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Integrated analysis of cellulose structure and properties using solid-state low-field H-NMR and photoacoustic spectroscopy.
Sci Rep
January 2025
Nonprofitable Organization Touche NPO, Sapporo, 060-004, Japan.
In this study, we explore the structural intricacies of cellulose, a polymer composed of glucose monomers arranged in a linear chain, primarily investigated through solid-state NMR techniques. Specifically, we employ low-field proton nuclear magnetic resonance (H-NMR) to delve into the diverse hydrogen atom types within the cellulose molecule. The low-field H-NMR technique allows us to discern these hydrogen atoms based on their distinct chemical shifts, providing valuable insights into the various functional groups present in cellulose.
View Article and Find Full Text PDFStereoselective 1,1'-glycosylation reactivity tuning with protecting groups.
Org Biomol Chem
January 2025
Department of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, A-1190 Austria.
Chemical 1,1'-glycosylation for the synthesis of non-reducing disaccharides is complicated by the need to simultaneously control the stereochemistry at two anomeric centers. While considerable progress has been made in the synthesis of α,α-disaccharides, the assembly of 1,1'-β,β- and 1,1'-β,α-linked non-reducing sugars has received comparatively less attention. Many naturally occurring non-reducing disaccharides and their biologically active mimetics feature asymmetrically located functional groups at different positions on the two pyranose rings, highlighting the demand for reliable stereoselective methods to synthesize fully orthogonally protected 1,1'-conjugated sugars suitable for targeted functionalisation to create important biomolecules.
View Article and Find Full Text PDFStructure and function of a β-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium.
Commun Biol
January 2025
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Galactosides are major carbohydrates that are found in plant cell walls and various prebiotic oligosaccharides. Studying the detailed biochemical functions of β-galactosidases in degrading these carbohydrates is important. In particular, identifying β-galactosidases with new substrate specificities could help in the production of potentially beneficial oligosaccharides.
View Article and Find Full Text PDFPhotoelectrocatalytic degradation of hyaluronic acid and regulation effects of its degradation products on gut microbiota in vitro.
Int J Biol Macromol
December 2024
SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, National & Local Joint Engineering Laboratory for Marine Bioactive Polysaccharide Development and Application, Liaoning Key Laboratory of Food Nutrition and Health, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China. Electronic address:
Hyaluronic acid (HA) has multiple biological activities which are closely related to its molecular weight. In the present study, the photoelectrocatalytic method was established for HA degradation and the influences of bias potentials, HO additions and reaction times on the degradation results were investigated to optimize the reaction condition. Moreover, a series of analysis methods, such as FT-IR and NMR were used to analyze chemical compositions of the degradation products, revealing that photoelectrocatalytic degradation did not damage the structural blocks of HA obviously.
View Article and Find Full Text PDFUnveiling the GT114 family: Structural characterization of A075L, a glycosyltransferase from Paramecium bursaria chlorella virus-1 (PBCV-1).
Protein Sci
December 2024
Basque Research and Technology Alliance (BRTA), Center for Cooperative Research in Biosciences (CIC bioGUNE), Derio, Spain.
Protein A075L is a β-xylosyltransferase that participates in producing the core of the N-glycans found in VP54, the major viral capsid protein of Paramecium bursaria chlorella virus-1 (PBCV-1). In this study, we present an X-ray crystallographic analysis of the apo form of A075L, along with its complexes with the sugar donor and with a trisaccharide acceptor. The protein structure shows a typical GT-B folding, with two Rossmann-like fold domains, in which the acceptor substrate binds to the N-terminal region, and the nucleotide-sugar donor binds to the C-terminal region.
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