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Purification and characterization of endoxylanase Xln-1 from Aspergillus niger B03

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Abstract

An extracellular endoxylanase was isolated from the xylanolytic complex of Aspergillus niger B03. The enzyme was purified to a homogenous form using consecutive ultrafiltration and anion exchange chromatography. The endoxylanase was a monomer protein with a molecular weight of 33,000 Da determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and 34,000 Da determined by gel filtration. The optimal pH and temperature values for the enzyme action were 6.0 and 60°C, respectively. Endoxylanase was stable at 40°C, pH 7.0 for 210 min. The thermal stability of the enzyme was significantly increased in the presence of glycerol and sorbitol. The enzyme activity was inhibited by Cu2+, Fe2+, Fe3+, and Ag1+, and it was activated by Mn2+. The substrate specificity and kinetic parameters of the enzyme were determined with different types of xylans. Endoxylanase displayed maximum activity in the case of oat spelt xylan, with an apparent K m value of 8.19 mg/ml. The substrate specificity and the product profile of the enzyme suggested it to be an endoxylanase.

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Acknowledgments

The research was carried out with a strain of Aspergillus niger, provided by Biovet JSC. The work was supported by the Grant-in-Aid for Scientific Research of Priority area (Agricultural science) from the Ministry of Education of Bulgaria.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Food Technologies, 26 Maritza Blvd., 4000, Plovdiv, Bulgaria

    Georgi Dobrev, Boriana Zhekova, Ginka Delcheva, Lidia Koleva, Nicola Tziporkov & Ivan Pishtiyski

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  1. Georgi Dobrev
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  2. Boriana Zhekova
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  3. Ginka Delcheva
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  4. Lidia Koleva
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  5. Nicola Tziporkov
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  6. Ivan Pishtiyski
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Correspondence to Boriana Zhekova.

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Dobrev, G., Zhekova, B., Delcheva, G. et al. Purification and characterization of endoxylanase Xln-1 from Aspergillus niger B03. World J Microbiol Biotechnol 25, 2095–2102 (2009). https://doi.org/10.1007/s11274-009-0112-5

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  • DOI: https://doi.org/10.1007/s11274-009-0112-5

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