Applied Microbiology and Biotechnology

, Volume 103, Issue 7, pp 3037–3048 | Cite as

Expression and characterization of two glucuronoyl esterases from Thielavia terrestris and their application in enzymatic hydrolysis of corn bran

  • Jiao Tang
  • Liangkun Long
  • Yunfeng Cao
  • Shaojun DingEmail author
Biotechnologically relevant enzymes and proteins


The thermophilic fungus Thielavia terrestris when cultured on cellulose produces a cocktail of thermal hydrolases with potential application in saccharification of lignocellulosic biomass and other biotechnological areas. Glucuronoyl esterases are considered to play a unique role as accessory enzymes in lignocellulosic material biodegradation by cleaving the covalent ester linkage between 4-O-methyl-D-glucuronic acid (MeGlcA) and lignin in lignin-carbohydrate complexes (LCCs). Two glucuronoyl esterases from T. terrestris named TtGE1 and TtGE2 were expressed in Pichia pastoris. Both esterases displayed features of thermophilic enzymes, with the optimal temperature at 45 °C and 55 °C. TtGE1 and TtGE2 exhibited activity towards methyl (4-nitrophenyl β-D-glucopyranosid) uronate (Me-GlcA-pNP) but no catalytic activity to benzyl-D-glucuronate (BnzGlcA), indicating the difference in substrate specificity from previously studied fungal GEs. A substantial increase in the release of monomeric sugars and glucuronic acid from autohydrolysis of corn bran was observed by the supplementing TtGEs into commercial xylanase; the results clearly demonstrated that the TtGEs played a significant role in this degradation process. This research on TtGEs enriches our knowledge of this novel class of fungal GEs. These newly characterized TtGEs could be used as promising accessory enzymes to improve the hydrolysis efficiency of commercial enzymes in saccharification of lignocellulosic materials due to their thermophilic characteristics.


Thielavia terrestris Glucuronoyl esterase Lignin-carbohydrate complexes Corn bran Substrate specificity 



This work was supported by a research grant (no. 31670591) from the National Natural Science Foundation of China, and a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions, and the Doctorate Fellowship Foundation of Nanjing Forestry University.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no competing interests.

Human and animal rights

This article does not contain any studies with human participants or animals.

Supplementary material

253_2019_9662_MOESM1_ESM.pdf (378 kb)
Table S1 (PDF 378 kb)
253_2019_9662_MOESM2_ESM.xlsx (25 kb)
Table S2 (XLSX 24 kb)


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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  • Jiao Tang
    • 1
  • Liangkun Long
    • 1
  • Yunfeng Cao
    • 1
  • Shaojun Ding
    • 1
    Email author
  1. 1.The Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical EngineeringNanjing Forestry UniversityNanjingChina

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