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The present study displays a comprehensive investigation into the micro- and macrostructures of gluten and its responses to temperature-induced changes, employing various analytical techniques. The integration of time domain-nuclear magnetic resonance (TD-NMR), differential scanning calorimetry (DSC), size-exclusion high-performance liquid chromatography (SE-HPLC), field emission scanning electron microscopy (FESEM), solid-state nuclear magnetic resonance (ssNMR), and multiphoton laser microscopy (MLM) measurements facilitates the multidimensional examination of gluten's phase distribution and structure across various scales. Notably, TD-NMR helps to refine prior T2 assignments for hydrated gluten through dynamic T2 measurements at sub-zero temperatures. The innovative application of TD-NMR uncovers insights into freezable water quantities and their changes under varying temperature conditions. Through real-time analyses utilizing not only TD-NMR but also MLM techniques, along with SE-HPLC measurements, the study highlights increased lacunarities in the gluten structure, particularly between 60 and 85 °C. These structural changes are attributed to heating effects that unfold and denature proteins and culminate in aggregation and crosslinking phenomena, leading to the release of water into macropores, hence changes in the water distribution in the gluten matrix. [ABSTRACT FROM AUTHOR]

Nanocelluloses occur under various crystalline forms that are currently being selectively used for a wide variety of high performance materials. In the present study, two cellulose nanofibers (CF-I) were mercerized by alkaline treatment (CF-II) without degradation, the same molar mass of 560,000 g/mol was measured. Both samples were acid hydrolyzed, leading to cellulose nanocrystals in native (CNC-I) and mercerized (CNC-II) forms. This study focuses on the detailed characterization of these two nanoparticle morphologies (light and neutron scattering, TEM, AFM), surface chemistry (zetametry and surface charge), crystallinity (XRD, 13C NMR), and average molar mass coupled to chromatographic techniques (SEC–MALLS-RI, A4F-MALLS-RI), revealing variations in the packing of the crystalline domains. The crystal size of CNC-II is reduced by half compared to CNC-I, with molar masses of individual chains of 41,000 g/mol and 22,000 g/mol for CNC-I and CNC-II, respectively, whereas the same surface charge density is measured. This study gives an example of complementary characterization techniques as well as results to help decipher the mechanism involved in mercerization. [ABSTRACT FROM AUTHOR]

Plant lignocellulosic biomass, mostly composed of cell walls, is one of the largest, mostly untapped, reserves of renewable carbon feedstock on the planet. Energy-rich polysaccharide polymers of plant cell walls can be broken down to produce fermentable sugars used to produce bioethanol. However, the complex structure of plant cell walls, and in particular, the presence of lignin, makes them recalcitrant to enzymatic degradation. Reducing this recalcitrance represents a major technological challenge. Brachypodium distachyon is an excellent model to identify parameters underlying biomass quality of energy grasses. In this work, we identified a mutant line spa1 with a so far undescribed phenotype combining brittleness with increased elasticity of the internodes. Mutant cell walls contain less crystalline cellulose and changes in hemicellulose and lignin quality and quantity. Using a dedicated reactor to follow in real-time, the evolution of straw particle size and sugar release during enzymatic digestion, we show that, despite the increased lignin content, the spa1 mutant has a dramatic reduced recalcitrance to saccharification compared to the WT. These observations demonstrate that other parameters besides lignin content are relevant for the improvement of biomass recalcitrance in energy grasses. [ABSTRACT FROM AUTHOR]

Probiotics represent a potential strategy to influence the host's immune system thereby modulating immune response. Lipoteichoic Acid (LTA) is a major immune-stimulating component of Gram-positive cell envelopes. This amphiphilic polymer, anchored in the cytoplasmic membrane by means of its glycolipid component, typically consists of a poly (glycerol-phosphate) chain with d-alanine and/or glycosyl substitutions. LTA is known to stimulate macrophages in vitro, leading to secretion of inflammatory mediators such as Nitric Oxide (NO). This study investigates the structure-activity relationship of purified LTA from three probiotic Bacillus strains ( Bacillus cereus CH, Bacillus subtilis CU1 and Bacillus clausii O/C). LTAs were extracted from bacterial cultures and purified. Chemical modification by means of hydrolysis at pH 8.5 was performed to remove d-alanine. The molecular structure of native and modified LTAs was determined by H NMR and GC-MS, and their inflammatory potential investigated by measuring NO production by RAW 264.7 macrophages. Structural analysis revealed several differences between the newly characterized LTAs, mainly relating to their d-alanylation rates and poly (glycerol-phosphate) chain length. We observed induction of NO production by LTAs from B. subtilis and B. clausii, whereas weaker NO production was observed with B. cereus. LTA dealanylation abrogated NO production independently of the glycolipid component, suggesting that immunomodulatory potential depends on d-alanine substitutions. d-alanine may control the spatial configuration of LTAs and their recognition by cell receptors. Knowledge of molecular mechanisms behind the immunomodulatory abilities of probiotics is essential to optimize their use. [ABSTRACT FROM AUTHOR]

Lytic polysaccharide monooxygenases (LPMOs) are a class of powerful oxidative enzymes that breakdown recalcitrant polysaccharides such as cellulose. Here we investigate the action of LPMOs on cellulose fibers. After enzymatic treatment and dispersion, LPMO-treated fibers show intense fibrillation. Cellulose structure modifications visualized at different scales indicate that LPMO creates nicking points that trigger the disintegration of the cellulose fibrillar structure with rupture of chains and release of elementary nanofibrils. Investigation of LPMO action using solid-state NMR provides direct evidence of modification of accessible and inaccessible surfaces surrounding the crystalline core of the fibrils. The chains breakage likely induces modifications of the cellulose network and weakens fibers cohesion promoting their disruption. Besides the formation of new initiation sites for conventional cellulases, this work provides the first evidence of the direct oxidative action of LPMOs with the mechanical weakening of the cellulose ultrastructure. LPMOs can be viewed as promising biocatalysts for enzymatic modification or degradation of cellulose fibers. [ABSTRACT FROM AUTHOR]