Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1

Biotechnol Lett. 2011 Jul;33(7):1441-7. doi: 10.1007/s10529-011-0579-7. Epub 2011 Mar 6.

Abstract

A xylanase gene was PCR-cloned from Thermoanaerobacterium saccharolyticum and expressed in Escherichia coli. The xylanase (XynA) consisted of a signal peptide, glycoside hydrolase family 10 domains, carbohydrate-binding modules, and surface layer homology domains. It was optimally active at 70-73°C and at pH 5-7. It had enhanced activity with NaCl with optimal activity at 0.4 M but was tolerant up to 2 M NaCl. The thermostable and salt-tolerant properties of this xylanase suggest that it may be useful for industrial applications.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / genetics
  • Enzyme Activators / metabolism
  • Enzyme Stability
  • Escherichia coli / genetics
  • Gene Expression
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Protein Sorting Signals / genetics
  • Protein Structure, Tertiary
  • Salts / metabolism*
  • Sequence Analysis, DNA
  • Temperature
  • Thermoanaerobacterium / enzymology*
  • Xylosidases / chemistry
  • Xylosidases / genetics*
  • Xylosidases / metabolism*

Substances

  • DNA, Bacterial
  • Enzyme Activators
  • Protein Sorting Signals
  • Salts
  • Xylosidases

Associated data

  • GENBANK/GQ868303