4.6 Article

Arabinogalactan Utilization by Bifidobacterium longum subsp. longum NCC 2705 and Bacteroides caccae ATCC 43185 in Monoculture and Coculture

期刊

MICROORGANISMS
卷 8, 期 11, 页码 -

出版社

MDPI
DOI: 10.3390/microorganisms8111703

关键词

arabinogalactan; Bifidobacterium longum; Bacteroides caccae; β -galactanase; α -L-arabinofuranosidase; β -L-arabinopyranosidase

资金

  1. NSERC (Discovery Grant)
  2. NSERC/Dairy Farmers of Ontario Industrial Research Chair in Dairy Microbiology

向作者/读者索取更多资源

Arabinogalactan (AG) has been studied as a potential prebiotic in view of stimulating bifidobacteria presence in the gut microbiota. However, bifidobacteria prefer fermentation of oligosaccharides to that of polysaccharides. The contribution of other gut bacteria may allow better growth of bifidobacteria on AG. beta-galactanases and beta-galactosidases are the main enzymes for the degradation of AG. Additional enzymes such as alpha-L-arabinofuranosidase and beta-L-arabinopyranosidase are required to remove the arabinose side chains. All of these predicted functions are encoded by the genomes of both Bifidobacterium longum subsp. longum NCC 2705 and Bacteroides caccae ATCC 43185. However, neither strain was able to grow significantly on AG, with 25% (B. longum subsp. longum NCC 2705) and 39% (Bac. caccae ATCC 43185) of AG degraded after 48-h fermentation, respectively. In this study, the beta-galactanase, beta-galactosidase, alpha-L-arabinofuranosidase, and beta-L-arabinopyranosidase from both strains were investigated. The extracellular beta-galactosidases of both B. longum subsp. longum NCC 2705 and Bac. caccae ATCC 43185 were able to cleave the beta-1,3; 1,4 and 1,6 linkages. However, the beta-galactosidase activity of B. longum subsp. longum NCC 2705 was weaker for the beta-1,4 linkage, compared with the beta-1,3 and 1,6 linkages. The arabinose side chains of AG inhibited the cleavage of beta-1,3 and 1,6 linkages by the endo-beta-galactanase from both strains, and partially inhibited the cleavage of beta-1,4 linkages by the endo-beta-1,4 galactanase from Bac. caccae ATCC 43185. The alpha-L-arabinofuranosidase and beta-L-arabinopyranosidase from both strains were unable to cleave arabinose from AG under the conditions used. These results show limited breakdown of AG by these two strains in monoculture. When cocultured with Bac. caccae ATCC 43185, B. longum subsp. longum NCC 2705 grew significantly better than in monoculture on AG after 6 h of fermentation (p < 0.05). The coculture showed 48% AG degradation after 48 h of fermentation, along with reduced pH. Furthermore, compared to monoculture of Bac. caccae ATCC 43185, the concentration of succinate significantly increased from 0.01 +/- 0.01 to 4.41 +/- 0.61 mM, whereas propionate significantly decreased from 13.07 +/- 0.37 to 9.75 +/- 2.01 mM in the coculture (p < 0.05). These results suggest that the growth and metabolic activities of Bac. caccae ATCC 43185 were restrained in the coculture, as the pH decreased due to the metabolism of B. longum subsp. longum NCC 2705.

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