Production, purification and characterization of a minor form of xylanase from Aspergillus versicolor

Carmona, Eleonora Cano; Fialho, Mauricio Batista; Buchgnani, Érika Bicalho; Coelho, Glauciane Danusa; Brocheto-Braga, Márcia Regina; Jorge, João Atı́lio

doi:10.1016/j.procbio.2004.01.010

Cited by 56 publications

(45 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…3b) of the PXII-1 preparation showed the presence of a hydrolysis zone that was coincident to the single PXII-1 protein band. The A. versicolor II 32 6.0-7.0 55 [13] A. awamori 2B.361 U2/1 PXII-1 32.87 5.0-5.5 50 Present work homogeneity of this preparation was further confirmed by mass spectrometry (MALDI-TOF), which showed a unique protein peak with a molecular mass of 32.87 kDa, a value that compares well to previously reported data on Aspergillus xylanases ( Table 3). The molecular mass of PXII-1 xylanase was within the range detected for xylanases belonging to the G/11 family [62].…”

Section: Sds-page and Mass Spectrometry Analysissupporting

confidence: 88%

“…The culture filtrate was fractionated by ultrafiltration, and the 100-kDa retentate was applied to the column. The xylanase activity peak and the corresponding PXI protein fractions are also shown result is consistent with the substrate specificity of purified xylanases from A. versicolor [12,13], A. caespitosus [54], and A. fischeri [51].…”

Section: Xylanase Substrate Specificity and Kinetic Parameterssupporting

confidence: 83%

“…The effects of amino acid-modifying agents, amino acids, chloride ions, sulfate ions, and EDTA on PXII-1 xylanase activity are shown in Tables 5 and 6. The presence of L-tryptophan in the reaction mixture increased xylanase activity by 37%, and a similar increase was observed for cysteine, confirming the presence of reduced thiol (cysteine) in the enzyme structure [13]. Similar results were found in the characterization of xylanase from Acrophialophora nainiana [65], which was demonstrated to be activated by cysteine and tryptophan; Clostridium thermocellum [64], which is activated by cysteine, tryptophan, and DTT; Penicillium capsulatum [25], which is activated by cysteine and DTT; Aspergillus niger, Penicillium corylophilum and Trichoderma longibrachiatum [11], which are activated by 9.3 mM of cysteine and tryptophan; and Trichoderma harzianum [24], which is activated by 20 mM of cysteine and DTT.…”

Section: Xylanase Hydrolytic Profilesupporting

confidence: 69%

“…The overall data for the apparent K m indicate that A. awamori xylanase shows higher affinity for the less branched birchwood xylan, which contains 90% xylose [51], in comparison to oat-spelt xylan, which contains 75% xylose, 10% arabinose, and 15% glucose [19]. However, the K m value of the PXII-1 preparation was higher in comparison with other Aspergillus-purified xylanases, such as that from A. fischeri (K m 4.88 mg/ml) [51], A. caespitosus (K m 3.9 mg/ml) [54] and A. ficuum AF-98 (K m 3.75 mg/ml) on birchwood xylan [23] and A. versicolor (K m 2.3 mg/ml) on oat-spelt xylan [13]. Xylanase PXII-1 also showed the highest K cat and K cat /K m values towards untreated birchwood xylan.…”

Section: Xylanase Substrate Specificity and Kinetic Parametersmentioning

confidence: 95%

“…, whereby a 64% increase in activity was observed. Carmona et al [13] reported that the presence of 10 mM Mn 2? stimulated the activity of purified xylanase from Aspergillus versicolor in more than 100% of activity.…”

Section: Xylanase Hydrolytic Profilementioning

confidence: 99%

See 4 more Smart Citations

Purification and characterization studies of a thermostable β-xylanase from Aspergillus awamori

Teixeira

Siqueira

Souza

et al. 2010

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

This study presents data on the production, purification, and properties of a thermostable β-xylanase produced by an Aspergillus awamori 2B.361 U2/1 submerged culture using wheat bran as carbon source. Fractionation of the culture filtrate by membrane ultrafiltration followed by Sephacryl S-200 and Q-Sepharose chromatography allowed for the isolation of a homogeneous xylanase (PXII-1), which was 32.87 kDa according to MS analysis. The enzyme-specific activity towards soluble oat spelt xylan, which was found to be 490 IU/mg under optimum reaction conditions (50°C and pH 5.0-5.5), was 17-fold higher than that measured in the culture supernatant. Xylan reaction products were identified as xylobiose, xylotriose, and xylotetraose. K (m) values (mg ml(-1)) for soluble oat spelt and birchwood xylan were 11.8 and 9.45, respectively. Although PXII-1 showed 85% activity retention upon incubation at 50 °C and pH 5.0 for 20 days, incubation at pH 7.0 resulted in 50% activity loss within 3 days. PXII-1 stability at pH 7.0 was improved in the presence of 20 mM cysteine, which allowed for 85% activity retention for 25 days. This study on the production in high yields of a remarkably thermostable xylanase is of significance due to the central role that this class of biocatalyst shares, along with cellulases, for the much needed enzymatic hydrolysis of biomass. Furthermore, stable xylanases are important for the manufacture of paper, animal feed, and xylooligosaccharides.

show abstract

Section: Sds-page and Mass Spectrometry Analysissupporting

confidence: 88%

Section: Xylanase Substrate Specificity and Kinetic Parameterssupporting

confidence: 83%

Section: Xylanase Hydrolytic Profilesupporting

confidence: 69%

Section: Xylanase Substrate Specificity and Kinetic Parametersmentioning

confidence: 95%

Section: Xylanase Hydrolytic Profilementioning

confidence: 99%

See 3 more Smart Citations

Purification and characterization studies of a thermostable β-xylanase from Aspergillus awamori

Teixeira

Siqueira

Souza

et al. 2010

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

Statistical optimization and kinetic modeling of xylanase production by Arthrobacter sp.

Aravindan

Selvaraj

Viruthagiri

2008

Asia-Pacific J Chem Eng

View full text Add to dashboard Cite

Xylanases are hydrolytic enzymes which randomly cleave the β-1, 4 backbone of the complex plant cell wall polysaccharide xylan. Diverse forms of these enzymes exist, displaying varying folds, mechanisms of action, substrate specificities, hydrolytic activities, and physicochemical characteristics. This article focuses on the fermentative production of xylanase from Arthrobacter sp. and the factors affecting the production. The batchsubmerged fermentation was carried out in a 250-ml Erlenmeyer flask. The inoculum size of 5% v/v, initial pH of 7.0, and shaking speed of 150 rpm at 32 • C were maintained for the optimization of medium components. The cell growth, xylanase activity, cellulase activity, protein, and pH were determined at regular time intervals. Plackett-Burman statistical methodology was adopted to study the effect of media components on xylanase production. The effect of temperature and pH was studied using optimized medium composition determined by Plackett-Burman experimental design. The maximum xylanase activity of 4.0 U ml −1 at 84 h at the optimum temperature of 35 • C and pH of 7.0 was obtained. 

show abstract

Purification and characterization of an alkaliphilic endo‐xylanase from Streptomyces althioticusLMZM and utilization in the pulp paper industry

Luo

Wang

Lin

et al. 2015

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND: Xylanase is the key enzyme involved in the conversion of lignocelluloses.RESULTS: An extracellular xylanase from Streptomyces althioticus LMZM submerged culture medium using corncob was purified and characterized. The enzyme was purified 12.65-fold through ammonium sulphate precipitation, Sephadex G-25, DEAE cellulose chromatography, followed by gel filtration through a Sephadex G-100 column. The molecular mass of purified xylanase was about 31.75 kDa. The enzyme was an endo-xylanase, as it degraded xylan to xylooligosaccharide with non-xylose after 24 h. The purified enzyme showed optimum activity at 60 ∘ C and at pH 8.0 but remained active over a wide range of pH (6.0-11.0) and temperature (40-80 ∘ C). The enzyme retained 98.72% and 69.50% residual enzyme activity at pH 8.0 and at 60 ∘ C after 1 h. The K m and V max values were found to be 43.03 mg mL −1 and 312.5 mol (min mg −1 ), respectively. The enzyme was remarkably activated by cysteine and Cu 2+ , and its activity was strongly inhibited by Hg 2+ . The brightness of kraft pulp was improved by this xylanase. CONCLUSION: Since the enzyme was active over a wide range of pH, and remained active at high temperature, it could find potential uses in biobleaching processes in pulp paper industries and in the production of xylooligosacaharides.

show abstract

Production, purification and characterization of a minor form of xylanase from Aspergillus versicolor

Cited by 56 publications

References 16 publications

Purification and characterization studies of a thermostable β-xylanase from Aspergillus awamori

Purification and characterization studies of a thermostable β-xylanase from Aspergillus awamori

Statistical optimization and kinetic modeling of xylanase production by Arthrobacter sp.

Purification and characterization of an alkaliphilic endo‐xylanase from Streptomyces althioticusLMZM and utilization in the pulp paper industry

Contact Info

Product

Resources

About