Purification and partial characterization of a basic xylanase produced by thermoalkaliphilic Bacillus sp. strain TAR-1

Biosci Biotechnol Biochem. 2000 Apr;64(4):887-90. doi: 10.1271/bbb.64.887.

Abstract

A basic xylanase was purified from the culture supernatant of thermoalkaliphilic Bacillus sp. strain TAR-1. Its molecular mass and isoelectric point were 23 kDa and > pH 9.3, respectively. The enzyme showed a broad pH profile and was optimally active at 70 degrees C. Analyses of xylan-degradation products and N-terminal amino acid sequence revealed that the enzyme would be a family 11/G endoxylanase.

MeSH terms

  • Bacillus / enzymology*
  • Chromatography, Thin Layer
  • Endo-1,4-beta Xylanases
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Xylans / metabolism
  • Xylosidases / chemistry
  • Xylosidases / classification
  • Xylosidases / isolation & purification
  • Xylosidases / metabolism*

Substances

  • Xylans
  • Xylosidases
  • Endo-1,4-beta Xylanases