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Enzymic Degradation of Sorghum Glucuronoarabinoxylans Leading to Tentative Structures by Marian A Verbruggen; Gerrit Beldman; Alphons G.J Voragen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Three glucuronoarabinoxylan GAX populations, obtained from water-unextractable cell wall material from sorghum by different alkali extractants, were digested by combinations of Ž . Ž . endo-xylanases Xyl I, Xyl III and GXH , arabinofuranosidases AXH and AraB and an Ž . a-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

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Author

Marian A Verbruggen; Gerrit Beldman; Alphons G.J Voragen

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0008-6215)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)