A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans

Fakhria M. Razeq, Edita Jurak, Peter J. Stogios, Ruoyu Yan, Maija Tenkanen, Mirjam A. Kabel, Weijun Wang, Emma R. Master*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)

Abstract

Background: Acetylated 4-O-(methyl)glucuronoxylan (GX) is the main hemicellulose in deciduous hardwood, and comprises a β-(1→4)-linked xylopyranosyl (Xylp) backbone substituted by both acetyl groups and α-(1→2)-linked 4-O-methylglucopyranosyluronic acid (MeGlcpA). Whereas enzymes that target singly acetylated Xylp or doubly 2,3-O-acetyl-Xylp have been well characterized, those targeting (2-O-MeGlcpA)3-O-acetyl-Xylp structures in glucuronoxylan have remained elusive. Results: An unclassified carbohydrate esterase (FjoAcXE) was identified as a protein of unknown function from a polysaccharide utilization locus (PUL) otherwise comprising carbohydrate-active enzyme families known to target xylan. FjoAcXE was shown to efficiently release acetyl groups from internal (2-O-MeGlcpA)3-O-acetyl-Xylp structures, an activity that has been sought after but lacking in known carbohydrate esterases. FjoAcXE action boosted the activity of α-glucuronidases from families GH67 and GH115 by five and nine times, respectively. Moreover, FjoAcXE activity was not only restricted to GX, but also deacetylated (3-O-Araf)2-O-acetyl-Xylp of feruloylated xylooligomers, confirming the broad substrate range of this new carbohydrate esterase. Conclusion: This study reports the discovery and characterization of the novel carbohydrate esterase, FjoAcXE. In addition to cleaving singly acetylated Xylp, and doubly 2,3-O-acetyl-Xylp, FjoAcXE efficiently cleaves internal 3-O-acetyl-Xylp linkages in (2-O-MeGlcpA)3-O-acetyl-Xylp residues along with densely substituted and branched xylooligomers; activities that until now were missing from the arsenal of enzymes required for xylan conversion.
Original languageEnglish
Article number74
JournalBiotechnology for Biofuels
Volume11
Issue number1
DOIs
Publication statusPublished - 22 Mar 2018

Keywords

  • Acetyl xylan esterase
  • Glucuronic acid
  • Polysaccharide utilization loci
  • SGNH hydrolase
  • Xylan
  • α-Glucuronidase

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    Razeq, F. M., Jurak, E., Stogios, P. J., Yan, R., Tenkanen, M., Kabel, M. A., Wang, W., & Master, E. R. (2018). A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans. Biotechnology for Biofuels, 11(1), [74]. https://doi.org/10.1186/s13068-018-1074-3