A comparison of two xylanases from the thermophilic fungi Thielavia terrestris and Thermoascus crustaceus.
Two thermophilic xylanases (xylanase II from Thielavia terrestris 255B and the 32-kDa xylanase from Thermoascus crustaceus 235E) were studied to determine if they had different and complementary modes of action when they hydrolysed various types of xylans. Partial amino acid sequencing showed that these two enzymes belonged to different families of beta-1,4-glycanases. Xylanase II achieved faster solubilization of insoluble xylan whereas the 32-kDa xylanase was more effective in producing xylose and short xylo-oligomers. An assessment of the combined hydrolytic action of the two xylanases did not reveal any co-operative action. The sugars released when the two thermophilic xylanases were used together were almost identical to those released when the 32-kDa xylanase acted alone. The two xylanases were able to remove about 12% of the xylan remaining in an aspen kraft pulp. This indicated that either one of these thermophilic enzymes may be useful for enhancing the bleaching of kraft pulps.
Gilbert
M
M
University of Ottawa, Department of Biology, Ontario, Canada.
Yaguchi
M
M
Watson
D C
DC
Wong
K K
KK
Breuil
C
C
Saddler
J N
JN
D000595:Amino Acid Sequence; D001203:Ascomycota / Q000201:enzymology*; D002523:Edible Grain / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000145:classification* / Q000235:genetics* / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010209:Paper; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D014934:Wood; D043325:Xylan Endo-1,3-beta-Xylosidase; D014990:Xylans / Q000378:metabolism
D014990:Xylans; D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase