| Title | Mode of Action and Active Site of Xylanase I from Trichoderma koningii ATCC 26113 | ||
| Author | Kim, Hyun-Ju · Sa-Ouk Kang * · Yung Chil Hah | ||
| Address | Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University | ||
| Bibliography | Korean Journal of Microbiology, 31(5),445-451, 1993 | ||
| DOI | |||
| Key Words | xylanase I, endo-enzyme, exo-enzyme activity, chemical modification, cysteine, tryptophan, Trichoderma koningii | ||
| Abstract | Xylanase I was purified from the culture filtrate of Trichoderma koningii ATCC 26113. The reaction products of xylotriose and xylotetraose are xylose and xylobiose, and the hydrolysis products of arabinoxylotriose are mainly xylose, arabinoxylobiose, and small amount of xylobiose and arabinoxylose. The enzyme does not liberate arabinose from arabinoxylan. The action patterns demonstrate that xylanse I is an endo-enzyme. The release of small amount of xylobiose and arabinoxylose from arabinoxylotriose indicates that xylanase I also has exo-enzyme activity. Chemical modification of the enzyme with iodoacetamide exhibits that one cysteine residue per molecule of the enzyme is essential for the activity. Modification of the enzyme with N-bromosuccinimide demonstrates that two of the twelve tryptophan residues are essential for its catalytic activity. | ||
| Download PDF | Kor_310514_445-451p.pdf | ||