Optimizing Salt Leakage Mitigation and Comparing Sorption-Desorption Characteristics of Polyacrylamide-Based Hydrogels.

Solid hygroscopic materials are extensively utilized in diverse fields, including adsorption heat transfer, adsorption heat storage, atmospheric water harvesting (AWH), and air conditioning dehumidification. The efficacy and energy efficiency of these materials in practical applications are significantly influenced by their adsorption and desorption properties. Yet, the introduction of inorganic salts to boost adsorption performance can result in issues like salt leakage. In this research, we prepared a polyacrylamide hydrogel through free radical polymerization, and its water-absorbing capabilities were improved by incorporating the hygroscopic salt lithium chloride. We compared it to a salt-based porous adsorbent, AlFum-LiCl, which also exhibited strong water adsorption properties and the potential for large-scale production. While AlFum-LiCl suffered from limited pores and salt leakage during high water uptake, the optimized PAM-LiCl displayed superior water sorption capabilities, showing no salt leakage even at water uptake of up to 3.5 g/g. At 25 °C, PAM-LiCl achieved equilibrium water uptake of 1.26 g/g at 30% RH and 3.15 g/g at 75% RH. In this context, utilizing 20 g of PAM-LiCl for the AWH experiment yielded daily water outputs of 8.34 L/kg at 30% RH and 16.86 L/kg at 75% RH. The salt-optimized PAM-LiCl hydrogel offers the benefit of application in higher relative humidity environments without the risk of deliquescence, underscoring its promise for atmospheric water harvesting.

Enhanced Water Sorption Performance of Polyacrylamide & Glass Fiber Paper Composites: Investigation and Comparison of Application in Desiccant Wheels.

The water sorption and desorption properties of solid adsorbent materials are crucial in rotary dehumidification systems. Metal organic frameworks (MOFs) and hydrogels are mostly at the laboratory stage due to factors like the synthesis process and yield. In this study, we utilized an eco-friendly and large-scale synthesis method to prepare polyacrylamide (PAM) hydrogels (yielding approximately 500 mL from a single polymerization). Subsequently, PAM was then coated onto glass fiber paper (GFP), which serves as a commonly employed substrate in desiccant wheels. By incorporating the hygroscopic salt LiCl and optimizing the content of each component, the water sorption performance of the composite was notably improved. The water sorption and desorption performances, as well as cycling stability, were evaluated and compared with composites containing aluminum fumarate, LiCl, and GFP (AlFum-LiCl&GFP). The results revealed that PAM-LiCl&GFP outperformed AlFum-LiCl&GFP in terms of sorption capacity throughout various relative humidity (RH) levels. It achieved a water uptake of 1.06 g·g-1 at 25 °C and 30% RH, corresponding to a water sorption rate coefficient K of 15.32 × 10-4 s-1. Furthermore, the lower desorption temperature (60 °C) resulting in a desorption ratio of 82.6%, along with the excellent cycling stability and effective performance as a desiccant wheel module, provide evidence for the potential application of PAM-LiCl&GFP in desiccant wheels.

Non-aqueous continuous-flow electrophoresis (NACFE): potential separation complement for continuous-flow organic synthesis.

We introduce non-aqueous continuous-flow electrophoresis (NACFE) in which the electrolyte is a solution of an organic salt in an aprotic organic solvent. NACFE can maintain steady-state separation of multiple hydrophobic organic species into individual molecular streams. It is a potential separation complement for continuous-flow organic synthesis. This proof-of-concept work will serve as a justification for efforts towards making NACFE a practical tool in flow chemistry.

Direct involvement of ombB, omaB, and omcB genes in extracellular reduction of Fe(III) by Geobacter sulfurreducens PCA.

The tandem gene clusters orfR-ombB-omaB-omcB and orfS-ombC-omaC-omcC of the metal-reducing bacterium Geobacter sulfurreducens PCA are responsible for trans-outer membrane electron transfer during extracellular reduction of Fe(III)-citrate and ferrihydrite [a poorly crystalline Fe(III) oxide]. Each gene cluster encodes a putative transcriptional factor (OrfR/OrfS), a porin-like outer-membrane protein (OmbB/OmbC), a periplasmic c-type cytochrome (c-Cyt, OmaB/OmaC) and an outer-membrane c-Cyt (OmcB/OmcC). The individual roles of OmbB, OmaB and OmcB in extracellular reduction of Fe(III), however, have remained either uninvestigated or controversial. Here, we showed that replacements of ombB, omaB, omcB, and ombB-omaB with an antibiotic gene in the presence of ombC-omaC-omcC had no impact on reduction of Fe(III)-citrate by G. sulfurreducens PCA. Disruption of ombB, omaB, omcB, and ombB-omaB in the absence of ombC-omaC-omcC, however, severely impaired the bacterial ability to reduce Fe(III)-citrate as well as ferrihydrite. These results unequivocally demonstrate an overlapping role of ombB-omaB-omcB and ombC-omaC-omcC in extracellular Fe(III) reduction by G. sulfurreducens PCA. Involvement of both ombB-omaB-omcB and ombC-omaC-omcC in extracellular Fe(III) reduction reflects the importance of these trans-outer membrane protein complexes in the physiology of this bacterium. Moreover, the kinetics of Fe(III)-citrate and ferrihydrite reduction by these mutants in the absence of ombC-omaC-omcC were nearly identical, which suggests that absence of any protein subunit eliminates function of OmaB/OmbB/OmcB protein complex. Finally, orfS was found to have a negative impact on the extracellular reduction of Fe(III)-citrate and ferrihydrite in G. sulfurreducens PCA probably by serving as a transcriptional repressor.

A trans-outer membrane porin-cytochrome protein complex for extracellular electron transfer by Geobacter sulfurreducens†PCA.

The multi-heme, outer membrane c-type cytochrome (c-Cyt) OmcB of Geobacter sulfurreducens was previously proposed to mediate electron transfer across the outer membrane. However, the underlying mechanism has remained uncharacterized. In G. sulfurreducens, the omcB gene is part of two tandem four-gene clusters, each is predicted to encode a transcriptional factor (OrfR/OrfS), a porin-like outer membrane protein (OmbB/OmbC), a periplasmic c-type cytochrome (OmaB/OmaC) and an outer membrane c-Cyt (OmcB/OmcC) respectively. Here, we showed that OmbB/OmbC, OmaB/OmaC and OmcB/OmcC of G. sulfurreducens PCA formed the porin-cytochrome (Pcc) protein complexes, which were involved in transferring electrons across the outer membrane. The isolated Pcc protein complexes reconstituted in proteoliposomes transferred electrons from reduced methyl viologen across the lipid bilayer of liposomes to Fe(III)-citrate and ferrihydrite. The pcc clusters were found in all eight sequenced Geobacter and 11 other bacterial genomes from six different phyla, demonstrating a widespread distribution of Pcc protein complexes in phylogenetically diverse bacteria. Deletion of ombB-omaB-omcB-orfS-ombC-omaC-omcC gene clusters had no impact on the growth of G. sulfurreducens PCA with fumarate but diminished the ability of G. sulfurreducens PCA to reduce Fe(III)-citrate and ferrihydrite. Complementation with the ombB-omaB-omcB gene cluster restored the ability of G. sulfurreducens PCA to reduce Fe(III)-citrate and ferrihydrite.

Degradation of the endoplasmic reticulum by autophagy in plants.

Eukaryotic cells have developed sophisticated strategies to contend with environmental stresses faced in their lifetime. Endoplasmic reticulum (ER) stress occurs when the accumulation of unfolded proteins within the ER exceeds the folding capacity of ER chaperones. ER stress responses have been well characterized in animals and yeast, and autophagy has been suggested to play an important role in recovery from ER stress. In plants, the unfolded protein response signaling pathways have been studied, but changes in ER morphology and ER homeostasis during ER stress have not been analyzed previously. Autophagy has been reported to function in tolerance of several stress conditions in plants, including nutrient deprivation, salt and drought stresses, oxidative stress, and pathogen infection. However, whether autophagy also functions during ER stress has not been investigated. The goal of our study was to elucidate the role and regulation of autophagy during ER stress in Arabidopsis thaliana.

Degradation of the endoplasmic reticulum by autophagy during endoplasmic reticulum stress in Arabidopsis.

In this article, we show that the endoplasmic reticulum (ER) in Arabidopsis thaliana undergoes morphological changes in structure during ER stress that can be attributed to autophagy. ER stress agents trigger autophagy as demonstrated by increased production of autophagosomes. In response to ER stress, a soluble ER marker localizes to autophagosomes and accumulates in the vacuole upon inhibition of vacuolar proteases. Membrane lamellae decorated with ribosomes were observed inside autophagic bodies, demonstrating that portions of the ER are delivered to the vacuole by autophagy during ER stress. In addition, an ER stress sensor, INOSITOL-REQUIRING ENZYME-1b (IRE1b), was found to be required for ER stress-induced autophagy. However, the IRE1b splicing target, bZIP60, did not seem to be involved, suggesting the existence of an undiscovered signaling pathway to regulate ER stress-induced autophagy in plants. Together, these results suggest that autophagy serves as a pathway for the turnover of ER membrane and its contents in response to ER stress in plants.

Autophagy: pathways for self-eating in plant cells.

Plants have developed sophisticated mechanisms to survive when in unfavorable environments. Autophagy is a macromolecule degradation pathway that recycles damaged or unwanted cell materials upon encountering stress conditions or during specific developmental processes. Over the past decade, our molecular and physiological understanding of plant autophagy has greatly increased. Most of the essential machinery required for autophagy seems to be conserved from yeast to plants. Plant autophagy has been shown to function in various stress responses, pathogen defense, and senescence. Some of its potential upstream regulators have also been identified. Here, we describe recent advances in our understanding of autophagy in plants, discuss areas of controversy, and highlight potential future directions in autophagy research.

TOR is a negative regulator of autophagy in Arabidopsis thaliana.

BACKGROUND: Autophagy is a protein degradation process by which cells recycle cytoplasmic contents under stress conditions or during senescence; a basal level of housekeeping autophagy also occurs under non-stressed conditions. Although a number of genes that function in autophagy (ATG genes) have been identified in plants, the upstream components that regulate the plant autophagy pathway are still obscure. Target of rapamycin (TOR) is a negative regulator of autophagy in both yeast and animals, and homologs of TOR in plants control plant growth and protein synthesis. However, a role for TOR in regulation of autophagy in plants has not been demonstrated previously. METHODOLOGY/PRINCIPAL FINDINGS: In this paper we used RNA interference (RNAi) to generate transgenic plants with reduced AtTOR transcript level. By observing monodansylcadaverine- (MDC) and GFP-AtATG8e-labeled autophagosomes, these plants were demonstrated to have constitutive AtATG18a-dependent autophagy. Reverse transcriptase-PCR also showed increased expression of some AtATG genes in the RNAi-AtTOR plants. Unlike autophagy induced by starvation or salt stress, an NADPH oxidase inhibitor did not inhibit the constitutive autophagy in the RNAi-AtTOR lines, indicating that AtTOR is either downstream of or in a parallel pathway to NADPH oxidase. CONCLUSIONS/SIGNIFICANCE: Together, our results provide evidence that TOR is a negative regulator of autophagy in plants.

Autophagy is required for tolerance of drought and salt stress in plants.

Autophagy is a protein degradation process in which cells recycle cytoplasmic contents when subjected to environmental stress conditions or during certain stages of development. Upon the induction of autophagy, a double membrane autophagosome forms around cytoplasmic components and delivers them to the vacuole or lysosome for degradation. In plants, autophagy has been shown previously to be induced during abiotic stresses including nutrient starvation and oxidative stress. In this paper, we demonstrate the induction of autophagy in high salt and osmotic stress conditions, concomitant with the upregulation of expression of an Arabidopsis thaliana autophagy-related gene AtATG18a. Autophagy-defective RNAi-AtATG18a plants are more sensitive to salt and drought conditions than wild-type plants, demonstrating a role for autophagy in the response to these stresses. NADPH oxidase inhibitors block autophagy induction upon nutrient starvation and salt stress, but not during osmotic stress, indicating that autophagy can be activated by NADPH oxidase-dependent or -independent pathways. Together our results indicate that diverse environmental stresses can induce autophagy and that autophagy is regulated by distinct signaling pathways in different conditions.