| Title | Mode of action anf active site of xylanase II from Trichoderma koningii ATCC 26113 | ||
| Author | Kim, Hyun Ju · Kang, Sa Ouk * · Hah, Yung Chil | ||
| Address | Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University | ||
| Bibliography | Korean Journal of Microbiology, 32(4),306-314, 1994 | ||
| DOI | |||
| Key Words | Xalanase II, endo-enzyme, tran-xylodisation, cysteinm tryptophan, Trichoderma koningii | ||
| Abstract | The action mode of xylanase II from Trichoderma koningii ATCC 26113 on xylan and related olifosaccharides(xylotrose, xylotetraose, and arabinoxylotriose) indicated that xylans II is an endo-enzyme and also hat trans-zylosidase activity. The ¹H-NMR studies of the rection products formed by xylanase II revealed that all the hydrolysis products of xylooligosaccharides by the enzyme have only β-1,40xylosidic linkage(s). Chemical modification of the enzyme with iodoacetamide showed that two cystein 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. | ||
| Download PDF | Kor_320411_306-314p.pdf | ||