661 results on '"GALACTO-OLIGOSACCHARIDES"'
Search Results
652. Eating Yogurt Supplemented with GOS, Prunes, and Linseed (Flaxseed) May Reduce Severity of Mild Constipation in Elderly Subjects.
- Abstract
An abstract of the study "Yoghurt containing galacto-oligosaccharides, prunes and linseed reduces the severity of mild constipation in elderly subjects," by U. Sairanen and colleagues published in the 2007 issue of the "European Journal of Clinical Nutrition" is presented.
- Published
- 2007
653. Prebiotics May Benefit Infants at a High Risk of Atopy.
- Abstract
The article presents an abstract of the article "A mixture of prebiotic oligosaccharides reduces the incidence of atopic dermatitis during the first six months of age," by G. Moro, G. Boehm, et al published in July 27, 2006 issue of the "Archives of Disease in Childhood."
- Published
- 2006
654. Metabolism of oligosaccharides and starch in lactobacilli: a review.
- Author
-
Gänzle MG and Follador R
- Abstract
Oligosaccharides, compounds that are composed of 2-10 monosaccharide residues, are major carbohydrate sources in habitats populated by lactobacilli. Moreover, oligosaccharide metabolism is essential for ecological fitness of lactobacilli. Disaccharide metabolism by lactobacilli is well understood; however, few data on the metabolism of higher oligosaccharides are available. Research on the ecology of intestinal microbiota as well as the commercial application of prebiotics has shifted the interest from (digestible) disaccharides to (indigestible) higher oligosaccharides. This review provides an overview on oligosaccharide metabolism in lactobacilli. Emphasis is placed on maltodextrins, isomalto-oligosaccharides, fructo-oligosaccharides, galacto-oligosaccharides, and raffinose-family oligosaccharides. Starch is also considered. Metabolism is discussed on the basis of metabolic studies related to oligosaccharide metabolism, information on the cellular location and substrate specificity of carbohydrate transport systems, glycosyl hydrolases and phosphorylases, and the presence of metabolic genes in genomes of 38 strains of lactobacilli. Metabolic pathways for disaccharide metabolism often also enable the metabolism of tri- and tetrasaccharides. However, with the exception of amylase and levansucrase, metabolic enzymes for oligosaccharide conversion are intracellular and oligosaccharide metabolism is limited by transport. This general restriction to intracellular glycosyl hydrolases differentiates lactobacilli from other bacteria that adapted to intestinal habitats, particularly Bifidobacterium spp.
- Published
- 2012
- Full Text
- View/download PDF
655. A pseudo steady-state model for galacto-oligosaccharides synthesis with β-galactosidase from Aspergillus oryzae.
- Author
-
Vera C, Guerrero C, Illanes A, and Conejeros R
- Subjects
- Fungal Proteins metabolism, Kinetics, Oligosaccharides biosynthesis, beta-Galactosidase metabolism, Aspergillus oryzae enzymology, Fungal Proteins chemistry, Models, Chemical, Oligosaccharides chemistry, beta-Galactosidase chemistry
- Abstract
A pseudo steady-state model for the kinetically controlled synthesis of galacto-oligosaccharides (GOS) with Aspergillus oryzae β-galactosidase is presented. The model accounts for the dynamics of lactose consumption and production of galactose, glucose, di, tri, tetra, and penta-oligosaccharides during the synthesis, being able to describe the total GOS content in the reaction medium at the experimental conditions evaluated. Experimental results show that the formation of GOS containing only galactose residues is significant at high conversions of substrate, which was taken into account in the model. The formation of enzyme transition complexes was considered and reasonable assumptions were made to reduce the number of parameters to be determined. The model developed has 8 parameters; 2 of them were experimentally determined and the other 6 were estimated by fitting to the experimental data using multiresponse regression. Temperature effect on kinetic and affinity constants was determined in the range from 40 to 55°C, and the data were fitted to Arrhenius type equation. Parameters of the proposed model are independent from the enzyme load in the reaction medium and, differently from previously reported models, they have a clear biochemical meaning. The magnitude of the kinetic and affinity constants of the enzyme suggests that the liberation of galactose from the galactosyl-enzyme complex is a very slow reaction and such complex is driven into GOS formation. It also suggests that the affinity for sugars of the galactosyl-enzyme complex is higher than that of the free enzyme., (Copyright © 2011 Wiley Periodicals, Inc.)
- Published
- 2011
- Full Text
- View/download PDF
656. Short-term effect of prebiotics administration on stool characteristics and serum cytokines dynamics in very young children with acute diarrhea.
- Author
-
Vaisman N, Press J, Leibovitz E, Boehm G, and Barak V
- Subjects
- Acute Disease, Child, Preschool, Diarrhea microbiology, Diarrhea physiopathology, Dietary Supplements, Double-Blind Method, Galactose administration & dosage, Humans, Infant, Interleukins blood, Placebos, Prospective Studies, Tumor Necrosis Factor-alpha blood, Cytokines blood, Diarrhea drug therapy, Feces microbiology, Oligosaccharides administration & dosage, Prebiotics
- Abstract
We investigated the effect of a mixture of long-chain fructo-oligosaccharides, galacto-oligosaccharides and acidic oligosaccharides on the number and consistency of stools and on immune system biomarkers in 104 supplemented and non-supplemented subjects (aged 9-24 months) with acute diarrhea. Interleukin-1 (IL-1), IL-1RA, IL-6, IL-8, IL-10, TNF-α and sIL-2R cytokine levels were determined. The significant decrease in number of stools and increase in stool consistency in the supplemented group was of little clinical relevance. The only significant change in pro- and anti-inflammatory cytokines was decreased TNF-α levels in the supplemented group. Prebiotic supplementation during acute diarrhea episodes did not influence the clinical course.
- Published
- 2010
- Full Text
- View/download PDF
657. Biochemical characterization of mutants in the active site residues of the β-galactosidase enzyme of Bacillus circulans ATCC 31382
- Author
-
Jelle B. Bultema, Bas J. H. Kuipers, Lubbert Dijkhuizen, and Host-Microbe Interactions
- Subjects
β-Galactosidase ,Catalytic residue ,GH2, glycoside hydrolase family 2 ,TRANSITION-STATE ,Galacto-oligosaccharides ,medicine.disease_cause ,Article ,General Biochemistry, Genetics and Molecular Biology ,chemistry.chemical_compound ,DNA, deoxyribonucleic acid ,PCR, polymerase chain reaction ,medicine ,Glycoside hydrolase ,Beta-galactosidase ,Escherichia coli ,lcsh:QH301-705.5 ,GOS, galacto-oligosaccharides ,chemistry.chemical_classification ,METAL-BINDING ,biology ,ortho-Nitrophenyl-β-galactoside ,Mutagenesis ,Active site ,MG2+ ,beta-Galactosidase ,GLU-416 ,o-NPG, ortho-nitrophenyl-β-galactoside ,Enzyme ,chemistry ,Biochemistry ,lcsh:Biology (General) ,ESCHERICHIA-COLI ,E. COLI ,Bacillus circulans ,biology.protein ,Tm, melting temperatures ,SD, standard deviation ,Transglycosylation activity - Abstract
Highlights • Active site characteristics of the β-galactosidase enzyme of Bacillus circulans ATCC 31382. • Residues essential for catalysis were identified by structure-based alignments. • Mutational analysis identified two catalytic glutamate amino acid residues., The Bacillus circulans ATCC 31382 β-galactosidase (BgaD) is a retaining-type glycosidase of glycoside hydrolase family 2 (GH2). Its commercial enzyme preparation, Biolacta N5, is used for commercial-scale production of galacto-oligosaccharides (GOS). The BgaD active site and catalytic amino acid residues have not been studied. Using bioinformatic routines we identified two putative catalytic glutamates and two highly conserved active site histidines. The site-directed mutants E447N, E532Q, and H345F, H379F had lost (almost) all catalytic activity. This confirmed their essential role in catalysis, as general acid/base catalyst (E447) and nucleophile (E532), and as transition state stabilizers (H345, H379), respectively.
- Full Text
- View/download PDF
658. Engineering a thermostable Halothermothrix orenii β-glucosidase for improved galacto-oligosaccharide synthesis
- Author
-
Hassan, Noor, Geiger, Barbara, Gandini, Rosaria, Patel, Bharat K.C., Kittl, Roman, Haltrich, Dietmar, Nguyen, Thu-Ha, Divne, Christine, and Tan, Tien Chye
- Subjects
Transglycosylation mutants ,Halothermophile ,β-Galactosidase ,060500 MICROBIOLOGY ,Galacto-oligosaccharides ,Halothermothrix ,Lactose conversion ,Applied Microbiology and Biotechnology ,β-Glucosidase ,Biotechnology - Abstract
Lactose is produced in large amounts as a by-product from the dairy industry. This inexpensive disaccharide can be converted to more useful value-added products such as galacto-oligosaccharides (GOSs) by transgalactosylation reactions with retaining β-galactosidases (BGALs) being normally used for this purpose. Hydrolysis is always competing with the transglycosylation reaction, and hence, the yields of GOSs can be too low for industrial use. We have reported that a β-glucosidase from Halothermothrix orenii (HoBGLA) shows promising characteristics for lactose conversion and GOS synthesis. Here, we engineered HoBGLA to investigate the possibility to further improve lactose conversion and GOS production. Five variants that targeted the glycone (−1) and aglycone (+1) subsites (N222F, N294T, F417S, F417Y, and Y296F) were designed and expressed. All variants show significantly impaired catalytic activity with cellobiose and lactose as substrates. Particularly, F417S is hydrolytically crippled with cellobiose as substrate with a 1000-fold decrease in apparent kcat, but to a lesser extent affected when catalyzing hydrolysis of lactose (47-fold lower kcat). This large selective effect on cellobiose hydrolysis is manifested as a change in substrate selectivity from cellobiose to lactose. The least affected variant is F417Y, which retains the capacity to hydrolyze both cellobiose and lactose with the same relative substrate selectivity as the wild type, but with ~10-fold lower turnover numbers. Thin-layer chromatography results show that this effect is accompanied by synthesis of a particular GOS product in higher yields by Y296F and F417S compared with the other variants, whereas the variant F417Y produces a higher yield of total GOSs.
- Full Text
- View/download PDF
659. Characterisation of Bifidobacterium induced from prebiotic (Galactooligosaccharide) supplemented pigs
- Author
-
Stanley, James and Stanley, James
- Abstract
Pork is the second most consumed meat worldwide and due to its increasing global demand, there is a requirement for the commercial pig farming industry to maintain efficient production while maintaining good animal welfare standards. Since the use of antibiotics as growth promoters was banned in the EU, the use of dietary fibres as prebiotics for growth promotion in livestock is a rapidly expanding area of scientific research. As such, bacteria that are significantly affected following the addition of prebiotics to animal feed are of great interest to understand the microbe-host relationship. Bifidobacteria inhabit the mammalian gastrointestinal tract and confer several host health benefits such as increased luminal short-chain fatty acid (SCFA) concentrations, lower pathogenic colonisation in the gut and reduced intestinal inflammation. Prebiotic galacto-oligosaccharides (GOS) have been shown to enrich Bifidobacterium populations in the hindgut, which has been correlated with increased acetate, butyrate and propionate production. Such SCFA are also suggested to improve fat and protein retention. This study aims to sequence Bifidobacterium spp. isolated from pigs fed a GOS supplemented diet and identify coding regions responsible for GOS metabolism and SCFA synthesis. Bacteria isolated from pig caecal and colonic samples were sequenced using the Illumina MiSeq sequencing platform. The complete genome sequences of Bifidobacterium animalis subsp. lactis, Bifidobacterium pseudolongum and Lactobacillus reuteri are reported. The assembled circular genomes were 1.96 (B. animalis subsp. lactis), 1.94 (L. reuteri) and 1.97 (B. pseudolongum) Mb and comprised of 1542, 1772-1774 and 1570-1572 protein coding genes, respectively. B. animalis subsp. lactis possessed genes for both the LacS/LacZ and LacEF/LacG pathways to fully metabolise GOS, whereas L. reuteri and B. pseudolongum possessed only the LacS/LacLM and LacS/LacZ, respectively. Furthermore, both Bifidobacteria possess
660. Studies of the microbiota and the prebiotic effects of galacto-oligosaccharides in suckling pigs.
- Author
-
Lee, Adam and Lee, Adam
- Abstract
Suckling is a unique period in porcine development where the early-life environment affects the composition of the microbiota. Colonic samples were collected from four suckling 22-day old, pigs each, in three separate trials and the microbiome composition assessed by 16s rRNA gene sequencing. Common colonic community indicators were identified from microbiota in each trial. Data could be pooled, where performance, bacterial diversity and abundance were not significantly different between repeated trials, except for a significant difference in Jaccard Similarity. Performance positively correlated with diversity and abundance of protein digesting and short-chain fatty acid producing taxonomic units, suggesting a nutritional role for these organisms. Poorly performing piglets receiving commercial milk replacers in rescue pens do not benefit from naturally occurring prebiotic galacto- oligosaccharides otherwise found in sow milk. In a study investigating effects of complete milk replacer supplemented with galacto-oligosaccharides, milk replacer plus galacto-oligosaccharides improved gut architectural features and villus/crypt ratio throughout the gastrointestinal tract, increased the number of goblet cells and revealed a differential abundance of beneficial probiotic bacteria, particularly Lactobacillus and Bifidobacterium demonstrating that galacto-oligosaccharides may be a useful addition to animal husbandry. Rotavirus causes significant mortality, morbidity and reduced performance in neonatal pigs. In a study of late gestational sows on a commercial farm with natural endemic rotavirus challenge, supplementation with galacto-oligosaccharides during late gestation significantly increased rotavirus specific antibodies in sow colostrum, reduced the number of infected piglets and suppressed piglet faecal pathogens indicating that galacto-oligosaccharide supplementation during late gestation may have a role in veterinary health settings.
661. β-galactosidase stability at high substrate concentrations
- Author
-
Remko M. Boom, Anja E.M. Janssen, and Anja Warmerdam
- Subjects
chemistry.chemical_classification ,Enzyme stability ,Multidisciplinary ,biology ,Research ,Concentrated systems ,Substrate (chemistry) ,β-galactosidase ,Enzymatic synthesis ,Galacto-oligosaccharides ,Enzyme assay ,chemistry.chemical_compound ,Enzyme ,chemistry ,Biochemistry ,Galactose ,biology.protein ,Bacillus circulans ,Enzyme activity ,Lactose ,Food Process Engineering ,VLAG ,Nuclear chemistry - Abstract
Enzymatic synthesis of galacto-oligosaccharides is usually performed at high initial substrate concentrations since higher yields are obtained. We report here on the stability of β-galactosidase from Bacillus circulans at 25, 40, and 60°C in buffer, and in systems with initially 5.0 and 30% (w/w) lactose. In buffer, the half-life time was 220 h and 13 h at 25 and 40°C, respectively, whereas the enzyme was completely inactivated after two hours at 60°C. In systems with 5.0 and 30% (w/w) lactose, a mechanistic model was used to correct the o NPG converting activity for the presence of lactose, glucose, galactose, and oligosaccharides in the activity assay. Without correction, the stability at 5.0% (w/w) lactose was overestimated, while the stability at 30% (w/w) lactose was underestimated. The inactivation constant k d was strongly dependent on temperature in buffer, whereas only a slight increase in k d was found with temperature at high substrate concentrations. The enzyme stability was found to increase strongly with the initial substrate concentrations. The inactivation energy E a appeared to be lower at high initial substrate concentrations.
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.