Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling

Walker, Johnnie A.; Pattathil, Sivakumar; Bergeman, Lai F.; Beebe, Emily T.; Deng, Kai; Mirzai, Maryam; Northen, Trent R.; Hahn, Michael G.; Fox, Brian G.

doi:10.1186/s13068-017-0703-6

Title: Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling

Journal Article · Thu Feb 02 00:00:00 EST 2017 · Biotechnology for Biofuels

DOI:https://doi.org/10.1186/s13068-017-0703-6· OSTI ID:1618668

Walker, Johnnie A.; Pattathil, Sivakumar; Bergeman, Lai F.; Beebe, Emily T.; Deng, Kai; Mirzai, Maryam; Northen, Trent R.; Hahn, Michael G.; Fox, Brian G.

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.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: FC02-07ER64494; AC02-05CH11231; PS02-717 06ER64304

OSTI ID:: 1618668

Alternate ID(s):: OSTI ID: 1379937

Journal Information:: Biotechnology for Biofuels, Journal Name: Biotechnology for Biofuels Vol. 10 Journal Issue: 1; ISSN 1754-6834

Publisher:: Springer Science + Business MediaCopyright Statement

Country of Publication:: Netherlands

Language:: English

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Cited by: 15 works

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Enzyme specificity

Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling Walker, Johnnie; Pattathil, Sivakumar; Bergeman, Lai https://doi.org/10.6084/m9.figshare.c.3681880 The current record is supplemented by this collection	collection	February 2017
Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling Walker, Johnnie; Pattathil, Sivakumar; Bergeman, Lai https://doi.org/10.6084/m9.figshare.c.3681880.v1 The current record is supplemented by this dataset	dataset	February 2017
MOESM1 of Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling Walker, Johnnie; Pattathil, Sivakumar; Bergeman, Lai https://doi.org/10.6084/m9.figshare.c.3681880_d1.v1 The current record is supplemented by this dataset	dataset	February 2017