The alkaline xylanase III from Fusarium oxysporum F3 belongs to family F/10

被引:34
作者
Christakopoulos, P [1 ]
Nerinckx, W [1 ]
Kekos, D [1 ]
Macris, B [1 ]
Claeyssens, M [1 ]
机构
[1] STATE UNIV GHENT, FAC SCI, DEPT BIOCHEM PHYSIOL & MICROBIOL, B-9000 GHENT, BELGIUM
关键词
xylanase; Fusarium oxysporum; enzyme purification; partial amino acid sequence;
D O I
10.1016/S0008-6215(97)00075-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Xylanase III from Fusarium oxysporum F3 was purified to homogeneity by ion-exchange chromatography and gel filtration. The enzyme has a molecular mass of 38 kDa, an isoelectric point of 9.5, and is maximally active on oat spelt xylan at pH 7 and 45 degrees C with a K-m of 0.8 mg/mL. The xylanase displays remarkable stability at pH 9.0. It is not active on xylotriose but hydrolyzes the 4-methylumbelliferyl glycosides of beta-xylobiose and beta-D-glucopyranosyl-(1 --> 4)-beta-D-xylopyranose and to a lower extent 4-methylumbelliferyl beta-cellobioside. When acted on xylooligosaccharides and xylan, analysis of reaction mixtures by high-pressure liquid chromatography shows preferred internal glycoside cleavage. Thus the purified enzyme appears to be a true endo-beta-1,4-xylanase. Partial amino acid analysis of xylanase III shows high sequence homology with xylanases of family F/10. (C) 1997 Elsevier Science Ltd.
引用
收藏
页码:191 / 195
页数:5
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