Xylan과 관련 다당류 (xylotriose, xylotetraose, arabinoxylotriose)에 대한 Trichoderma koningii ATCC 26113에서 분리된 xylanase II의 작용양상은 xylanase II가 endo-enzyme이고 transxylosidation의 활성을 가지고 있다고 보여진다. Xylanase II에 의해 형성된 반응산물을 $^1HNMR$ 분광법으로 분석한 결과는 본 효소에 의해 얻어진 xylooligosaccharides의 가수분해산물은 모두가 ${eta}$-1,4-xylosidic linkage만을 가지고 있는 것으로 판명되었다. 본 효소를 iodoacetamide로 화학적으로 변형시켰을 때 효소 mole당 cysteine 잔기가 두 개가 활성에 필요한 것으로 보여졌으며, N-bromosuccinimide 로 처리하였을 때는 활성부위에 tryptophan 잔기가 여덟 개 존재하는 것으로 판명되었다.
The action mode of xylanase II from Trichoderma koningii ATCC 26113 on xylan and related oligosaccharides (xylotriose, xylotetraose, and arabinoxylotriose) indicated that xylanase II is an endo-enzyme and also has trans-xylosidase activity. The $^1HNMR$-NMR studies of the reaction products formed by xylanase II revealed that all the hydrolysis products of xylooligosaccharides by the enzyme have only ${eta}$-1,4-xylosidic linkage(s). Chemical modification of the enzyme with iodoacetamide showed that two cysteine residues per molecule of the enzyme was essential for the activity. Modification of the enzyme with N-bromosuccinimide demonstrated that four of the eight tryptophan residues were involved in its active site.
