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 $K_{m}$ values for oat-spelt xylan, larchwood xylan and Avicel are 7.48, 1.98 and 13.33 mg/ml, respectively. The hydrolysis products of oat-spelt xylan by xylanase II are xylose, xylobiose, xylotriose and arabinoxylotriose, while the reaction products of larchwood xylan are xylose, xylobiose, xylotriose and small amount of higher oligomers. The action paterns of the enzyme demonstrate that xylanase II is endo-enzyme.

Keywords

Trichoderma koningii;xylanase II;endo-xylanase