ENZYMATIC DEGRADATION OF SORGHUM GLUCURONOARABINOXYLANS LEADING TO TENTATIVE STRUCTURES

Citation
Ma. Verbruggen et al., ENZYMATIC DEGRADATION OF SORGHUM GLUCURONOARABINOXYLANS LEADING TO TENTATIVE STRUCTURES, Carbohydrate research, 306(1-2), 1998, pp. 275-282
Citations number
36
Categorie Soggetti
Chemistry Applied","Chemistry Inorganic & Nuclear",Biology
Journal title
ISSN journal
00086215
Volume
306
Issue
1-2
Year of publication
1998
Pages
275 - 282
Database
ISI
SICI code
0008-6215(1998)306:1-2<275:EDOSGL>2.0.ZU;2-3
Abstract
Three glucuronoarabinoxylan (GAX) populations, obtained from water-une xtractable cell wall material from sorghum by different alkali extract ants, were digested by combinations of endo-xylanases (Xyl I, Xyl III and GXH), arabinofuranosidases (AXH and AraB) and an ru-glucuronidase (GlcAase). All three GAX populations were shown to be rather poorly de gradable, due to the very high degree of substitution, as well as the substitution pattern. The barium hydroxide-extracted GAX showed a maxi mum 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 b etween Xyl I and AXH. Both neutral and acidic arabinoxylan oligomers w ere formed. The GlcAase acted only upon oligomeric material released b y 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 so rghum GAX. Evidence was obtained that the xylan backbone of especially the GAX extracted by 4 M KOH, is substituted by arabinose and glucuro nic acid according to a strict pattern, which hinders the enzymes to a ct. (C) 1998 Elsevier Science Ltd. All rights reserved.