1 H NMR analysis of the lactose/β-galactosidase-derived galacto-oligosaccharide components of Vivinal® GOS up to DP5

Leeuwen, Sander S. van; Kuipers, Bas J. H.; Dijkhuizen, Lubbert; Kamerling, Johannis P.

doi:10.1016/j.carres.2014.08.012

Cited by 66 publications

(93 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GOS components and products of enzymatic digestion were analyzed by high-pH anion-exchange chromatography on a Dionex DX500 work station equipped with an ED40 pulsed amperometric detection system (HPAEC-PAD) as described previously26. The oligosaccharides were separated on a CarboPac PA-1 column (250 by 5 mm; Dionex) using a system of buffer A = 0.1 M NaOH, buffer B = 0.6 M NaOAc in 0.1 M NaOH, buffer C = deionized water and buffer D = 50 mM NaOAc.…”

Section: Methodsmentioning

confidence: 99%

“…GOS are synthesized on a large scale by incubating specific β-galactosidase enzymes with high concentrations of lactose where the enzymes form complex GOS mixtures via transglycosylation reactions that contain many molecules of differing length, linkage type and branching24252627. When consumed, GOS reach the distal colon similar to HMOs where they are degraded by resident bacteria28, promoting the growth of bacterial families, including Bifidobacteriaceae and Bacteroidaceae , in the intestine of infants in a similar ratio to that found in the gut microbiota of breast-fed infants.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Prebiotic galactooligosaccharides activate mucin and pectic galactan utilization pathways in the human gut symbiont Bacteroides thetaiotaomicron

Bueren

Leeuwen

Dijkhuizen

2017

Sci Rep

Self Cite

View full text Add to dashboard Cite

Galactooligosaccharides (GOS) are prebiotic carbohydrates that impart changes in the gut bacterial composition of formula-fed infants to more closely resemble that of breast-fed infants. Consuming human milk oligosaccharides (HMOs) provides specific bacterial strains with an advantage for colonizing the infant intestine. These same effects are seen in infants after GOS consumption, however GOS are very complex mixtures and the underlying molecular mechanisms of how GOS mimic HMOs are relatively unknown. Here we studied the effects of GOS utilization on a prominent gut symbiont, Bacteroides thetaiotaomicron, which has been previously shown to consume HMOs via mucin O-glycan degradation pathways. We show that several pathways for targeting O-mucin glycans are activated in B. thetaiotaomicron by GOS, as well as the galactan utilization sytem. Characterization of the endo-galactanase from this system identified activity on various longer GOS substrates while a subset of GOS compounds were identified as potential activators of mucin glycan metabolism in B. thetaiotaomicron. Our results show that GOS functions as an inducer of mucin-glycan pathways while providing a nutrient source in the form of β-(1 → 4)-galactan. These metabolic features of GOS mixtures may serve to explain the beneficial effects that are seen for GOS supplemented infant formula.

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Prebiotic galactooligosaccharides activate mucin and pectic galactan utilization pathways in the human gut symbiont Bacteroides thetaiotaomicron

Bueren

Leeuwen

Dijkhuizen

2017

Sci Rep

Self Cite

View full text Add to dashboard Cite

show abstract

“…34 As a typical example of the NMR analysis of the different Sia-GOS DP fractions, a short discussion of the spectra of mono- …”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 99%

Enzymatic Decoration of Prebiotic Galacto-oligosaccharides (Vivinal GOS) with Sialic Acid Using Trypanosoma cruzi trans-Sialidase and Two Bovine Sialoglycoconjugates as Donor Substrates

Wilbrink

Kate

Sanders

et al. 2015

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Decoration of prebiotic galacto-oligosaccharides (GOS) with sialic acid yields mixtures of GOS and sialylated GOS (Sia-GOS), novel products that are expected to have both prebiotic and antiadhesive functionalities. The recombinantly produced trans-sialidase enzyme from Trypanosoma cruzi (TcTS), an enzyme with the ability to transfer (α2-3)-linked sialic acid from sialogalactoglycans to asialogalactoglycans, was employed to catalyze this sialylation. As sialic acid acceptor substrates, Vivinal GOS and derived fractions of specific degree of polymerization were taken. As sialic acid donor substrates, bovine κ-casein-derived glycomacropeptide [>99% N-acetylneuraminic acid (Neu5Ac); <1% N-glycolylneuraminic acid (Neu5Gc)] and bovine blood plasma glycoprotein mixture (45% Neu5Ac; 55% Neu5Gc) were selected, yielding potential food and feed products, respectively. High-pH anion-exchange chromatography, matrix-assisted laser-desorption ionization time-of-flight mass spectrometry, and nuclear magnetic resonance spectroscopy were used for product analysis.

show abstract

“…Furthermore, a wide range of products has been examined for the synthesis of GOS by BgaD. Recently van Leeuwen et al reported the regioselectivity of the enzyme reaction by NMR analysis [16].…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of β‐galactosidase from Bacillus circulans ATCC 31382 (BgaD) and the construction of the thermophilic mutants

et al. 2015

View full text Add to dashboard Cite

b-Galactosidase (EC 3.2.1.23) from Bacillus circulans ATCC 31382, designated BgaD, exhibits high transglycosylation activity to produce galacto-oligosaccharides. BgaD has been speculated to have a multiple domain architecture including a F5/8-type C domain or a discoidin domain in the C-terminal peptide region from amino acid sequence analysis. Here, we solved the first crystal structure of the C-terminal deletion mutant BgaD-D, consisting of sugar binding, Glyco_hydro, catalytic and bacterial Ig-like domains, at 2.5A. In the asymmetric unit, two molecules of BgaD-D were identified and the value of V M was estimated to be 5.0 A 3 ÁDa À1 . It has been speculated that BgaD-D consists of four domains. From the structural analysis, however, we clarified that BgaD-D consists of five domains. We identified a new domain structure comprised of b-sheets in BgaD. The catalytic domain exhibits a TIM barrel structure with a small pocket suited for accommodating the disaccharides. Detailed structural information for the amino acid residues related to activity and substrate specificity was clarified in the catalytic domain. Furthermore, using the structural information, we successfully constructed some thermostable mutants via protein engineering method. DatabaseCoordinates for the BgaD-D structure have been deposited in the Protein Data Bank under accession code 4YPJ

show abstract

1 H NMR analysis of the lactose/β-galactosidase-derived galacto-oligosaccharide components of Vivinal® GOS up to DP5

Cited by 66 publications

References 10 publications

Prebiotic galactooligosaccharides activate mucin and pectic galactan utilization pathways in the human gut symbiont Bacteroides thetaiotaomicron

Prebiotic galactooligosaccharides activate mucin and pectic galactan utilization pathways in the human gut symbiont Bacteroides thetaiotaomicron

Enzymatic Decoration of Prebiotic Galacto-oligosaccharides (Vivinal GOS) with Sialic Acid Using Trypanosoma cruzi trans-Sialidase and Two Bovine Sialoglycoconjugates as Donor Substrates

Crystal structure of β‐galactosidase from Bacillus circulans ATCC 31382 (BgaD) and the construction of the thermophilic mutants

Contact Info

Product

Resources

About