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Article Synopsis
  • TcXyn30A is an enzyme from Talaromyces cellulolyticus that acts as a reducing-end xylose-releasing exoxylanase, capable of cleaving xylose from xylan and xylooligosaccharides.
  • The first crystal structures of TcXyn30A, both with and without bound xylose, show that it forms a dimer, with the binding site for xylose located at the dimer interface.
  • Structural insights suggest that specific amino acid arrangements allow TcXyn30A to effectively bind and process various xylan derivatives, revealing important aspects of its ReX activity.
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Glucuronoxylans represent a significant fraction of woody biomass, and its decomposition is complicated by the presence of lignin-carbohydrate complexes (LCCs). Herein, LCCs from birchwood were used to investigate the potential coordinated action of a glucuronoyl esterase (TtCE15A) and two α-glucuronidases (SdeAgu115A and AxyAgu115A). When supplementing α-glucuronidase with equimolar quantities of TtCE15A, total MeGlcpA released after 72 h by SdeAgu115A and AxyAgu115A increased from 52% to 67%, and 61% to 95%, respectively.

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

Appl Microbiol Biotechnol

April 2019

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 Engineering, Nanjing Forestry University, Nanjing, 210037, Jiangsu, China.

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.

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Fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization. Therefore, identification and characterization of new FGEs are of critical importance.

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Structural characterization of hemicellulose released from corn cob in continuous flow type hydrothermal reactor.

J Biosci Bioeng

February 2019

Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University, 4-17-1 Wakasato, Nagano 380-8553, Japan; Institute of Engineering, Academic Assembly, Shinshu University, 4-17-1 Wakasato, Nagano 380-8553, Japan. Electronic address:

Hydrothermal reaction is known to be one of the most efficient procedures to extract hemicelluloses from lignocellulosic biomass. We investigated the molecular structure of xylooligosaccharides released from corn cob in a continuous flow type hydrothermal reactor designed in our group. The fraction precipitable from the extract with four volumes of ethanol was examined by H-NMR spectroscopy and MALDI-TOF MS before and after enzymatic treatment with different purified enzymes.

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