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Fig. 5 | Biotechnology for Biofuels

Fig. 5

From: The xyl-doc gene cluster of Ruminiclostridium cellulolyticum encodes GH43- and GH62-α-l-arabinofuranosidases with complementary modes of action

Fig. 5

Representative arabinoxylan structure and the sites of cleavage by the accessory Xyl-Doc enzymes. Linear backbone of β-(1 → 4)-linked d-xylopyranosyl units (Xylp) decorated by α-l-arabinofuranosyl (Araf) α-(1 → 2) or α-(1 → 3)-linked. Acetyl substitutions (Ac) of xylose residues are also found. Some of Araf residues are linked to ferulic acids (FA) allowing the formation of arabinoxylan–arabinoxylan cross-links. A: linkage putatively cleaved by RcAbf43A formerly named GH4316-1229. B: linkage cleaved by RcAbf43Ad2,3 formerly named GH4310-1233. C: linkage cleaved by RcAbf62m2,3 formerly named GH62-1234. D: linkages cleaved by RcAbf62Bm2,3Axe6 formerly named GH62-CE6-1240. E: linkage cleaved by the putative feruloyl esterase product of the gene at locus Ccel_1232

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