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Marine Bacteroidetes enzymatically digest xylans from terrestrial plants.
Dutschei, Theresa; Beidler, Irena; Bartosik, Daniel; Seeßelberg, Julia-Maria; Teune, Michelle; Bäumgen, Marcus; Ferreira, Soraia Querido; Heldmann, Julia; Nagel, Felix; Krull, Joris; Berndt, Leona; Methling, Karen; Hein, Martin; Becher, Dörte; Langer, Peter; Delcea, Mihaela; Lalk, Michael; Lammers, Michael; Höhne, Matthias; Hehemann, Jan-Hendrik; Schweder, Thomas; Bornscheuer, Uwe T.
Afiliación
  • Dutschei T; Department of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University Greifswald, Greifswald, Germany.
  • Beidler I; Department of Pharmaceutical Biotechnology, Institute of Pharmacy, University of Greifswald, Greifswald, Germany.
  • Bartosik D; Department of Pharmaceutical Biotechnology, Institute of Pharmacy, University of Greifswald, Greifswald, Germany.
  • Seeßelberg JM; Institute of Marine Biotechnology e.V., Greifswald, Germany.
  • Teune M; Department of Protein Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Bäumgen M; Department of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University Greifswald, Greifswald, Germany.
  • Ferreira SQ; Department of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University Greifswald, Greifswald, Germany.
  • Heldmann J; Department of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University Greifswald, Greifswald, Germany.
  • Nagel F; Department of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University Greifswald, Greifswald, Germany.
  • Krull J; Department of Biophysical Chemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Berndt L; Institute of Marine Biotechnology e.V., Greifswald, Germany.
  • Methling K; Center for Marine Environmental Sciences, University of Bremen, Bremen, Germany.
  • Hein M; Department of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Becher D; Department of Cellular Biochemistry and Metabolomics, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Langer P; Department of Organic Chemistry, Institute of Chemistry, University of Rostock, Rostock, Germany.
  • Delcea M; Department of Microbial Proteomics, Institute of Microbiology, University of Greifswald, Greifswald, Germany.
  • Lalk M; Department of Organic Chemistry, Institute of Chemistry, University of Rostock, Rostock, Germany.
  • Lammers M; Department of Biophysical Chemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Höhne M; Department of Cellular Biochemistry and Metabolomics, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Hehemann JH; Department of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Schweder T; Department of Protein Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
  • Bornscheuer UT; Institute of Marine Biotechnology e.V., Greifswald, Germany.
Environ Microbiol ; 25(9): 1713-1727, 2023 09.
Article en En | MEDLINE | ID: mdl-37121608
Marine 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 ß-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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Xilanos / Flavobacteriaceae Idioma: En Revista: Environ Microbiol Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Xilanos / Flavobacteriaceae Idioma: En Revista: Environ Microbiol Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido