Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3

 
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Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3 (EN)

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

N/A (EN)

Two low molecular mass endo-1,4-β-D-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45-8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55°C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-D-glucopyranosyl)-β-D-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11.Two low molecular mass endo-1,4-β-D-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45-8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55 °C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-D-glucopyranosyl)-β-D-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11. (EN)

journalArticle

Biotechnology (EN)
unclassified drug (EN)
Chromatography, Ion Exchange (EN)
Partial amino acid sequence (EN)
Molecular Weight (EN)
Enzyme purification (EN)
Cellulose (EN)
fusarium oxysporum (EN)
Molecular Sequence Data (EN)
Substrate Specificity (EN)
alkaline xylanase (EN)
Molecular weight (EN)
enzyme purification (EN)
Xylanase (EN)
amino acid sequence (EN)
High pressure liquid chromatography (EN)
Isoelectric Point (EN)
Reaction kinetics (EN)
Xylan Endo-1,3-beta-Xylosidase (EN)
Xylosidases (EN)
Chemical bonds (EN)
pH (EN)
Fusarium (EN)
priority journal (EN)
Ion exchange (EN)
Isoelectric points (EN)
Enzymes (EN)
enzyme analysis (EN)
Amino Acid Sequence (EN)
Fusarium oxysporum (EN)
Purification (EN)
Enzyme Stability (EN)
Thermodynamic stability (EN)
article (EN)
Hydrolysis (EN)
Sequence Homology, Amino Acid (EN)
controlled study (EN)
nonhuman (EN)
Enzyme kinetics (EN)
Chromatography, Gel (EN)
Hydrogen-Ion Concentration (EN)

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

Journal of Biotechnology (EN)

1996


Elsevier Science B.V., Amsterdam, Netherlands (EN)



*Η εύρυθμη και αδιάλειπτη λειτουργία των διαδικτυακών διευθύνσεων των συλλογών (ψηφιακό αρχείο, καρτέλα τεκμηρίου στο αποθετήριο) είναι αποκλειστική ευθύνη των αντίστοιχων Φορέων περιεχομένου.