A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans
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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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Date
2018-03
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Language
en
Pages
12
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Biotechnology for Biofuels, Volume 11, issue 1
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.Description
| openaire: EC/H2020/648925/EU//BHIVE
Keywords
Acetyl xylan esterase, Glucuronic acid, Polysaccharide utilization loci, SGNH hydrolase, Xylan, α-Glucuronidase
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Citation
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, vol. 11, no. 1, 74 . https://doi.org/10.1186/s13068-018-1074-3