Recombinant xylanase from Streptomyces coelicolor Ac-738: characterization and the effect on xylan-containing products

• Published in: World journal of microbiology & biotechnology 2014-03, Vol.30 (3), p.801-808
• Main Authors: Lisov, Alexander V, Belova, Oksana V, Andreeva-Kovalevskaya, Zhanna I, Budarina, Zhanna I, Solonin, Alexander A, Vinokurova, Nataliya G, Leontievsky, Alexey A
• Format: Article
• Language: English
• Subjects: Amino acids; Analysis; Applied Microbiology; Avena - metabolism; Bacteria; Biochemistry; Biomedical and Life Sciences; Biosynthesis; Biotechnology; cadmium; Cloning; cobalt; DNA; E coli; EDTA (chelating agent); Environmental Engineering/Biotechnology; Enzyme Activators - metabolism; Enzyme Inhibitors - metabolism; Enzyme Stability; Enzymes; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Feeds; Flour; Gene Expression; Genes; Genetic recombination; Hydrogen-Ion Concentration; hydrolysis; Life Sciences; Lignin; manganese; Metals - metabolism; Microbiology; Microorganisms; Molecular Weight; oats; Original Paper; Peptides; Plasmids; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; signal peptide; soy flour; Streptomyces coelicolor; Streptomyces coelicolor - enzymology; Streptomyces coelicolor - genetics; Studies; sugars; Temperature; thermal stability; Triticum - metabolism; Triticum aestivum; Wheat; Wheat bran; xylan; Xylanase; xylanases; Xylans - metabolism; Xylosidases - chemistry; Xylosidases - genetics; Xylosidases - isolation & purification; Xylosidases - metabolism
• ISSN: 0959-3993; 1573-0972
• DOI: 10.1007/s11274-013-1480-4

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.