Showing papers on "Melibiose published in 2022"
TL;DR: In this article, a macroporous niobium phosphate (NbP) sample was synthesized by a sol-gel method accompanied by phase separation with co-continuous macropore structure and high P/Nb molar ratio.
7 citations
TL;DR: The novel species Furfurilactobacillus milii sp.
Abstract: Genomic characterization of Furfurilactobacillus rossiae revealed that strains which were previously identified as F. rossiae are genetically heterogeneous. The 16S rRNA gene sequences of strains FUA3430, FUA3583, C5, FUA3115 and FUA3119, were 99.6 % identical to F. rossiae but the core genome analysis revealed that these strains share less than 93 % average nucleotide identity (ANI) with the F. rossiae type strain DSM 15814T. Because the ANI value is below the threshold for delineation of bacterial species, we propose the novel species Furfurilactobacillus milii sp. nov. with the type strain FUA3430T (=DSM 113338T=LMG 32478T). Strains of F. milii have smaller genomes than F. rossiae, lack the pdu-cbi-cob-hem cluster which is responsible for 1,2-propanediol utilization in F. rossiae, and lack genes involved in ethanolamine utilization. Two strains of the novel species (FUA3430T and FUA3583) were compared to F. rossiae FUA3214. Analysis of the cellular fatty acid composition and metabolite analysis did not reveal significant differences between F. milii sp. nov. and F. rossiae FUA3124. Although the growth requirements with respect to temperature and pH were very similar, only the strain of F. rossiae utilized melibiose and d-xylose. Morphological differences were also seen in the colony and cell size of the novel compared to F. rossiae.
4 citations
TL;DR: Through the analysis of disaccharide configuration, it was found that the glycation efficiency of the reducing disacCharide linked by a 1 → 6 glycoside bond was higher than that by a1 → 4 glycosides bond, and reducing sugar with β type was better than that with α type.
Abstract: Melibiose, cellobiose, maltose, lactose, turanose, and isomaltulose were selected to be glycated with OVA. The number of free amino groups of OVA modified with different disaccharides decreased, and the secondary and tertiary structures of the modified OVA also changed greatly. Moreover, the glycation sites detected by HPLC-HCD-MS/MS were all on the sensitized epitopes of OVA, which reduced the binding ability of IgG and IgE of glycated OVA. In addition, the glycation sites with the highest DSP in different samples were located in the irregular coil region of OVA. Among the six disaccharides, the glycation reaction between melibiose and OVA was the most obvious. Through the analysis of disaccharide configuration, it was found that the glycation efficiency of the reducing disaccharide linked by a 1 → 6 glycoside bond was higher than that by a 1 → 4 glycoside bond, and reducing sugar with β type was better than that with α type. These findings would provide a theoretical reference for the use of different sugars in food production.
4 citations
TL;DR: In this paper , the proteins modified by Melibiose-derived AGE (MAGE) were identified in human body fluids, such as serum, plasma, and peritoneal fluids.
Abstract: Melibiose-derived AGE (MAGE) is an advanced glycation end-product formed in vitro in anhydrous conditions on proteins and protein-free amino acids during glycation with melibiose. Our previous studies revealed the presence of MAGE antigen in the human body and tissues of several other species, including muscles, fat, extracellular matrix, and blood. MAGE is also antigenic and induces generation of anti-MAGE antibody. The aim of this paper was to identify the proteins modified by MAGE present in human body fluids, such as serum, plasma, and peritoneal fluids. The protein-bound MAGE formed in vivo has been isolated from human blood using affinity chromatography on the resin with an immobilized anti-MAGE monoclonal antibody. Using mass spectrometry and immunochemistry it has been established that MAGE epitope is present on several human blood proteins including serum albumin, IgG, and IgA. In serum of diabetic patients, mainly the albumin and IgG were modified by MAGE, while in healthy subjects IgG and IgA carried this modification, suggesting the novel AGE can impact protein structure, contribute to auto-immunogenicity, and affect function of immunoglobulins. Some proteins in peritoneal fluid from cancer patients modified with MAGE were also observed and it indicates a potential role of MAGE in cancer.
3 citations
TL;DR: In this paper , a real-time PCR test and a culture medium based on molecular and phenotypic signatures of O80:H2 EHEC were assessed on a collection of strains and stool samples.
Abstract: Enterohemorrhagic Escherichia coli (EHEC) O80:H2, belonging to sequence type ST301, is among the main causes of hemolytic and uremic syndrome in Europe, a major concern in young children. Aside from the usual intimin and Shiga toxin virulence factors (VFs), this emerging serotype possesses a mosaic plasmid combining extra-intestinal VF- and antibiotic resistance-encoding genes. This hybrid pathotype can be involved in invasive infections, a rare occurrence in EHEC infections. Here, we aimed to optimize its detection, improve its clinical diagnosis, and identify its currently unknown reservoir. O80:H2 EHEC strains isolated in France between 2010 and 2018 were phenotypically and genetically analyzed and compared with non-O80 strains. The specificity and sensitivity of a PCR test and a culture medium designed, based on the molecular and phenotypic signatures of O80:H2 EHEC, were assessed on a collection of strains and stool samples. O80:H2 biotype analysis showed that none of the strains (n = 137) fermented melibiose versus 5% of non-O80 EHEC (n = 19/352). This loss of metabolic function is due to deletion of the entire melibiose operon associated with the insertion of a 70-pb sequence (70mel), a genetic scar shared by all ST301 strains. This metabolic hallmark was used to develop a real-time PCR test (100% sensitivity, 98.3% specificity) and a melibiose-based culture medium including antibiotics, characterized by 85% specificity and sensitivity for clinical specimens. These new tools may facilitate the diagnosis of this atypical clone, help the food industry to identify the reservoir and improve our epidemiological knowledge of this threatening and emerging clone.
2 citations
TL;DR: Melibiose could effectively induce the metabolite product of α-galactosidase by T. reesei, which showed good performance in degrading the galactose substituent from GM backbone, and can lay the foundation for the industrial technology amplification of LMW-GM production for further application.
2 citations
TL;DR: Guan et al. as mentioned in this paper used single-molecule force spectroscopy to investigate substrate-induced structural changes of MelB from Salmonella typhimurium, and showed that both substrates guide MelB transporters to populate two different mechanically stabilized states, and contribute mechanistic insights to the alternating-access action for the galactoside/cation symport catalyzed by MelB.
1 citations
TL;DR: Bacteriological methods of isolation of enterobacteria from the feces of the maize fly and their identification and morphological properties were studied: gram-negative rods collected in groups or arranged singly, the presence of a capsule was established.
Abstract: The aim of the work is to carry out bacteriological methods of isolation of enterobacteria from the feces of the maize fly and their identification.Fecal masses were selected after molting from a male maize runner named Rabbit morphs Bloodred het Pied-Sided (Fig.1). Date of release from the egg: 06/19/2020.The primary sowing of "tampon-loop" was carried out on chocolate agar and Endo medium. The final identification was carried out by the RapID ONE System test system (Thermo Fisher Scientific, USA).As a result of the work, morphological properties were studied: gram-negative rods collected in groups or arranged singly, the presence of a capsule was established.Isolated E.coli cleaved lactose, sugar aldehyde, glucose, mannitol, sorbitol, rhamnose, melibiose and arabinose, possessed enzymes lysine decarboxylase, ornithine decarboxylase, γ-glutamyltranspeptidase, reacted with aliphatic thiol.
TL;DR: Substrate hydrolysis and simultaneous formation of transgalactosylation products (α-GOS) with numerous substrates (sugar/sugar alcohols, oligosaccharides, and complex carbohydrates) which were verified by TLC and HPLC analysis.
Abstract: Abstract α-Galactosidase hydrolyzes the α-1,6-linkage present at the non-reducing end of the sugars and results in the release of galactosyl residue from oligosaccharides like melibiose, raffinose, stachyose, etc. In the present study we report, α-galactosidase from Bacillus flexus isolated from Manikaran hot springs (India). Maximum enzyme production was obtained in guar gum and soybean meal after 72 h at 150 rpm. While, the temperature/pH of production was optimized at 50 °C and 7.0, respectively. Isoenzymes (α-gal I and II) were obtained and characterized based on temperature/pH optima along with their stability profile. JS27 α-Gal II was purified with a final purification fold of 11.54. Native and SDS-PAGE were used to determine the molecular weight of the enzyme as 86 and 41 kDa, respectively, indicating its homodimeric form. JS27 α-Gal II showed optimum enzyme activity at 55 °C and pH 7 (10 min). The enzyme displayed Km value of 2.3809 mM and V max of 2.0 × 104 µmol/min/ml with pNPG as substrate. JS27 α-Gal II demonstrated substrate hydrolysis and simultaneous formation of transgalactosylation products (α-GOS) with numerous substrates (sugar/sugar alcohols, oligosaccharides, and complex carbohydrates) which were verified by TLC and HPLC analysis. α-GOS are significant functional food ingredients and can be explored as prebiotics.
TL;DR: MelBSt catalyzes the coupled transport of galactosides with cations (H+, Li+, or Na+) and is a prototype for Na+-coupled major facilitator superfamily transporters as discussed by the authors .
TL;DR: In this paper , the physicochemical properties and structures of myoglobin glycated with melibiose under different conditions were analyzed using liquid chromatography coupled with mass spectrometry, and the results indicated that the formation of in vitro MAGE adduct is initiated by coupling Melibiose to a model myoglobin protein.
Abstract: MAGE (melibiose-derived advanced glycation end-product) is the glycation product generated in the reaction of a model protein with melibiose. The in vivo analog accumulates in several tissues; however, its origin still needs explanation. In vitro MAGE is efficiently generated under dry conditions in contrast to the reaction carried in an aqueous solvent. Using liquid chromatography coupled with mass spectrometry, we analyzed the physicochemical properties and structures of myoglobin glycated with melibiose under different conditions. The targeted peptide analysis identified structurally different AGEs, including crosslinking and non-crosslinking modifications associated with lysine, arginine, and histidine residues. Glycation in a dry state was more efficient in the formation of structures containing an intact melibiose moiety (21.9%) compared to glycation under aqueous conditions (15.6%). The difference was reflected in characteristic fluorescence that results from protein structural changes and impact on a heme group of the model myoglobin protein. Finally, our results suggest that the formation of in vitro MAGE adduct is initiated by coupling melibiose to a model myoglobin protein. It is confirmed by the identification of intact melibiose moieties. The intermediate glycation product can further rearrange towards more advanced structures, including cross-links. This process can contribute to a pool of AGEs accumulating locally in vivo and affecting tissue biology.