Mode of action anf active site of xylanase II from Trichoderma koningii ATCC 26113

Trichoderma koningii ATCC 26113에서 분리된 xylanase II의 작용양상과 활성부위

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 ${\beta}$-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.

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 ${\beta}$-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.