Comprehensive functional characterization of the glycoside hydrolase family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification. (7th December 2017)
- Record Type:
- Journal Article
- Title:
- Comprehensive functional characterization of the glycoside hydrolase family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification. (7th December 2017)
- Main Title:
- Comprehensive functional characterization of the glycoside hydrolase family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification
- Authors:
- Nelson, Cassandra E.
Attia, Mohamed A.
Rogowski, Artur
Morland, Carl
Brumer, Harry
Gardner, Jeffrey G. - Other Names:
- Bakken Lars R. guestEditor.
Frostegård Åsa guestEditor. - Abstract:
- Summary: 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 relatedSummary: 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. … (more)
- Is Part Of:
- Environmental microbiology. Volume 19:Number 12(2017:Dec.)
- Journal:
- Environmental microbiology
- Issue:
- Volume 19:Number 12(2017:Dec.)
- Issue Display:
- Volume 19, Issue 12 (2017)
- Year:
- 2017
- Volume:
- 19
- Issue:
- 12
- Issue Sort Value:
- 2017-0019-0012-0000
- Page Start:
- 5025
- Page End:
- 5039
- Publication Date:
- 2017-12-07
- Subjects:
- Microbial ecology -- Periodicals
Environmental Microbiology -- Periodicals
579.17 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1462-2912;screen=info;ECOIP ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920/issues ↗
http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=emi ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1462-2920.13959 ↗
- Languages:
- English
- ISSNs:
- 1462-2912
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3791.522600
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8727.xml