Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling
Abstract
Glycoside hydrolases (GHs) are enzymes that hydrolyze polysaccharides into simple sugars. To better understand the specificity of enzyme hydrolysis within the complex matrix of polysaccharides found in the plant cell wall, we studied the reactions of individual enzymes using glycome profiling, where a comprehensive collection of cell wall glycan-directed monoclonal antibodies are used to detect polysaccharide epitopes remaining in the walls after enzyme treatment and quantitative nanostructure initiator mass spectrometry (oxime-NIMS) to determine soluble sugar products of their reactions. Single, purified enzymes from the GH5_4, GH10, and GH11 families of glycoside hydrolases hydrolyzed hemicelluloses as evidenced by the loss of specific epitopes from the glycome profiles in enzyme-treated plant biomass. The glycome profiling data were further substantiated by oxime-NIMS, which identified hexose products from hydrolysis of cellulose, and pentose-only and mixed hexose-pentose products from the hydrolysis of hemicelluloses. The GH10 enzyme proved to be reactive with the broadest diversity of xylose-backbone polysaccharide epitopes, but was incapable of reacting with glucose-backbone polysaccharides. In contrast, the GH5 and GH11 enzymes studied here showed the ability to react with both glucose- and xylose-backbone polysaccharides. The identification of enzyme specificity for a wide diversity of polysaccharide structures provided by glycome profiling, and the correlatedmore »
- Authors:
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- OSTI Identifier:
- 1618668
- Alternate Identifier(s):
- OSTI ID: 1379937
- Grant/Contract Number:
- FC02-07ER64494; AC02-05CH11231; PS02-717 06ER64304
- Resource Type:
- Published Article
- Journal Name:
- Biotechnology for Biofuels
- Additional Journal Information:
- Journal Name: Biotechnology for Biofuels Journal Volume: 10 Journal Issue: 1; Journal ID: ISSN 1754-6834
- Publisher:
- Springer Science + Business Media
- Country of Publication:
- Netherlands
- Language:
- English
- Subject:
- 09 BIOMASS FUELS; Glycoside hydrolase; Xylanase; Xyloglucanase; Glycome profiling; Nanostructure-initiator mass spectrometry; Enzyme specificity
Citation Formats
Walker, Johnnie A., Pattathil, Sivakumar, Bergeman, Lai F., Beebe, Emily T., Deng, Kai, Mirzai, Maryam, Northen, Trent R., Hahn, Michael G., and Fox, Brian G. Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling. Netherlands: N. p., 2017.
Web. doi:10.1186/s13068-017-0703-6.
Walker, Johnnie A., Pattathil, Sivakumar, Bergeman, Lai F., Beebe, Emily T., Deng, Kai, Mirzai, Maryam, Northen, Trent R., Hahn, Michael G., & Fox, Brian G. Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling. Netherlands. https://doi.org/10.1186/s13068-017-0703-6
Walker, Johnnie A., Pattathil, Sivakumar, Bergeman, Lai F., Beebe, Emily T., Deng, Kai, Mirzai, Maryam, Northen, Trent R., Hahn, Michael G., and Fox, Brian G. Thu .
"Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling". Netherlands. https://doi.org/10.1186/s13068-017-0703-6.
@article{osti_1618668,
title = {Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling},
author = {Walker, Johnnie A. and Pattathil, Sivakumar and Bergeman, Lai F. and Beebe, Emily T. and Deng, Kai and Mirzai, Maryam and Northen, Trent R. and Hahn, Michael G. and Fox, Brian G.},
abstractNote = {Glycoside hydrolases (GHs) are enzymes that hydrolyze polysaccharides into simple sugars. To better understand the specificity of enzyme hydrolysis within the complex matrix of polysaccharides found in the plant cell wall, we studied the reactions of individual enzymes using glycome profiling, where a comprehensive collection of cell wall glycan-directed monoclonal antibodies are used to detect polysaccharide epitopes remaining in the walls after enzyme treatment and quantitative nanostructure initiator mass spectrometry (oxime-NIMS) to determine soluble sugar products of their reactions. Single, purified enzymes from the GH5_4, GH10, and GH11 families of glycoside hydrolases hydrolyzed hemicelluloses as evidenced by the loss of specific epitopes from the glycome profiles in enzyme-treated plant biomass. The glycome profiling data were further substantiated by oxime-NIMS, which identified hexose products from hydrolysis of cellulose, and pentose-only and mixed hexose-pentose products from the hydrolysis of hemicelluloses. The GH10 enzyme proved to be reactive with the broadest diversity of xylose-backbone polysaccharide epitopes, but was incapable of reacting with glucose-backbone polysaccharides. In contrast, the GH5 and GH11 enzymes studied here showed the ability to react with both glucose- and xylose-backbone polysaccharides. The identification of enzyme specificity for a wide diversity of polysaccharide structures provided by glycome profiling, and the correlated identification of soluble oligosaccharide hydrolysis products provided by oxime-NIMS, offers a unique combination to understand the hydrolytic capabilities and constraints of individual enzymes as they interact with plant biomass.},
doi = {10.1186/s13068-017-0703-6},
journal = {Biotechnology for Biofuels},
number = 1,
volume = 10,
place = {Netherlands},
year = {Thu Feb 02 00:00:00 EST 2017},
month = {Thu Feb 02 00:00:00 EST 2017}
}
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https://doi.org/10.1186/s13068-017-0703-6
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