Xylan-Degrading Enzymes from the Thermophilic Fungus Humicola lanuginosa (Griffon and Maublanc) Bunce : Action Pattern of Xylanase and β-Glucosidase on Xylans, Xylooligomers and Arabinoxylooligomers

概要

論文の詳細を見る
The mode of action of xylanase and β-glucosidase purified from the culture filtrate of Humicola lanuginosa (Griffon and Maublanc) Bunce on the xylan extracted from sugarcane bagasse and on two commercially available larchwood and oat spelt xylans, on xylooligomers and on arabinoxylooligomers was studied. While larchwood and oat spelt xylans were hydrolyzed to the same extent in 24 h, sugarcane bagasse xylan was hydrolyzed to a lesser extent in the same period. It was found that the rate of hydrolysis of xylooligomers by xylanase increased with increase in chain length, while β-glucosidase acted rather slowly on all the oligomers tested. Xylanase exhibited predominant "endo" action on xylooligomers attacking the xylan chain at random while β-glucosidase had "exo" actoin, releasing one xylose residue at a time. On arabinoxylooligomers, however, xylanase exhibited "exo" action. Thus, it appears that the presence of the arabinose substituent has, in some way, rendered the terminal xylose-xylose linkage more susceptible to xylanase action. It was also observed that even after extensive hydrolysis with both the enzymes, substantial amounts of the parent arabinoxylooligomer remained unhydrolyzed together with the accumulation of arabinoxylobiose. It can therefore be concluded that the presence of the arabinose substituent in the xylan chain results in linkages that offer resistance to both xylanase and β-glucosidase action.
公益社団法人日本生物工学会の論文
1996-06-25

Xylan-Degrading Enzymes from the Thermophilic Fungus Humicola lanuginosa (Griffon and Maublanc) Bunce : Action Pattern of Xylanase and β-Glucosidase on Xylans, Xylooligomers and Arabinoxylooligomers

スポンサーリンク

概要

著者

関連論文

スポンサーリンク