Applied Biochemistry and Biotechnology

, Volume 168, Issue 4, pp 899–909

A Novel Alkaliphilic Xylanase from the Newly Isolated Mesophilic Bacillus sp. MX47: Production, Purification, and Characterization

  • Won-Jae Chi
  • Da Yeon Park
  • Yong-Keun Chang
  • Soon-Kwang Hong
Article

DOI: 10.1007/s12010-012-9828-z

Cite this article as:
Chi, W., Park, D.Y., Chang, Y. et al. Appl Biochem Biotechnol (2012) 168: 899. doi:10.1007/s12010-012-9828-z

Abstract

A newly isolated bacterial strain, Bacillus sp. MX47, was actively producing extracellular xylanase only in xylan-containing medium. The xylanase was purified from the culture broth by two chromatographic steps. The xylanase had an apparent molecular weight of 26.4 kDa with an NH2-terminal sequence (Gln-Gly-Gly-Asn-Phe) distinct from that of reported proteins, implying it is a novel enzyme. The optimum pH and temperature for xylanase activity were 8.0 and 40 °C, respectively. The enzyme activity was severely inhibited by many divalent metal ions and EDTA at 5 mM. The xylanase was highly specific to beechwood and oat spelt xylan, however, not active on carboxymethyl cellulose (CMC), avicel, pectin, and starch. Analysis of the xylan hydrolysis products by Bacillus sp. MX47 xylanase indicated that it is an endo-β-1,4-xylanase. It hydrolyzed xylan to xylobiose as the end product. The Km and Vmax values toward beechwood xylan were 3.24 mg ml−1 and 58.21 μmol min−1 mg−1 protein, respectively.

Keywords

XylanaseEndo-β-1,4-xylanaseXylobioseBacillus sp.PurificationChromatography

Supplementary material

12010_2012_9828_MOESM1_ESM.doc (301 kb)
ESM 1(DOC 301 kb)

Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Won-Jae Chi
    • 1
  • Da Yeon Park
    • 1
  • Yong-Keun Chang
    • 2
  • Soon-Kwang Hong
    • 1
  1. 1.Department of Biological ScienceMyongji UniversityYonginSouth Korea
  2. 2.Department of Chemical and Biomolecular EngineeringKorea Advanced Institute of Science and TechnologyDaejeonSouth Korea