Abstract
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.
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This work was supported by an EurAsEC program of The Ministry of Education and Science of the Russian Federation, project No 16.11.M04.0010.
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Lisov, A.V., Belova, O.V., Andreeva-Kovalevskaya, Z.I. et al. Recombinant xylanase from Streptomyces coelicolor Ac-738: characterization and the effect on xylan-containing products. World J Microbiol Biotechnol 30, 801–808 (2014). https://doi.org/10.1007/s11274-013-1480-4
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DOI: https://doi.org/10.1007/s11274-013-1480-4