Purification and characterization of low molecular weight alkali stable xylanase from Neosartorya spinosa UZ-2-11 |
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| Institution: | 1. Graduate School, Khon Kaen University, Khon Kaen, 40002, Thailand;2. Biology Program, Faculty of Science, Buriram Rajabhat University, Buriram, 31000, Thailand;3. Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand;4. Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Tottori, 680-8553, Japan;5. Department of Microbiology, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand;1. Graduate school of Infection Control Sciences, Kitasato University, 5-9-1, Shirokane, Minato-ku, Tokyo, 108-8641, Japan;2. Kitasato Institute for Life Sciences, Kitasato University, 5-9-1, Shirokane, Minato-ku, Tokyo, 108-8641, Japan;1. Department of Plant Protection, Faculty of Plant Production, Gorgan University of Agricultural Sciences and Natural Resources, Gorgan, Iran;2. Biotechnology Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran;3. Department of Biology, Rutgers University, New Brunswick, NJ, USA;4. Department of Biotechnology & Plant Breeding, Faculty of Plant Production, Gorgan University of Agricultural Sciences and Natural Resources, Gorgan, Iran;1. Research Institute of Innovative Technology for the Earth, 9-2 Kizugawadai, Kizugawa, Kyoto, 619-0292, Japan;2. Plant Pathology & Plant-Microbe Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, NY, USA |
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| Abstract: | Alkaliphilic xylanase from Neosartorya spinosa UZ-2-11 was purified using a three-step of purification scheme of ammonium sulphate precipitation followed by Sephadex G-100 gel filtration and DEAE-cellulose ion-exchange chromatography, and compared its properties with N. tatenoi KKU-CLB-3-2-4-1 of our previous report. The purified xylanase from N. spinosa UZ-2-11 exhibited maximum activity at pH 9.0 and 45 °C which was similar to endo-xylanase from N. tatenoi KKU-CLB-3-2-4-1. However, this enzyme was stable in a range of pH 6.0–11.0. It was also more stable at a high temperature of 50 °C where the activity was still up to 50% after heating for 120 min. The xylanase was purified 7.89-fold with 3.0% of yield to obtain a specific activity of 11.88 U/mg. The molecular weight of xylanase from this fungus was 27.68 kDa. The Km and Vmax values of the purified xylanase were 0.24 mg/mL and 15.85 μmol/min/mg, respectively. The xylanase activity was moderately inhibited by Hg2+ at a concentration of 10 mM, which was different to the case of N. tatenoi KKU-CLB-3-2-4-1 where Hg2+ was a strong inhibitor. In addition, the hydrolysed birchwood xylan was obtained mailnly xylobiose, xylotriose, xylotetraose and xylopentaose as end products, suggesting that it was an endo-xylanase. |
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| Keywords: | Alkaliphilic xylanase Ascomycota Birchwood xylan |
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