Gilbert M, Yaguchi M, Watson D C, Wong K K, Breuil C, Saddler J N
University of Ottawa, Department of Biology, Ontario, Canada.
Appl Microbiol Biotechnol. 1993 Dec;40(4):508-14. doi: 10.1007/BF00175740.
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.
对两种嗜热木聚糖酶（来自特异腐质霉255B的木聚糖酶II和来自嗜热ascus crustaceus 235E的32 kDa木聚糖酶）进行了研究，以确定它们在水解各种类型木聚糖时是否具有不同且互补的作用模式。部分氨基酸测序表明，这两种酶属于不同的β-1,4-聚糖酶家族。木聚糖酶II能更快地使不溶性木聚糖溶解，而32 kDa木聚糖酶在产生木糖和短木寡糖方面更有效。对这两种木聚糖酶联合水解作用的评估未发现任何协同作用。两种嗜热木聚糖酶一起使用时释放的糖几乎与32 kDa木聚糖酶单独作用时释放的糖相同。这两种木聚糖酶能够去除白杨硫酸盐浆中剩余木聚糖的约12%。这表明这些嗜热酶中的任何一种都可能有助于提高硫酸盐浆的漂白效果。
