Purification and Some Physical Properties of Acid-cellulase from Aspergillus niger

Ikeda, Ryoko; Yamamoto, Tatsuto; Funatsu, Masaru

doi:10.1271/bbb1961.37.1153

Cited by 11 publications

(2 citation statements)

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“…Temperature and pH are the two important ambient factors that can directly influence the cellulase stability. In the production of cellulose enzyme bacteria, such as A. niger (Ikeda et al, 1973;Sohail et al., 2009) and Trichoderma reesei (Sprey and Lambert, 1983;Szengyel and Zacchi 2000), the acid enzyme is commonly produced, for which the optimal pH has typically been between 4.0 and 6.0. Some microbes also exhibit basophil and alkali resistance (Ariffin et al, 2006;Singh et al, 2004).…”

Section: Stability Of Cellulasementioning

confidence: 99%

Characteristics of cellulase in cellulose-degrading bacterium strain Clostridium straminisolvens (CSK1)

Wang¹,

Hua²,

Wang³

et al. 2017

Afr. J. Microbiol. Res.

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Microbial degradation of biomass was considered as a clean and highly efficient approach to produce bioenergy, as it could mitigate the urgent demand for limited petroleum and natural gas. A thermophilic microbial consortium (MC1) was proved a high efficiency cellulose-degrading bacterial community in previous studies. A novel anaerobic, thermophilic, and cellulolytic bacterium (strain CSK1) was isolated from MC1. The cellulase activity characteristics of CSK1 were analyzed and evaluated by exploring new measuring conditions via the 3,5-dinitrosalicylic acid (DNS) spectrophotometry and the carboxymethyl cellulose (CMC) saccharogenic power method. The results indicated that the optimal measuring wavelength, reaction temperature, and pH value, were 530 nm, 60°C and 6.0, respectively. The ideal reaction time to achieve stable and significant measuring cellulase activity was about 10 min. Cellulase of CSK1 remained stable when the temperature was below 70°C, and the pH between 5.0 and 10.0, and its activity was quickly reduced when the temperature and pH exceeded such ranges. The cellulase activity of CSK1 reached the highest level on culturing day 8, and high correlations were found among cellulase activity variation, pH and CSK1 biomass change.

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Section: Stability Of Cellulasementioning

confidence: 99%

Characteristics of cellulase in cellulose-degrading bacterium strain Clostridium straminisolvens (CSK1)

Wang¹,

Hua²,

Wang³

et al. 2017

Afr. J. Microbiol. Res.

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“…IKEDA et al (24) and very recently HURST et al (20) have isolated two different A. niger endo-l,4-13-glucanases in homogeneous form. The only other highly purified A. niger endo-l,4-13-glucanase tested on a mixed-linked 13-glucan was described by CLARKE and STONE (7), but the physico-chemical and chemical properties of this enzyme preparation have not been examined.…”

Section: Introductionmentioning

confidence: 99%

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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Effect of chemical modification of cellulose on the activity of a cellulase from Aspergillus niger

Boyer

Redmond

1983

Biotech & Bioengineering

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Five chemically modified forms of cellulose were prepared, characterized, and tested as substrates for a homogeneous glucanohydrolase from A. niger. The relative order of reactivity at pH 4.0 was DEAE = PEI > benzyl DEAE > cellulose > P > CM.The following abbreviations are used throughout the article: (RBB) Remazol brilliant blue R; (DEAE) diethylamino ethyl; (PEI) polethyleneimine; (CM) carboxymenthyl; (P) phospho; (DS) degree of RBB dye substitution of cellulose, in mol dye/100 glucose. This indicates that positively charged cellulose substrates are more susceptible to hydrolysis by the cellulase. This observation strengthens an earlier proposal that caroxyl groups on the enzyme are involved in substrate binding and catalytic action. Chemical modification is suggested as a method to increase the rate of enzymatic hydrolysis of cellulose, a process now in the commercial development stage.

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Purification and Some Physical Properties of Acid-cellulase from Aspergillus niger

Cited by 11 publications

References 0 publications

Characteristics of cellulase in cellulose-degrading bacterium strain Clostridium straminisolvens (CSK1)

Characteristics of cellulase in cellulose-degrading bacterium strain Clostridium straminisolvens (CSK1)

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

Effect of chemical modification of cellulose on the activity of a cellulase from Aspergillus niger

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