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Fig. 3 | Biotechnology for Biofuels

Fig. 3

From: The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans

Fig. 3

XacAbf51 releases Araf from mono- and di-substituted AXOS and from arabinoxylan. Capillary zone electrophoresis profiles of AXOS before (red lines) and after (black lines) incubation with XacAbf51. Although the peaks of decorated and undecorated oligosaccharides were indistinguishable in this assay, the increase of arabinose (Ara) peak after enzyme treatment shows the capacity of XacAbf51 to release Araf from several AXOS and from arabinoxylan and arabinan. a A3X = 32-α-l-arabinofuranosyl-xylobiose; b A2XX = 23-α-l-arabinofuranosyl-xylotriose; c A2+3XX = 23, 33-di-α-l-arabinofuranosyl-xylotriose; d XA3XX = 33-α-l-arabinofuranosyl-xylotetraose; e XA2+3XX = 23, 33-di-α-l-arabinofuranosyl-xylotetraose; f arabinoxylan from wheat flour and arabinan from sugar beet. Black arrowheads represent the migration time of arabinose (Ara), xylobiose (X2), xylotriose (X3) and xylotetraose (X4) standard runs. Red arrowheads represent the substrate migration time (0 min, without enzyme). In (f), the Ara released from arabinan was used as a reference for the analysis of arabinoxylan cleavage, due to the anomalous migration of Ara in these conditions, compared to the standard run

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