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 journal › Article
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).
|Research areas and keywords||
Subject classification (UKÄ) – MANDATORY
|Publication status||Published - 2015|
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: Thesis › Doctoral Thesis (compilation)