Recombinant xylanase from Streptomyces coelicolor Ac-738: characterization and the effect on xylan-containing products
Autor: | N. G. Vinokurova, A. V. Lisov, Zhanna I. Budarina, Alexander A. Solonin, Alexey A. Leontievsky, O. V. Belova, Zhanna I. Andreeva-Kovalevskaya |
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Rok vydání: | 2013 |
Předmět: |
Avena
Physiology Enzyme Activators Gene Expression Streptomyces coelicolor Applied Microbiology and Biotechnology chemistry.chemical_compound Hydrolysis Enzymatic hydrolysis Enzyme Stability Escherichia coli Xylobiose Glycoside hydrolase Enzyme Inhibitors Triticum chemistry.chemical_classification biology Temperature food and beverages General Medicine Hydrogen-Ion Concentration biology.organism_classification Xylan Recombinant Proteins Molecular Weight Xylosidases Enzyme Biochemistry chemistry Metals Xylanase Xylans Biotechnology |
Zdroj: | World Journal of Microbiology and Biotechnology. 30:801-808 |
ISSN: | 1573-0972 0959-3993 |
DOI: | 10.1007/s11274-013-1480-4 |
Popis: | A xylanase gene was isolated from the genomic DNA of Streptomyces coelicolor Ac-738. The 723-bp full-length gene encoded a 241-amino acid peptide consisting of a 49-residue putative TAT signal peptide and a glycoside hydrolase family-11 domain. The mature enzyme called XSC738 was expressed in Escherichia coli M15[pREP4]. The electrophoretically homogeneous protein with a specific activity of 167 U/mg for beechwood xylan was purified. The pH optimum of XSC738 was at pH 6; a high activity was retained within a pH range of 4.5-8.5. The enzyme was thermostable at 50-60 °C and retained an activity at pH 3.0-7.0. Xylanase XSC738 was activated by Mn²⁺, Co²⁺ and largely inhibited by Cd²⁺, SDS and EDTA. The products of xylan hydrolysis were mainly xylobiose, xylotriose, xylopentaose and xylohexose. Xylotetraose appeared as a minor product. Processing of such agricultural xylan-containing products as wheat, oats, soy flour and wheat bran by xylanase resulted in an increased content of sugars. |
Databáze: | OpenAIRE |
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