Purification of the major endoglucanase from <i>Aspergillus fumigatus</i> Fresenius

Parry, Jocelyn B.; Stewart, James J. P.; Heptinstall, John

doi:10.1042/bj2130437

Cited by 32 publications

(9 citation statements)

References 24 publications

(28 reference statements)

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“…4b). These results suggest that our enzyme was stable up to 60°C and above this temperature; a rapid decrease in stability takes place particularly after incubation for 1 h. On the other hand, endoglucanase from A. niger (Parry et al 1983) and Bacillus strains CH43 and HR68 (Mawadza et al 2000) was reported to be stable up to 50°C.…”

Section: Effect Of Temperature On Enzyme Activity and Stabilitymentioning

confidence: 77%

Purification and characterization of an acidothermophilic cellulase enzyme produced by Bacillus subtilis strain LFS3

Rawat

Tewari

2012

Extremophiles

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In the present investigation, a microorganism hydrolyzing carboxymethylcellulose (CMC) was isolated and identified as Bacillus subtilis strain LFS3 by 16S rDNA sequence analysis. The carboxymethylcellulase (CMCase) enzyme produced by the B. subtilis strain LFS3 was purified by (NH₄)₂SO₄ precipitation, ion exchange and gel filtration chromatography, with an overall recovery of 15 %. Native-PAGE analysis of purified CMCase revealed the molecular weight of enzyme to be about 185 kDa. The activity profile of CMCase enzyme showed the optimum activity at temperature 60 °C and pH 4.0, respectively. The enzyme activity was induced by Na⁺, Mg²⁺, NH₄⁺, and EDTA, whereas strongly inhibited by Hg²⁺ and Fe³⁺. The purified enzyme hydrolyzed CMC, filter paper, and xylan, but not p-nitrophenyl β-D-glucopyranoside and cellulose. Kinetic analysis of purified enzyme showed the K(m) value of 2.2 mg/ml. Thus, acidophilic as well as thermophilic nature makes this cellulase a suitable candidate for current mainstream biomass conversion into fuel and other industrial processes.

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Section: Effect Of Temperature On Enzyme Activity and Stabilitymentioning

confidence: 77%

Purification and characterization of an acidothermophilic cellulase enzyme produced by Bacillus subtilis strain LFS3

Rawat

Tewari

2012

Extremophiles

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“…Aspergillus sp. is known to produce a variety of cellulolytic enzymes including endo-β-1,4-glucanase or CMCase [31,36,37]. In the present work, different trials were conducted to purify the crude EG produced by A. terreus DSM 826.…”

Section: Discussionmentioning

confidence: 99%

Purification and properties of an endoglucanase of Aspergillus terreus DSM 826

Elshafei

Hassan

Haroun

et al. 2009

J. Basic Microbiol.

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Endoglucanase (EG) from A. terreus DSM 826 grown on sugar cane bagasse as a carbon source was purified using acetone fractionation, then a Sepharose-4B chromatographic column, with purification of about 27-fold and 10.5% recovery. The optimum temperature and pH for activity of the purified EG were found to be 50 degrees C and pH 4.8, respectively. The purified enzyme can stand heating up to 50 degrees C for 1 h without apparent loss of activity. However, the enzyme, incubated at 80 degrees C for 5 min, showed about 56% loss of activity. Optimum EG activity was recorded with a citrate buffer system (pH 4.8; 0.05 M). Co2+ (2.5 x 10(-2) M) and Zn2+ (5 x 10(-2) M) were found to activate the purified EG of A. terreus DSM 826 by about 83 and 25%, respectively. On the other hand, Hg2+ inhibited the activity of the purified EG by about 50 and 71% at a concentration of 2.5 x 10(-2) and 5 x 10(-2) M, respectively. Carboxymethyl cellulose was found to be the best substrate for the purified EG, with V(max) values of 4.35 micrpmol min(-1) mg(-1) protein.

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“…A maximum decrease of the enzyme activity was recorded when heating the enzyme at 90°C for 30 min. Endoglucanase from A. fumigatus was reported to be stable at 50°C (Parry et al, 1983). This comparison shows that the heat stability of CMCase from A. oryzae is higher than that of the enzyme mention previously.…”

Section: Thermal Stabilitymentioning

confidence: 65%

“…The optimal pH for endoglucanase from Aspergillus niger was found to be 6.0 to 7.0 (Parry et al, 1983). Akiba et al (1995) reported that cellulase production was high at pH 4.0 and pH 4.5 by A. niger.…”

Section: Effect Of Ph On the Production Of Cellulolytic Enzymesmentioning

confidence: 99%

Physiological studies of cellulase complex enzymes of Aspergillus oryzae and characterization of carboxymethyl cellulase

Youssef¹

2011

Afr. J. Microbiol. Res.

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Investigation of the production of cellulase complex enzymes by the fungus Aspergillus oryzae on soluble bio-cellulosic waste like cheese whey was the goal of this work. The effects of incubation period, substrate concentration, initial pH and temperature on the production of endoglucanase, exoglucanase and cellulase (filter paper activity FPA) activities, were investigated. Seven days incubation period with an initial pH value of 6 and temperature of 40°C, and cheese whey concentration of 10% yielded the highest specific activities with 1.5 fold increases for endoglucanase and 1.4 fold increases for exoglucanase. Cellulase specific activity represented as FPA showed no fold increase at all. The optimum temperature of endoglucanase was observed at 55°C, and the enzyme activity has abroad pH range between 3.8 to 8.0 and 24.91% of the original activity was retained after heat treatment at 90C for 30 min. Analysis of the partial purified enzyme preparation by SDS -PAGE revealed one protein band showing cellulolytic activity, The molecular weight of this band was estimated to be around 45.000 Daltons.

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Purification of the major endoglucanase from Aspergillus fumigatus Fresenius

Cited by 32 publications

References 24 publications

Purification and characterization of an acidothermophilic cellulase enzyme produced by Bacillus subtilis strain LFS3

Purification and characterization of an acidothermophilic cellulase enzyme produced by Bacillus subtilis strain LFS3

Purification and properties of an endoglucanase of Aspergillus terreus DSM 826

Physiological studies of cellulase complex enzymes of Aspergillus oryzae and characterization of carboxymethyl cellulase

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