Marine Bacteroidetes enzymatically digest xylans from terrestrial plants

Author:

Dutschei Theresa1ORCID,Beidler Irena2,Bartosik Daniel23,Seeßelberg Julia‐Maria4ORCID,Teune Michelle1ORCID,Bäumgen Marcus1,Ferreira Soraia Querido1,Heldmann Julia1,Nagel Felix5,Krull Joris36,Berndt Leona7,Methling Karen8,Hein Martin9,Becher Dörte10,Langer Peter9,Delcea Mihaela5,Lalk Michael8,Lammers Michael7,Höhne Matthias4ORCID,Hehemann Jan‐Hendrik36,Schweder Thomas23ORCID,Bornscheuer Uwe T.1

Affiliation:

1. Department of Biotechnology & Enzyme Catalysis Institute of Biochemistry, University Greifswald Greifswald Germany

2. Department of Pharmaceutical Biotechnology Institute of Pharmacy, University of Greifswald Greifswald Germany

3. Institute of Marine Biotechnology e.V. Greifswald Germany

4. Department of Protein Biochemistry Institute of Biochemistry, University of Greifswald Greifswald Germany

5. Department of Biophysical Chemistry Institute of Biochemistry, University of Greifswald Greifswald Germany

6. Center for Marine Environmental Sciences University of Bremen Bremen Germany

7. Department of Synthetic and Structural Biochemistry Institute of Biochemistry, University of Greifswald Greifswald Germany

8. Department of Cellular Biochemistry and Metabolomics Institute of Biochemistry, University of Greifswald Greifswald Germany

9. Department of Organic Chemistry Institute of Chemistry, University of Rostock Rostock Germany

10. Department of Microbial Proteomics Institute of Microbiology, University of Greifswald Greifswald Germany

Abstract

AbstractMarine Bacteroidetes that degrade polysaccharides contribute to carbon cycling in the ocean. Organic matter, including glycans from terrestrial plants, might enter the oceans through rivers. Whether marine bacteria degrade structurally related glycans from diverse sources including terrestrial plants and marine algae was previously unknown. We show that the marine bacterium Flavimarina sp. Hel_I_48 encodes two polysaccharide utilization loci (PULs) which degrade xylans from terrestrial plants and marine algae. Biochemical experiments revealed activity and specificity of the encoded xylanases and associated enzymes of these PULs. Proteomics indicated that these genomic regions respond to glucuronoxylans and arabinoxylans. Substrate specificities of key enzymes suggest dedicated metabolic pathways for xylan utilization. Some of the xylanases were active on different xylans with the conserved β‐1,4‐linked xylose main chain. Enzyme activity was consistent with growth curves showing Flavimarina sp. Hel_I_48 uses structurally different xylans. The observed abundance of related xylan‐degrading enzyme repertoires in genomes of other marine Bacteroidetes indicates similar activities are common in the ocean. The here presented data show that certain marine bacteria are genetically and biochemically variable enough to access parts of structurally diverse xylans from terrestrial plants as well as from marine algal sources.

Publisher

Wiley

Subject

Ecology, Evolution, Behavior and Systematics,Microbiology

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