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Title: Comprehensive functional characterization of the Glycoside Hydrolase Family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification

Journal Article · · Environmental Microbiology
 [1];  [2];  [3];  [3];  [2]; ORCiD logo [1]
  1. Univ. of Maryland Baltimore County (UMBC), Baltimore, MD (United States)
  2. Univ. of British Columbia, Vancouver (Canada)
  3. Newcastle Univ., Newcastle Upon Tyne (United Kingdom)

Here, lignocellulose degradation is central to the carbon cycle and renewable biotechnologies. The xyloglucan (XyG), β(1!3)/β(1!4) mixed-linkage glucan (MLG), and β(1!3) glucan components of lignocellulose represent significant carbohydrate energy sources for saprophytic microorganisms. The bacterium Cellvibrio japonicus has a robust capacity for plant polysaccharide degradation, due to a genome encoding a large contingent of Carbohydrate-Active Enzymes (CAZymes), many of whose specific functions remain unknown. Using a comprehensive genetic and biochemical approach we have delineated the physiological roles of the four C. japonicus Glycoside Hydrolase Family 3 (GH3) members on diverse β-glucans. Despite high protein sequence similarity and partially overlapping activity profiles on disaccharides, these β-glucosidases are not functionally equivalent. Bgl3A has a major role in MLG and sophorose utilization, and supports β(1!3) glucan utilization, while Bgl3B underpins cellulose utilization and supports MLG utilization. Bgl3C drives β(1!3) glucan utilization. Finally, Bgl3D is the crucial β-glucosidase for XyG utilization. This study not only sheds the light on the metabolic machinery of C. japonicus, but also expands the repertoire of characterized CAZymes for future deployment in biotechnological applications. In particular, the precise functional analysis provided here serves as a reference for informed bioinformatics on the genomes of other Cellvibrio and related species.

Research Organization:
Univ. of Maryland Baltimore County (UMBC), Baltimore, MD (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
SC0014183
OSTI ID:
1406244
Journal Information:
Environmental Microbiology, Vol. 19; ISSN 1462-2912
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 18 works
Citation information provided by
Web of Science

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Cited By (10)

Identification and characterization of α-xylosidase involved in xyloglucan degradation in Aspergillus oryzae journal November 2019
Laminarin is a major molecule in the marine carbon cycle journal March 2020
Substrate specificity, regiospecificity, and processivity in glycoside hydrolase family 74 journal July 2019
Molecular recognition of the beta‐glucans laminarin and pustulan by a SusD‐like glycan‐binding protein of a marine Bacteroidetes journal October 2018
Complete Genome Sequences of Cellvibrio japonicus Strains with Improved Growth When Using α-Diglucosides journal October 2019
In vitro and in vivo characterization of three Cellvibrio japonicus glycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions journal February 2018
Plant–necrotroph co-transcriptome networks illuminate a metabolic battlefield journal May 2019
In vitro and in vivo characterization of three Cellvibrio japonicus glycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions text January 2018
In vitro and in vivo characterization of three Cellvibrio japonicus glycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions text January 2018
Molecular recognition of the beta-glucans laminarin and pustulan by a SusD-like glycan-binding protein of a marine Bacteroidetes text January 2018

Figures / Tables (7)