A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans

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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 , vol. 11 , 74 . https://doi.org/10.1186/s13068-018-1074-3

Title: A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans
Author: Razeq, Fakhria M.; Jurak, Edita; Stogios, Peter J.; Yan, Ruoyu; Tenkanen, Maija; Kabel, Mirjam A.; Wang, Weijun; Master, Emma R.
Contributor organization: Department of Food and Nutrition
Carbohydrate Chemistry and Enzymology
Doctoral Programme in Food Chain and Health
Food Sciences
Date: 2018-03-22
Language: eng
Number of pages: 12
Belongs to series: Biotechnology for Biofuels
ISSN: 1754-6834
DOI: https://doi.org/10.1186/s13068-018-1074-3
URI: http://hdl.handle.net/10138/237878
Abstract: Background: Acetylated 4-O-(methyl) glucuronoxylan (GX) is the main hemicellulose in deciduous hardwood, and comprises a beta-(1 -> 4)-linked xylopyranosyl (Xylp) backbone substituted by both acetyl groups and alpha-(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 alpha-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.
Subject: Acetyl xylan esterase
Glucuronic acid
Polysaccharide utilization loci
SGNH hydrolase
414 Agricultural biotechnology
1183 Plant biology, microbiology, virology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion

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