The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch
Abstract Background Glucuronoyl esterases belong to carbohydrate esterase family 15 and catalyze de-esterification. Their natural function is presumed to be cleavage of ester linkages in lignin–carbohydrate complexes particularly those linking lignin and glucuronoyl residues in xylans in hardwood. R...
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doaj-1aeca78da25446a39b047429b14fc9d82020-11-24T21:00:33ZengBMCBiotechnology for Biofuels1754-68342018-03-011111910.1186/s13068-018-1075-2The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birchCaroline Mosbech0Jesper Holck1Anne S. Meyer2Jane Wittrup Agger3Center for Bioprocess Engineering, Department of Chemical and Biochemical Engineering, Technical University of DenmarkCenter for Bioprocess Engineering, Department of Chemical and Biochemical Engineering, Technical University of DenmarkCenter for Bioprocess Engineering, Department of Chemical and Biochemical Engineering, Technical University of DenmarkCenter for Bioprocess Engineering, Department of Chemical and Biochemical Engineering, Technical University of DenmarkAbstract Background Glucuronoyl esterases belong to carbohydrate esterase family 15 and catalyze de-esterification. Their natural function is presumed to be cleavage of ester linkages in lignin–carbohydrate complexes particularly those linking lignin and glucuronoyl residues in xylans in hardwood. Results Here, we show for the first time a detailed product profile of aldouronic acids released from birchwood lignin by a glucuronoyl esterase from the white-rot fungus Cerrena unicolor (CuGE). CuGE releases substrate for GH10 endo-xylanase which results in significantly increased product release compared to the action of endo-xylanase alone. CuGE also releases neutral xylo-oligosaccharides that can be ascribed to the enzymes feruloyl esterase side activity as demonstrated by release of ferulic acid from insoluble wheat arabinoxylan. Conclusion The data verify the enzyme’s unique ability to catalyze removal of all glucuronoxylan associated with lignin and we propose that this is a direct result of enzymatic cleavage of the ester bonds connecting glucuronoxylan to lignin via 4-O-methyl glucuronoyl-ester linkages. This function appears important for the fungal organism’s ability to effectively utilize all available carbohydrates in lignocellulosic substrates. In bioprocess perspectives, this enzyme is a clear candidate for polishing lignin for residual carbohydrates to achieve pure, native lignin fractions after minimal pretreatment.http://link.springer.com/article/10.1186/s13068-018-1075-2Glucuronoyl esterasesCE15LCCGlucuronoxylanAldouronic acidsLignin |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Caroline Mosbech Jesper Holck Anne S. Meyer Jane Wittrup Agger |
spellingShingle |
Caroline Mosbech Jesper Holck Anne S. Meyer Jane Wittrup Agger The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch Biotechnology for Biofuels Glucuronoyl esterases CE15 LCC Glucuronoxylan Aldouronic acids Lignin |
author_facet |
Caroline Mosbech Jesper Holck Anne S. Meyer Jane Wittrup Agger |
author_sort |
Caroline Mosbech |
title |
The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch |
title_short |
The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch |
title_full |
The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch |
title_fullStr |
The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch |
title_full_unstemmed |
The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch |
title_sort |
natural catalytic function of cuge glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch |
publisher |
BMC |
series |
Biotechnology for Biofuels |
issn |
1754-6834 |
publishDate |
2018-03-01 |
description |
Abstract Background Glucuronoyl esterases belong to carbohydrate esterase family 15 and catalyze de-esterification. Their natural function is presumed to be cleavage of ester linkages in lignin–carbohydrate complexes particularly those linking lignin and glucuronoyl residues in xylans in hardwood. Results Here, we show for the first time a detailed product profile of aldouronic acids released from birchwood lignin by a glucuronoyl esterase from the white-rot fungus Cerrena unicolor (CuGE). CuGE releases substrate for GH10 endo-xylanase which results in significantly increased product release compared to the action of endo-xylanase alone. CuGE also releases neutral xylo-oligosaccharides that can be ascribed to the enzymes feruloyl esterase side activity as demonstrated by release of ferulic acid from insoluble wheat arabinoxylan. Conclusion The data verify the enzyme’s unique ability to catalyze removal of all glucuronoxylan associated with lignin and we propose that this is a direct result of enzymatic cleavage of the ester bonds connecting glucuronoxylan to lignin via 4-O-methyl glucuronoyl-ester linkages. This function appears important for the fungal organism’s ability to effectively utilize all available carbohydrates in lignocellulosic substrates. In bioprocess perspectives, this enzyme is a clear candidate for polishing lignin for residual carbohydrates to achieve pure, native lignin fractions after minimal pretreatment. |
topic |
Glucuronoyl esterases CE15 LCC Glucuronoxylan Aldouronic acids Lignin |
url |
http://link.springer.com/article/10.1186/s13068-018-1075-2 |
work_keys_str_mv |
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