Purification and partial characterization of a basic xylanase produced by thermoalkaliphilic Bacillus sp. strain TAR-1.
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.
Takahashi
H
H
Department of Bioengineering, Tokyo Institute of Technology, Yokohama, Japan.
Nakai
R
R
Nakamura
S
S
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*
D014990:Xylans; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases