For a study, it was determined that oats, barley, algae, and mushrooms all contained β-glucans, which were dietary nutrients. The macromolecules’ immune-modulatory properties were widely recognized, but how they were digested by human gut bacteria was unknown. Bacteroides uniformis JCM 13288 T was discovered to grow on laminarin, pustulant, and porphyrin. The strain’s genome, which was roughly 5.05 megabase pairs long and comprised 4868 protein-coding genes, was sequenced. Two possible polysaccharide utilization loci for β-glucans were found from the genome based on the bacterium’s growth patterns, and related four putative genes were cloned, expressed, purified, and described. BuGH16, BuGH30, and BuGH158 were endo-acting glycoside hydrolases (GHs), while BuGH3 was an exo-acting glycoside hydrolase. BuGH3, BuGH16, and BuGH158 were able to cleave linear Exo/endo-β-1-3 links, but BuGH30 could digest endo-β-1-6 linkages. BuGH30 and BuGH158 were investigated further for their functions in glucan digestion and oligosaccharide synthesis, respectively. The BuGH30 was found to cleave long-chain β-1-6 linked glucans, yielding gentiobiose as an end product. BuGH158 was used to make oligosaccharides with degrees of polymerization ranging from 2 to 7 from soluble curdlan. Researchers showed that gut bacteria used these oligosaccharides, despite the fact that they didn’t grow or grow badly on laminarin. As a result, B. uniformis JCM 13288 T was capable of not only using β-glucans but also sharing these glycans with human gut bacteria, potentially maintaining gut microbial equilibrium.
Link:www.tandfonline.com/doi/full/10.1080/19490976.2020.1826761
