Temperature effect in the production of multiple xylanases by Aspergillus fumigatus

Lenartovicz, Veridiana; Souza, Cristina Giatti Marques de; Moreira, Fabiana Guillen; Peralta, Rosane Marina

doi:10.1002/1521-4028(200212)42:6<388::aid-jobm388>3.0.co;2-h

Cited by 21 publications

(10 citation statements)

References 15 publications

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“…The optimized xylanase activity was higher than that reported for A. nidulans KK-99 (40 IU/mL), 28) Penicillium oxalicum (14.5 IU/mL), 29) and Chaetomium thermophilum (61 IU/mL), 30) and comparable to that from A. fumigatus (125.1 IU/mL). 31) The optimized operational parameters by CCD were then applied in a laboratory scale-up in 8-liter batch fermentation. A significant increase in xylanase activity was observed for the bioreactor which resulted in 106.2 IU/mL of xylanase after fermentation for 5 d. This might have been due to improved correlate morphology and engineering parameters such as quality of mixing, oxygen transfer rate, volumetric oxygen, and heat transfer coefficients during filamentous fermentation in the large-scale bioreactor system.…”

Section: Resultsmentioning

confidence: 99%

Optimization of Xylanase Production fromAspergillus nigerfor Biobleaching of Eucalyptus Pulp

Khonzue¹,

Laothanachareon²,

Rattanaphan³

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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A crude endo-xylanase produced by Aspergillus niger BCC14405 was investigated for its potential in pre-bleaching of chemical pulp from eucalyptus. The optimal fermentation conditions on the basis of optimization using response surface methodology included cultivation in a complex medium comprising wheat bran, rice bran, and soybean meal supplemented with yeast extract, glucose, peptone, and lactose with a starting pH of 6.0 for 7 d. This resulted in production of 89.5 IU/mL of xylanase with minor cellulase activity. Proteomic analysis using LC/MS/MS revealed that the crude enzyme was a composite of hemicellulolytic enzymes, including endo-β-1,4-xylanase and other hemicellulolytic enzymes attacking arabinoxylan and mannan. Pretreatment of the pulp at a xylanase dosage of 10 IU/g increased the brightness ceiling after the C-Eop-H bleaching step up to 3.0% using a chlorine charge with a C-factor of 0.16-0.20. Xylanase treatment also led to reduction in chlorine charge of at least 20%, with an acceptable brightness level. The enzyme pretreatment resulted in a slight increase in pulp viscosity, suggesting an increase in relative cellulose content. The crude enzyme was potent in the enzyme-aided bleaching of chemical pulp in an environmentally friendly pulping process.

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Section: Resultsmentioning

confidence: 99%

Optimization of Xylanase Production fromAspergillus nigerfor Biobleaching of Eucalyptus Pulp

Khonzue¹,

Laothanachareon²,

Rattanaphan³

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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“…The highest xylanase production with wheat bran was possible because this substrate is rich in proteins and hemicelluloses, which are used by microorganisms as sources of energy and carbon, through specific enzymes such as xylanase. Wheat bran, among other substrates used in solid systems, is the most efficient, because it does not perform catabolic repression on the enzymatic activity (LENARTOVICZ et al, 2002).…”

Section: Resultsmentioning

confidence: 99%

“…Xylanase is one of the microbial extracellular enzymes that has attracted great interest due to its biotechnological potential in many industrial processes, e.g., in the production of oligosaccharides (PELLERIN et al, 1991); in the food industry (HALTRICH et al, 1996); cellulose and paper industry (YAUN; RUGYU, 1999); xylitol and ethanol production (BEG et al, 2001); cellular proteins, liquid fuels, and other chemical substances (CHAN et al, 2002). Xylanases catalyze xylan hydrolysis, and many environmental factors affect production of these enzymes, but carbon source can induce or repress the catabolic activity of them, which can this enzyme biosynthesis, such as: temperature and cultivation time (HALTRICH et al, 1996); and substrate used (LENARTOVICZ et al, 2002;.…”

Section: Introductionmentioning

confidence: 99%

Biomasses and Xylanase Production by Strains of Penicillium Isolated From Brazilian Atlantic Forest

2009

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Six Penicillium strains were isolated from soil at a depth of 0 15 cm in the Juréia-Itatins Ecology Station (JIES), in the São Paulo State, Brazil. They were evaluated for xylanase production under different temperatures and carbon sources. The best carbon source and temperature were first determined in an automated Bioscreen C system, verifying the growth of microorganisms. Liquid media containing tap water with 2% carbohydrate and/or 1% nitrogen sources were used. Afterwards, Penicillium citrinum, P. fellutanum, P. rugulosum and P. decumbens were cultivated in 250 mL Erlenmeyer flasks with 50 mL of culture medium containing tap water sole 2% carbon source (fructose, glucose, mannitol, sucrose or xylose) and 1% yeast extract as a nitrogen source at pH 5.0 and 28o C, with agitation of 150 rpm for 72 hours. These same strains, except P. decumbens, and P. purpurogenum were cultivated in solid substrate with wheat bran under the same environmental conditions to study the potential of xylanase activity. Maximum xylanase activity was observed in cultures with wheat bran, without the addition of any other carbon source, using inocula containing 1 x 107 spores.mL-1 (28o C, pH 5.0, 72 h). It can be concluded that P. fellutanum and P. citrinumare a good xylanase producers under the conditions of 28º C. The results of xylanase activity were 54% less at 28º C in liquid cultures media cultures than in solid substrate.

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“…High molecular weight xylanases of above 200 kDa were reported from Aspergillus fumigatus AR1 (Anthony et al 2003). Lenartovicz et al (2002) reported presence of both high molecular (45.7 & 39.8 kDa) and low molecular weight (18.2 kDa) xylanases from Aspergillus fumigatus.…”

Section: Introductionmentioning

confidence: 98%

Purification and characterization of a high molecular weight endoxylanase from the solid-state culture of an alkali-tolerant Aspergillus fumigatus MKU1

Thiagarajan

Jeya

Gunasekaran

2005

World J Microbiol Biotechnol

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A high molecular weight endoxylanase (XylF2) from the solid state culture of Aspergillus fumigatus MKU1 was purified to homogeneity by a combination of tube gel electrophoresis and electroelution methods. The purity was demonstrated by SDS-PAGE and the molecular mass of the XylF2 was found to be 66 kDa. The optimal pH and temperature for activity were 5.0 and 90°C, respectively. The apparent K m and V max values of XylF2 with oat spelt xylan as substrate were 1.6 mg/ml and 3.25 mmol/min/mg protein respectively. The enzyme showed high activity towards oat spelt xylan while negligible activity was observed on carboxymethylcellulose. The activity of XylF2 was strongly inhibited by Hg 2+ , Ni 2+ , Zn 2+ , SDS and N-bromosuccinimide and stimulated by L-cysteine and iodoacetamide. The hydrolysis of oat spelt xylan by XylF2 released only xylo-oligosaccharides.

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Temperature effect in the production of multiple xylanases by Aspergillus fumigatus

Cited by 21 publications

References 15 publications

Optimization of Xylanase Production fromAspergillus nigerfor Biobleaching of Eucalyptus Pulp

Optimization of Xylanase Production fromAspergillus nigerfor Biobleaching of Eucalyptus Pulp

Biomasses and Xylanase Production by Strains of Penicillium Isolated From Brazilian Atlantic Forest

Purification and characterization of a high molecular weight endoxylanase from the solid-state culture of an alkali-tolerant Aspergillus fumigatus MKU1

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