Korean Journal of Microbiology (미생물학회지)
- Volume 31 Issue 2
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- Pages.157-165
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- 1993
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Purification and Characterization of Xylanase II from Trichoderma koningii ATCC 26113
Trichoderma koningii ATCC 26113으로부터 Xylanase II의 순수분리 및 특성
- Kim, Hyun-Ju (Department of Microbiology, College of Natural Sciences) ;
- Kang. Sa Ouk (Research Center for Molecular Microbiology, Seoul National University) ;
- Hah, Yung-Chil (Department of Microbiology, College of Natural Sciences)
- Published : 1993.04.01
Abstract
A 1, 4-.betha.-D-xylanase, designated as xylanase II, was purified from the culture filtrate of Trichoderma koningii ATCC 251131 by column chromatography on Sephadex G-75, SP-Sephadex C-50, DEAE-Sephadex A-50 and Sephadex G-50 with an overall yield of 6.97%. It has a molecular weight of 21.000 and an isoelectric point of 9.4. The enzyme activity is optimal at pH 5.0 and at a temperature of 50.deg.C. Xylanase II is stable up to 50.deg.C, while 40 and 90% of its activity are lost after the incubation for 30 and 60 min at 60.deg.C. The enzyme degrades xylan with relatively high activity, as well as carboxymethylcellulose and Avicel. Its