A. Blanco et al., PURIFICATION AND PROPERTIES OF XYLANASE-A FROM ALKALI-TOLERANT BACILLUS SP STRAIN BP-23, Applied and environmental microbiology, 61(12), 1995, pp. 4468-4470
Xylanase A from the recently isolated Bacillus sp, strain BP-23 was pu
rified 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 comple
tely inhibited by N-bromosuccinimide. The main products of birchwood x
ylan 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 xyla
nases from family F.