ArticleApplied and environmental microbiology2009
Characterization of two novel alpha-glucosidases from Bifidobacterium breve UCC2003.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 65 citations in OpenAlex.
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- Comparative genomics and genotype-phenotype associations in Bifidobacterium breve.Scientific reports · 2018Article
- Carbohydrate Syntrophy enhances the establishment of Bifidobacterium breve UCC2003 in the neonatal gut.Scientific reports · 2018Article
- Bifidobacteria and the infant gut: an example of co-evolution and natural selection.Cellular and molecular life sciences : CMLS · 2018Review
- The First Microbial Colonizers of the Human Gut: Composition, Activities, and Health Implications of the Infant Gut Microbiota.Microbiology and molecular biology reviews : MMBR · 2017Review
- GABA-producing Bifidobacterium dentium modulates visceral sensitivity in the intestine.Neurogastroenterology and motility · 2017Article
- Glycosulfatase-Encoding Gene Cluster in Bifidobacterium breve UCC2003.Applied and environmental microbiology · 2016Article
- Genomics of the Genus Bifidobacterium Reveals Species-Specific Adaptation to the Glycan-Rich Gut Environment.Applied and environmental microbiology · 2016Review
- Proteinaceous Molecules Mediating Bifidobacterium-Host Interactions.Frontiers in microbiology · 2016Review
- Diversity, ecology and intestinal function of bifidobacteria.Microbial cell factories · 2014Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two alpha-glucosidase-encoding genes (agl1 and agl2) from Bifidobacterium breve UCC2003 were identified and characterized. Based on their similarity to characterized carbohydrate hydrolases, the Agl1 and Agl2 enzymes are both assigned to a subgroup of the glycosyl hydrolase family 13, the alpha-1,6-glucosidases (EC 3.2.1.10). Recombinant Agl1 and Agl2 into which a His(12) sequence was incorporated (Agl1(His) and Agl2(His), respectively) exhibited hydrolytic activity towards panose, isomaltose, isomaltotriose, and four sucrose isomers--palatinose, trehalulose, turanose, and maltulose--while also degrading trehalose and, to a lesser extent, nigerose. The preferred substrates for both enzymes were panose, isomaltose, and trehalulose. Furthermore, the pH and temperature optima for both enzymes were determined, showing that Agl1(His) exhibits higher thermo and pH optima than Agl2(His). The two purified alpha-1,6-glucosidases were also shown to have transglycosylation activity, synthesizing oligosaccharides from palatinose, trehalulose, trehalose, panose, and isomaltotriose.
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