Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 43713
Title Enzymic degradation of sorghum glucuronoarabinoxylans leading to tentative structures.
Author(s) Verbruggen, M.A.; Beldman, G.; Voragen, A.G.J.
Source Carbohydrate Research : an international journal 306 (1998). - ISSN 0008-6215 - p. 275 - 282.
Department(s) Food Chemistry and Microbiology
Publication type Refereed Article in a scientific journal
Publication year 1998
Abstract Three glucuronoarabinoxylan (GAX) populations, obtained from water-unextractable cell wall material from sorghum by different alkali extractants, were digested by combinations of endo-xylanases (Xyl I, Xyl III and GXH), arabinofuranosidases (AXH and AraB) and an -glucuronidase (GlcAase). All three GAX populations were shown to be rather poorly degradable, due to the very high degree of substitution, as well as the substitution pattern. The barium hydroxide-extracted GAX showed a maximum degree of degradation of almost 12%, using Xyl I combined with GXH and AXH. The GAX population extracted by 4 M KOH was hardly degraded by any of the tested combinations. In all cases, Xyl III showed lowest activity upon the three extracts. Synergistic effects were observed between Xyl I and AXH. Both neutral and acidic arabinoxylan oligomers were formed. The GlcAase acted only upon oligomeric material released by Xyl I. No synergistic effects were observed between the GXH and AXH. Combining the patterns of degradation with the modes of action of the enzymes, structures were proposed for the different populations of sorghum GAX. Evidence was obtained that the xylan backbone of especially the GAX extracted by 4 M KOH, is substituted by arabinose and glucuronic acid according to a strict pattern, which hinders the enzymes to act.
There are no comments yet. You can post the first one!
Post a comment
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.