ArticleJournal of agricultural and food chemistry2016
Transferase Activity of Lactobacillal and Bifidobacterial β-Galactosidases with Various Sugars as Galactosyl Acceptors.
Article in Journal of agricultural and food chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant IsolateACS catalysis · 2026Article
- A GH42 β‑Galactosidase from the Human IsolateACS omega · 2025Article
- Safety and Modulatory Effects of Humanized Galacto-Oligosaccharides on the Gut Microbiome.Frontiers in nutrition · 2021Article
- Discovery of Novel High-Molecular Weight Oligosaccharides Containing N-Acetylhexosamine in Bovine Colostrum Whey Permeate Hydrolyzed with Aspergillus oryzae β-Galactosidase.Journal of agricultural and food chemistry · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The β-galactosidases from Lactobacillus reuteri L103 (Lreuβgal), Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 (Lbulβgal), and Bifidobacterium breve DSM 20281 (Bbreβgal-I and Bbreβgal-II) were investigated in detail with respect to their propensity to transfer galactosyl moieties onto lactose, its hydrolysis products D-glucose and D-galactose, and certain sugar acceptors such as N-acetyl-D-glucosamine (GlcNAc), N-acetyl-D-galactosamine (GalNAc), and L-fucose (Fuc) under defined, initial velocity conditions. The rate constants or partitioning ratios (kNu/kwater) determined for these different acceptors (termed nucleophiles, Nu) were used as a measure for the ability of a certain substance to act as a galactosyl acceptor of these β-galactosidases. When using Lbulβgal or Bbreβgal-II, the galactosyl transfer to GlcNAc was 6 and 10 times higher than that to lactose, respectively. With lactose and GlcNAc used in equimolar substrate concentrations, Lbulβgal and Bbreβgal-II catalyzed the formation of N-acetyl-allolactosamine with the highest yields of 41 and 24%, respectively, as calculated from the initial GlcNAc concentration.
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Registered trials
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