A new Flavovacterium johnsoniae isolate encodes an enzyme that is essentially identical with a recently discovered novel acetylxylan esterase, capable of liberating 3-O-acetyl group from 4-O-methyl-d-glucuronic acid-substituted xylopyranosyl (Xylp) residues (Razeq et al., 2018). In addition to deesterification of the 2-O-MeGlcA-substituted Xylp residues in acetylglucuronoxylan, the enzyme acts equally well on doubly acetylated Xylp residues from which it liberates only the 3-O-acetyl groups, leaving the 2-O-acetyl groups untouched. 3-O-Monoacetylated Xylp residues are attacked with a significantly reduced affinity. The resulting 2-O-acetylated xylan was used to investigate for the first time the migration of the 2-O-acetyl group to position 3 within the polysaccharide. In contrast to easy acetyl group migration along the monomeric xylopyranosides or non-reducing-end terminal Xylp residues of xylooligosaccharides, such a migration in the polymer required much longer heating at 100 °C. The specificity of the xylan 3-O-deacetylase was, however, no so strict on acetylated methyl and 4-nitrophenyl xylopyranosides.
Keywords: 2-O-acetyglucuronoxylan; 3-O-deacetylase; Acetyl group migration; Hardwood acetylglucuronoxylan; Novel acetylxylan esterase; Novel regiospecificity.
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