular activity of the A. niger enzyme on the mixed-linked substrate is similar to the values found for some of the Sporotrichum pulverulentum endo-l,4-13-glucanases acting on CM-cellulose (2).…”

Section: Discussionsupporting

confidence: 60%

Purification of a fungal endo-β-glucanase with high activity on barley β-glucan

Svensson

1978

Carlsberg Res. Commun.

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An endo-13-glucanase was purified from a commercial enzyme preparation of fungal origin by ammonium sulphate fractionation, ion exchange chromatography, and gel filtration followed by preparative isoelectric focusing. The enzyme was homogeneous in sedimentation equilibrium analysis from which the molecular weight was determined to be 23.500 in agreement with the value 23.653 calculated on the basis of the amino acid composition. The enzyme did not contain carbohydrate and a molecular weight of 24.000 estimated by polyacrylamide gel electrophoresis in dodecyl sulphate after 2-mercaptoethanol treatment, indicated that it consisted of a single polypeptide chain. It had an isoelectric point of 4.47. The enzyme rapidly decreased the specific viscosity of barley fl-glucan with a small concomitant increase in reducing sugar. Its activity toward carboxymethyl-cellulose, acid-swollen cellulose, and a mixture of cellodextrins was low. Laminarin, carboxymethyl-pachyman, cellobiose, and p-nitrophenyl-13-D-glucoside were not hydrolyzed. The Km for hydrolysis of barley 13-glucan and carboxymethyl-cellulose was 1.8 and I 1 mg/ml, respectively, the corresponding molecular activities being 7750 and 750 equivalents of glucosidic bonds hydrolyzed per min per mole of enzyme. The products of exhaustive hydrolysis of barley !%glucan were 4.3% glucose, 4.2% disaccharide, 72.7% trisaccharide, and 18.8% tetrasaccharide, higher oligomers and polymers were absent. The enzymic activity was completely destroyed by treatment with N-bromosuccinimide but was insensitive to EDTA, sulfhydryl modifying reagents, and glucono-l,5-1actone.

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Section: Discussionsupporting

confidence: 60%

Purification of a fungal endo-β-glucanase with high activity on barley β-glucan

Svensson

1978

Carlsberg Res. Commun.

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“…Eight different types of fermentation media, (M-I to M-VIII) already reported by Eggins and Pugh (1962), Mandel and Reese (1960), Romanelli et al (1975), Coutts and Smith (1976), Saddler (1982), Macris and Panayatou (1989), Almin et al (1975) and Riou et al (1998) respectively, were screened for the production of β-glucosidase. Different carbon sources, for example, carboxymethyl cellulose (CMC), cellulose powder, lactose, maltose, sucrose, wheat bran and cellobiose (1%, w/v) were added to fermentation medium to test their effect on enzyme production.…”

Section: Optimization Of Fermentation Parametersmentioning

confidence: 99%

Metabolic engineering and thermodynamic characterization of an extracellular -glucosidase produced by Aspergillus niger

Zahoor¹,

Javed²,

Aftab³

et al. 2011

Afr. J. Biotechnol.

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The production of an extracellular β-glucosidase by Aspergillus niger NRRL 599 was optimized using submerged fermentation technique. Effect of different media, different carbon sources, initial pH of the fermentation medium, temperature, incubation period and inoculum size on the production of β-glucosidase enzyme was investigated. A. niger NRRL 599 produced maximum extracellular β-glucosidase (4.48 U/mg) in Eggins and Pugh medium with 1% wheat bran (w/v) at pH 5.5 inoculated with 4% conidial suspension after 96 h of incubation at 30°C. Purified β-glucosidase gave K m and V max values of 3.11 mM and 20.83 U/mg respectively for pNPG hydrolysis. The enzyme was optimally active at pH 4.8 and at temperature of 60°C. Thermodynamic parameters, E a , ∆H and ∆S were found to be 52.17 KJ/mol, 49.90 J/mol.K and -71.69 KJ/mol, respectively. The pKa 1 and pKa 2 of ionizable groups of active site residues involved in V max were calculated to be 4.1 and 6.0 respectively.

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“…However, the wood-rotting fungus Phanerochaete chrysosporium is able to efficiently degrade lignocellulose, and it secretes an array of enzymes that hydrolyze cellulose and hemicellulose (1,5,6,12,13,41). The culture filtrate of P. chrysosporium grown in the presence of cellulose contains CBHs belonging to GH families 6 and 7 (43) and four EGs in GH families 5 and 12 (15,42), suggesting that the basidiomycete has a cellulolytic system that is similar to that of ascomycetes.…”

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confidence: 99%

Characterization of an Endoglucanase Belonging to a New Subfamily of Glycoside Hydrolase Family 45 of the BasidiomycetePhanerochaete chrysosporium

Igarashi

Ishida

Hori

et al. 2008

Appl Environ Microbiol

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The wood decay fungus Phanerochaete chrysosporium has served as a model system for the study of lignocellulose conversions, but aspects of its cellulolytic system remain uncertain. Here, we report identifying the gene that encodes the glycoside hydrolase (GH) family 45 endoglucanase (EG) from the fungus, cloning the cDNA, determining its heterologous expression in the methylotrophic yeast Pichia pastoris, and characterizing the recombinant protein. The cDNA consisted of 718 bp, including an open reading frame encoding a 19-amino-acid signal peptide, a 7-amino-acid presequence at the N-terminal region, and a 180-amino-acid mature protein, which has no cellulose binding domain. Analysis of the amino acid sequence revealed that the protein has a low similarity (<22%) to known fungal EGs belonging to the GH family 45 (EGVs). No conserved domain of this family was found by a BLAST search, suggesting that the protein should be classified into a new subdivision of this GH family. The recombinant protein has hydrolytic activity toward amorphous cellulose, carboxylmethyl cellulose, lichenan, barley ␤-glucan, and glucomannan but not xylan. Moreover, a synergistic effect was observed with the recombinant GH family 6 cellobiohydrolase from the same fungus toward amorphous cellulose as a substrate, indicating that the enzyme may act in concert with other cellulolytic enzymes to hydrolyze cellulosic biomass in nature.

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Extracellular Enzyme System Utilized by the FungusSporotrichum pulverulentum (Chrysosporium lignorum)for the Breakdown of Cellulose

Cited by 58 publications

References 14 publications

Purification of a fungal endo-β-glucanase with high activity on barley β-glucan

Purification of a fungal endo-β-glucanase with high activity on barley β-glucan

Metabolic engineering and thermodynamic characterization of an extracellular -glucosidase produced by Aspergillus niger

Characterization of an Endoglucanase Belonging to a New Subfamily of Glycoside Hydrolase Family 45 of the BasidiomycetePhanerochaete chrysosporium

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