Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23.
Xylanase A from the recently isolated Bacillus sp. strain BP-23 was purified to homogeneity. The enzyme shows a molecular mass of 32 kDa and an isoelectric point of 9.3. Optimum temperature and pH for xylanase activity were 50 degrees C and 5.5 respectively. Xylanase A was completely inhibited by N-bromosuccinimide. The main products of birchwood xylan hydrolysis were xylotetraose and xylobiose. The enzyme was shown to facilitate chemical bleaching of pulp, generating savings of 38% in terms of chlorine dioxide consumption. The amino-terminal sequence of xylanase A has a conserved sequence of five amino acids found in xylanases from family F.
Department of Microbiology, Faculty of Biology, University of Barcelona, Spain.
A
A
Blanco
T
T
Vidal
J F
JF
Colom
F I
FI
Pastor
D000468:Alkalies; D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D004351:Drug Resistance; D043364:Endo-1,4-beta Xylanases; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014995:Xylosidases / Q000737:chemistry / Q000302:isolation & purification*
D000468:Alkalies; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases