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.

Johan Morrill, Evelina Kulcinskaja, Anna Maria Sulewska, Sampo Lahtinen, Henrik Stålbrand, Birte Svensson, Maher Abou Hachem

Research output: Contribution to journalArticlepeer-review

26 Citations (SciVal)

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).
Original languageEnglish
Article number26
JournalBMC Biochemistry
Volume16
Issue number1
DOIs
Publication statusPublished - 2015

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology

Keywords

  • Probiotic bacteria
  • Surface plasmon resonance
  • Mannan
  • Gut microbiota
  • Carbohydrate-binding module
  • Bifidobacterium

Fingerprint

Dive into the research topics of '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.'. Together they form a unique fingerprint.

Cite this