Mode of action of the xylan-degrading enzymes from Aspergillus awamori on alkali-extractable cereal arabinoxylans

4)-beta-D-xylanases I and III from Aspergillus awamori CMI 142717 and the digests subjected to analysis by high performance anion-exchange chromatography. Clear differences in the mode of action of the two endo-(1-->4)-beta-D-xylanases were observed. When counting from the reducing end, at least one unsubstituted xylopyranosyl residue adjacent to singly substituted xylopyranosyl residues or two unsubstituted xylopyranosyl residues adjacent to doubly substituted xylopyranosyl residues cannot be removed by endo-(1-->4)-beta-D-xylanase I. At least two unsubstituted xylopyranosyl residues adjacent to singly or doubly substituted xylopyranosyl residues cannot be removed by endo-(1-->4)-beta-D-xylanase III. beta-D-Xylosidase from the same xylanolytic system was able to remove terminal xylopyranosyl residues from the nonreducing end of branched oligosaccharides only when two contiguous unsubstituted xylopyranosyl residues were present adjacent to singly or doubly substituted xylopyranosyl residues. -->
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Jazyk: English
ISSN: 0008-6215
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27025f7ce7205c915c6759cffd0b0318
https://research.wur.nl/en/publications/mode-of-action-of-the-xylan-degrading-enzymes-from-aspergillus-aw
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Přírůstkové číslo: edsair.doi.dedup.....27025f7ce7205c915c6759cffd0b0318
Autor: Alphons G. J. Voragen, Remco J. Viëtor, F.J.M. Kormelink, Harry Gruppen
Jazyk: angličtina
Rok vydání: 1993
Předmět:
Zdroj: Carbohydrate Research : an international journal, 249, 355-367
Carbohydrate Research : an international journal 249 (1993)
ISSN: 0008-6215
Popis: Alkali-extractable cereal arabinoxylan and oligosaccharides of known structure derived from it by enzymic hydrolysis were treated with endo-(1-->4)-beta-D-xylanases I and III from Aspergillus awamori CMI 142717 and the digests subjected to analysis by high performance anion-exchange chromatography. Clear differences in the mode of action of the two endo-(1-->4)-beta-D-xylanases were observed. When counting from the reducing end, at least one unsubstituted xylopyranosyl residue adjacent to singly substituted xylopyranosyl residues or two unsubstituted xylopyranosyl residues adjacent to doubly substituted xylopyranosyl residues cannot be removed by endo-(1-->4)-beta-D-xylanase I. At least two unsubstituted xylopyranosyl residues adjacent to singly or doubly substituted xylopyranosyl residues cannot be removed by endo-(1-->4)-beta-D-xylanase III. beta-D-Xylosidase from the same xylanolytic system was able to remove terminal xylopyranosyl residues from the nonreducing end of branched oligosaccharides only when two contiguous unsubstituted xylopyranosyl residues were present adjacent to singly or doubly substituted xylopyranosyl residues.
Databáze: OpenAIRE