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Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.
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C. thermocellum is an important candidate for sustainable and cost-effective production of bioethanol through consolidated bioprocessing. In addition to unsurpassed cellulose deconstruction, industrial application and fundamental studies would benefit from improvement of glucose and fructose consumption.
In vitro d-glucose absorption by intestinal segments from active and hibernating, irradiated and nonirradiated ground squirrels
Absorption of d-glucose by intestinal segments
Effect of large dose of reserpine given intraperitoneally on intestinal absorption of D- glucose /in vitro/ in hamsters
In vitro study of D-glucose intestinal absorption in active and hibernating, irradiated and nonirradiated ground squirrel
Catalytic decomposition of glucose in aqueous solution by thermal protenoids
Acceleration stress-induced changes in fat metabolism, level of circulating glucose and corticosterone level in rats
Serum glucose and free fatty acids in man during prolonged exercise
Polydipsia elicited by synergistic action of saccharin and glucose solution
High frequency blood glucose oscillations in man
We have elicited a reliable Raman spectral signature for glucose in rabbit aqueous humor across mammalian physiological ranges in a rabbit model stressed by recent myocardial infarction.
Nannochloropsis species have garnered significant interest for biofuel production due to their ability to accumulate high levels of triacylglycerols (TAGs), especially following nitrogen-starvation. Furthermore, the first response to nutrient starvation is the synthesis of chrysolaminarin, a soluble β-1,3-glucan with β-1,6-branching. We employ CRISPR/Cas9 to knock out two key enzymes responsible for the synthesis of this oligosaccharide: a beta-glucan synthase (BGS) gene putatively responsible for the glucose β-1,3-linkages, and a transglycosylase (TGS) which putatively catalyzes β-1,6-branching. Analysis of the biomass from the generated mutants confirmed an ~5-fold decrease in the accumulation of soluble carbohydrate following nitrogen starvation, without an observed growth defect in a diel light-cycling regime compared to CRISPR-expressing controls.
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a genetic trait that can cause hemolytic anemia. To date, over 150 nonsynonymous mutations have been identified in G6PD, with pathogenic mutations clustering near the dimer and/or tetramer interface and the allosteric NADP + -binding site. Recently, our lab identified a small molecule that activates G6PD variants by stabilizing the allosteric NADP + and dimer complex, suggesting therapeutics that target these regions may improve structural defects. Here, we elucidated the connection between allosteric NADP + binding, oligomerization, and pathogenicity to determine whether oligomer stabilization can be used as a therapeutic strategy for G6PD deficiency (G6PD def ). We first solved the crystal structure for G6PD K403Q , a mutant that mimics the physiological acetylation of wild-type G6PD in erythrocytes and demonstrated that loss of allosteric NADP + binding induces conformational changes in the dimer. These structural changes prevent tetramerization, are unique to Class I variants (the most severe form of G6PD def ), and cause the deactivation and destabilization of G6PD. We also introduced nonnative cysteines at the oligomer interfaces and found that the tetramer complex is more catalytically active and stable than the dimer. Furthermore, stabilizing the dimer and tetramer improved protein stability in clinical variants, regardless of clinical classification, with tetramerization also improving the activity of G6PD K403Q and Class I variants. These findings were validated using enzyme activity and thermostability assays, analytical size-exclusion chromatography (SEC), and SEC coupled with small-angle X-ray scattering (SEC-SAXS). Taken together, our findings suggest a potential therapeutic strategy for G6PD def and provide a foundation for future drug discovery efforts.
Biomass-derived chemicals can offer unique chemical functionality relative to petroleum-derived building blocks. To this end, here we report that β-ketoadipic acid (βKA), a C6 diacid with a β-ketone group, can be used as a performance-advantaged replacement for adipic acid in a nylon-6,6 analog. Building on our previous efforts to produce shikimate-derived products from carbohydrates, Pseudomonas putida KT2440 is engineered to produce βKA from glucose, achieving a 26 g/L titer. Following purification, βKA imparts an increase of 69 degrees C above the nylon-6,6 glass transition temperature and 20% reduced water permeability, equivalent to nylon-6,10. Molecular simulations predict that the enhanced thermal properties result from rigidity introduced by the β-ketone. Process analysis predicts that βKA can be produced for US$1.94/kg from sugars, requiring 63% less energy and emitting 43% less greenhouse gases than fossil-based adipic acid. Overall, this study illustrates the potential for βKA to serve as a useful building block for bio-based polymers.
Enzymes are nature’s catalysts, but their instability outside native environments limits practical applications. Metal–organic frameworks (MOFs) offer a promising platform for enzyme immobilization, enhancing stability, and reusability through their tunable porosity and crystallinity. While ZIF-based MOFs have been extensively studied, metal azolate framework-7 (MAF-7) remains largely unexplored for biomimetic mineralization. Its hydrophilic character makes it a promising alternative for enzyme encapsulation; however, the role of essential basic modulators such as ammonium hydroxide (NH 4 OH) on enzyme structure and function has not been investigated. Here, in this study, we examine the NH 4 OH mediated synthesis of glucose oxidase within MAF-7 using powder X-ray diffraction (PXRD), scanning electron microscopy (SEM), transmission electron microscopy (TEM), cryogenic transmission electron microscopy (cryo-TEM), and enzyme assays. Our results show that NH 4 OH modulates crystal morphology, enzyme activity, and nucleation behavior, with higher concentrations leading to partial enzyme denaturation and reduced catalytic performance. By integrating time-resolved cryo-TEM with activity assays, we uncover how modulator concentration impacts early stage crystallization and enzyme folding, a mechanistic insight not previously demonstrated in MOF systems. These findings highlight modulator chemistry as a critical, underexplored variable in MOF synthesis, advancing rational design strategies for enzyme@MOFs (E@MOF) beyond ZIFs and toward more tunable, biocompatible frameworks like MAF-7.
The industrial processing of sugars and sugar-containing mixtures is gaining widespread use as a form of renewable manufacturing from biomass. To aid in process modeling for design and optimization, a commonly available thermodynamic model is needed that describes the phase equilibrium of these compounds. This work compiles and compares models for solid–liquid and vapor–liquid phase equilibrium from the available data for the representative sugars glucose, fructose, and sucrose in the representative solvents water, methanol, and ethanol, including data for multisugar, multisolvent systems. Additionally, the nonrandom two-liquid (NRTL) model was chosen for these systems because of its widespread use in industry and the availability of parameters for many solvents and cosolutes. The association-NRTL (aNRTL) model was investigated as an improvement for modeling sugars, which may experience a high degree of association because of their many hydroxy groups. Both models accurately capture the data and are able to predict the behavior of multisugar systems with only solute–solvent interaction parameters. The aNRTL model shows an improvement over the baseline NRTL model that is most significant for sucrose, the component with the highest association strength, and least significant for fructose, which has the lowest association strength.
Energy status and nutrients regulate photosynthetic protein expression. The unicellular green alga Chromochloris zofingiensis switches off photosynthesis in the presence of exogenous glucose (+Glc) in a process that depends on hexokinase (HXK1). Here, we show that this response requires that cells lack sufficient iron (–Fe). Cells grown in –Fe+Glc accumulate triacylglycerol (TAG) while losing photosynthesis and thylakoid membranes. However, cells with an iron supplement (+Fe+Glc) maintain photosynthesis and thylakoids while still accumulating TAG. Proteomic analysis shows that known photosynthetic proteins are most depleted in heterotrophy, alongside hundreds of uncharacterized, conserved proteins. Photosynthesis repression is associated with enzyme and transporter regulation that redirects iron resources to (a) respiratory instead of photosynthetic complexes and (b) a ferredoxin-dependent desaturase pathway supporting TAG accumulation rather than thylakoid lipid synthesis. Combining insights from diverse organisms from green algae to vascular plants, we show how iron and trophic constraints on metabolism aid gene discovery for photosynthesis and biofuel production.
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common blood disorder, presenting multiple symptoms, including hemolytic anemia. It affects 400 million people worldwide, with more than 160 single mutations reported in G6PD. The most severe mutations (about 70) are classified as class I, leading to more than 90% loss of activity of the wild-type G6PD. The crystal structure of G6PD reveals these mutations are located away from the active site, concentrating around the noncatalytic NADP + -binding site and the dimer interface. However, the molecular mechanisms of class I mutant dysfunction have remained elusive, hindering the development of efficient therapies. To resolve this, we performed integral structural characterization of five G6PD mutants, including four class I mutants, associated with the noncatalytic NADP + and dimerization, using crystallography, small-angle X-ray scattering (SAXS), cryogenic electron microscopy (cryo-EM), and biophysical analyses. Comparisons with the structure and properties of the wild-type enzyme, together with molecular dynamics simulations, bring forward a universal mechanism for this severe G6PD deficiency due to the class I mutations. We highlight the role of the noncatalytic NADP + -binding site that is crucial for stabilization and ordering two β-strands in the dimer interface, which together communicate these distant structural aberrations to the active site through a network of additional interactions. This understanding elucidates potential paths for drug development targeting G6PD deficiency.