Applied Microbiology and Biotechnology

, Volume 102, Issue 5, pp 2191–2201 | Cite as

A novel glucuronoyl esterase from Aspergillus fumigatus—the role of conserved Lys residue in the preference for 4-O-methyl glucuronoyl esters

  • Hung Hiep Huynh
  • Nozomi Ishii
  • Ichiro Matsuo
  • Manabu Arioka
Biotechnologically relevant enzymes and proteins


Cellulose in plant cell walls is mainly covered by hemicellulose and lignin, and thus efficient removal of these components is thought to be a key step in the optimal utilization of lignocellulose. The recently discovered carbohydrate esterase (CE) 15 family of glucuronoyl esterases (GEs) which cleave the linkages between the free carboxyl group of d-glucuronic acid in hemicellulose and the benzyl groups in lignin residues could contribute to this process. Herein, we report the identification, functional expression, and enzymatic characterization of a GE, AfGE, from the filamentous fungus Aspergillus fumigatus. AfGE was heterologously expressed in Aspergillus oryzae, and the purified enzyme displayed the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. AfGE is a potentially industrially applicable enzyme due to its characteristic as a thermophilic enzyme with the favorable temperature of 40–50 °C at pH 5. Molecular modeling and site-directed mutagenesis studies of AfGE demonstrated that Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring.


Aspergillus fumigatus Catalytic triad Glucuronoyl esterase Methoxy group Preference 



We are grateful to Dr. Daisuke Hagiwara (Medical Mycology Research Center, Chiba University, Japan) for providing the genomic DNA of the A. fumigatus Af293 strain.

Funding information

This work was supported by a Grant-in-Aid for Scientific Research (No. 16K14879) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (MEXT) and a research grant from the Institute for Fermentation, Osaka. H. H. H. is a recipient of the MEXT Scholarship.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Supplementary material

253_2018_8739_MOESM1_ESM.pdf (84 kb)
ESM 1 (PDF 84 kb)


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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Hung Hiep Huynh
    • 1
  • Nozomi Ishii
    • 2
  • Ichiro Matsuo
    • 2
  • Manabu Arioka
    • 1
  1. 1.Department of BiotechnologyThe University of TokyoTokyoJapan
  2. 2.Department of Chemistry and Chemical BiologyGunma UniversityMaebashiJapan

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