The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes.

Research output: Contribution to journalArticle

Abstract

β-Mannans are abundant and diverse plant structural and storage polysaccharides. Certain human gut microbiota members including health-promoting Bifidobacterium spp. catabolize dietary mannans. Little insight is available on the enzymology of mannan deconstruction in the gut ecological niche. Here, we report the biochemical properties of the first family 5 subfamily 8 glycoside hydrolase (GH5_8) mannanase from the probiotic bacterium Bifidobacterium animalis subsp. lactis Bl-04 (BlMan5_8).

Details

Authors
  • Johan Morrill
  • Evelina Kulcinskaja
  • Anna Maria Sulewska
  • Sampo Lahtinen
  • Henrik Stålbrand
  • Birte Svensson
  • Maher Abou Hachem
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology

Keywords

  • Probiotic bacteria, Surface plasmon resonance, Mannan, Gut microbiota, Carbohydrate-binding module, Bifidobacterium
Original languageEnglish
Article number26
JournalBMC Biochemistry
Volume16
Issue number1
Publication statusPublished - 2015
Publication categoryResearch
Peer-reviewedYes

Related research output

Johan Morrill, 2017, Lund, Sweden: Lund University, Faculty of Science, Department of Chemistry, Division of Biochemistry and Structural Biology. 245 p.

Research output: ThesisDoctoral Thesis (compilation)

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