Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of Two Endoxylanases from an Alkaliphilic Bacillus halodurans C-1

  • Tachaapaikoon Chakrit (School of Bioresources and Technology, King Mongkut's University of Technology Thonburi) ;
  • Lee Yun-Sik (Department of Surgery, University of Pennsylvania, School of Medicine, Philadelphia) ;
  • Rantanakhanokchai Khanok (School of Bioresources and Technology, King Mongkut's University of Technology Thonburi) ;
  • Pinitglang Surapong (Department of Food Science and Technology, University of the Thai, Chamber of Commerce) ;
  • Kyu Khin Lay (School of Bioresources and Technology, King Mongkut's University of Technology Thonburi) ;
  • Rho Min-Suk (Department of Pathology, Seoul National University, College of Medicine) ;
  • Lee Si-Kyung (Department of Applied Biology and Chemistry, Konkuk University)
  • Published : 2006.04.01
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Abstract

Two endoxylanases from an alkaliphilic bacterium, Bacillus halodurans C-1, were purified 3.8- and 7.9- fold with specific activities of 9.4 and 19.8U/mg protein, respectively. The molecular masses of both purified enzymes were 23 and 47 kDa, respectively, and 23 kDa xylanase I (Xyl I) exhibited an optimum pH at 7.0, whereas 47 kDa xylanase II (Xyl II) showed a broad pH range of 5.0 to 9.0. The temperature optima of both xylanases were $60^{\circ}C\;and\;70^{\circ}C$, respectively. Both were stable in the pH range of 6.0 to 9.0 and 5.0 to 10.0, respectively, and they were stable up to $60^{\circ}C\;and\;70^{\circ}C$, respectively. The $K_m\;and\;V_{max}$ of Xyl I were 4.33mg/ml and $63.5{\mu}mol/min/mg$, respectively, whereas Xyl II had a $K_m$ value of 0.30 mg/ml and $V_{max}$ of $210{\mu}mol/min/mg$. Both xylanases hydrolyzed xylans from birchwood, oat spelt, and larchwood. However, they showed different modes of action; a series of xylooligosaccharides larger than xylotriose were released as the major products by Xyl I, whereas xylobiose and xylotriose were the main products by Xyl II. The maximum synergistic action of the two enzymes on hydrolysis of xylan was 2.16 with the ratio of Xyl I to Xyl II at 1:9.

Keywords

References

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