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Razeq FM, Jurak E, Stogios PJ, et al. A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans. Biotechnol Biofuels. 2018;11:74doi: 10.1186/s13068-018-1074-3.
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, 1174. https://doi.org/10.1186/s13068-018-1074-3
Razeq, Fakhria M, et al. "A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans." Biotechnology for biofuels vol. 11 (2018): 74. doi: https://doi.org/10.1186/s13068-018-1074-3
Razeq FM, Jurak E, Stogios PJ, Yan R, Tenkanen M, Kabel MA, Wang W, Master ER. A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans. Biotechnol Biofuels. 2018 Mar 22;11:74. doi: 10.1186/s13068-018-1074-3. eCollection 2018. PMID: 29588659; PMCID: PMC5863359.
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Biotechnol Biofuels. 2018 Mar 22;11:74. doi: 10.1186/s13068-018-1074-3. eCollection 2018.

A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans.

Biotechnology for biofuels

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

Affiliations

  1. 1Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON M5S 3E5 Canada.
  2. 2Department of Bioproducts and Biosystems, Aalto University, Kemistintie 1, 00076 Aalto Espoo, Finland.
  3. 3Department of Food and Environmental Sciences, University of Helsinki, P.O. Box 66, 00014 Helsinki, Finland.
  4. 4Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.

PMID: 29588659 PMCID: PMC5863359 DOI: 10.1186/s13068-018-1074-3

Abstract

BACKGROUND: Acetylated 4-

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-

CONCLUSION: This study reports the discovery and characterization of the novel carbohydrate esterase, FjoAcXE. In addition to cleaving singly acetylated Xyl

Keywords: Acetyl xylan esterase; Glucuronic acid; Polysaccharide utilization loci; SGNH hydrolase; Xylan; α-Glucuronidase

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