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

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1997 (EN)
The alkaline xylanase III from Fusarium oxysporum F3 belongs to family F/10 (EN)

Christakopoulos, P (EN)
Macris, B (EN)
Nerinckx, W (EN)
Claeyssens, M (EN)
Kekos, D (EN)

N/A (EN)

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. (EN)


Partial amino acid sequence (EN)
Molecular Weight (EN)
Enzyme purification (EN)
fusarium oxysporum (EN)
Molecular Sequence Data (EN)
Substrate Specificity (EN)
enzyme isolation (EN)
ion exclusion chromatography (EN)
gel filtration (EN)
enzyme purification (EN)
Xylanase (EN)
amino acid sequence (EN)
enzyme activity (EN)
Isoelectric Point (EN)
Xylosidases (EN)
Fusarium (EN)
Triticum aestivum subsp. spelta (EN)
umbelliferone derivative (EN)
priority journal (EN)
Amino Acid Sequence (EN)
Fusarium oxysporum (EN)
Enzyme Stability (EN)
article (EN)
Amino Acids (EN)
Sequence Homology, Amino Acid (EN)
glucoside (EN)
nonhuman (EN)
Sequence Analysis (EN)
Endo-1,4-beta Xylanases (EN)
Hydrogen-Ion Concentration (EN)

Εθνικό Μετσόβιο Πολυτεχνείο (EL)
National Technical University of Athens (EN)

Carbohydrate Research (EN)



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