Applied Microbiology and Biotechnology

, Volume 72, Issue 6, pp 1210–1216

Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific

Biotechnologically Relevant Enzymes and Proteins

DOI: 10.1007/s00253-006-0416-4

Cite this article as:
Wu, S., Liu, B. & Zhang, X. Appl Microbiol Biotechnol (2006) 72: 1210. doi:10.1007/s00253-006-0416-4


A novel xylanase-producing thermophilic strain MT-1 was isolated from a deep-sea hydrothermal field in east Pacific. A xylanase gene encoding 331 amino-acid peptide from this isolate was cloned and expressed in Escherichiacoli. The recombinant xylanase exhibited maximum activity at 70°C and had an optimum pH of 7.0. It was active up to 90°C and showed activity over a wide pH ranging from 5.5 to 10.0. The crude xylanase presented similar properties in temperature and pH to those of the recombinant xylanase. The recombinant xylanase was stable in 1 mM of enzyme inhibitors (PMSF, EDTA, 2-ME or DTT) and in 0.1% detergents (Tween 20, Chaps or Triton X-100), whereas, it was strongly inhibited by sodium dodecyl sulfate (SDS) (1 mM). In addition, its catalytic function was stable in the presence of Li+, Na+ or K+. However, it was strongly inhibited by Ni2+, Mn2+, Co2+, Cu2+, Zn2+, Cd2+, Hg2+ and Al3+ (1 or 0.1 mM). The Km and Vmax of the recombinant xylanase for oat spelt xylan were calculated to be 1.579 mg/ml and 289 μmol/(min • mg), respectively. Our study, therefore, presented a rapid overexpression and purification of xylanase from deep-sea thermophile aimed at improving the enzyme yield for industrial applications and scientific research.

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  1. 1.School of Life SciencesXiamen UniversityXiamen 361005People’s Republic of China
  2. 2.Key Laboratory of Marine Biogenetic Resources, Third Institute of OceanographyState Oceanic AdministrationXiamen 361005People’s Republic of China

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