title: Purification and partial characterization of a basic xylanase produced by thermoalkaliphilic Bacillus sp. strain TAR-1.
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.
authors.affiliation: Department of Bioengineering, Tokyo Institute of Technology, Yokohama, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Takahashi
authors.forename: R
authors.initials: R
authors.lastname: Nakai
authors.forename: S
authors.initials: S
authors.lastname: Nakamura
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D002855:Chromatography, Thin Layer; D043364:Endo-1,4-beta Xylanases; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D014990:Xylans / Q000378:metabolism; D014995:Xylosidases / Q000737:chemistry / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D014990:Xylans; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases