One type of covalent linkages connecting lignin and hemicellulose in plant cell walls is the ester linkage between 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols. An enzyme that could hydrolyze such linkages, named glucuronoyl esterase, occurs in the cellulolytic system of the wood-rotting fungus Schizophyllum commune. Here we report partial amino acid sequences of the enzyme and the results of subsequent search for homologous genes in sequenced genomes. The homologous genes of unknown functions were found in genomes of several filamentous fungi and one bacterium. The gene corresponding to the cip2 gene of Hypocrea jecorina (Trichoderma reesei), known to be up-regulated under conditions of induction of cellulolytic and hemicellulolytic enzymes, was over-expressed in H. jecorina. The product of the cip2 gene was purified to homogeneity and shown to exhibit glucuronoyl esterase activity.
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http://dx.doi.org/10.1016/j.febslet.2007.07.041 | DOI Listing |
Int J Biol Macromol
December 2024
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. Electronic address:
Lignin-carbohydrate esters (LC-esters) formed by glucuronoarabinoxylan and lignin are a key factor for the recalcitrance of corn bran, understanding LC-esters change during pretreatment and enzymatic hydrolysis by glucuronoyl esterases (GEs) is essential to the sustainable utilization of corn bran. Herein, hydrolysis performances of three GEs, SbGE15A, SbGE15B, and SbGE15C from Sordaria brevicollis with different subclades and modularity, and changes in enzyme-reachable LC-esters during different pretreatments of corn bran have been comprehensively compared. F enzymes, SbGE15B and SbGE15C showed higher catalytic activity towards model and natural substrates than F enzyme, SbGE15A.
View Article and Find Full Text PDFBiochem Biophys Res Commun
November 2024
Faculty of Engineering, Shinshu University, 4-17-1 Wakasato, Nagano, 380-8553, Japan. Electronic address:
Lignin-carbohydrate complexes (LCCs) present a considerable hurdle to the economic utilization of lignocellulosic biomass. Glucuronoyl esterase (GE) is an LCC-degrading enzyme that catalyzes the cleavage of the cross-linkages between lignin and xylan in LCCs. Benzyl-d-glucuronate (Bn-GlcA), a commercially available substrate, is widely used to evaluate GE activity assays.
View Article and Find Full Text PDFProtein J
August 2024
Lethbridge Research and Development Centre, Agriculture and Agri-Food Canada, Lethbridge, AB, Canada.
Environ Pollut
September 2024
Industrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Heroon Polytechniou 9, Zografou, 15772, Athens, Greece. Electronic address:
Plastic pollution presents a global challenge, impacting ecosystems, wildlife, and economies. Polyethylene terephthalate (PET), widely used in products like bottles, significantly contributes to this issue due to poor waste collection. In recent years, there has been increasing interest in plant biomass-degrading enzymes for plastic breakdown, due to the structural and physicochemical similarities between natural and synthetic polymers.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
May 2024
Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Life Sciences, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden.
Glucuronoyl esterases (GEs) are serine-type hydrolase enzymes belonging to carbohydrate esterase family 15 (CE15), and they play a central role in the reduction of recalcitrance in plant cell walls by cleaving ester linkages between glucuronoxylan and lignin in lignocellulose. Recent studies have suggested that bacterial CE15 enzymes are more heterogeneous in terms of sequence, structure, and substrate preferences than their fungal counterparts. However, the sequence space of bacterial GEs has still not been fully explored, and further studies on diverse enzymes could provide novel insights into new catalysts of biotechnological interest.
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