This study examined multi-scale structural alterations of maize starches varying in amylose content during pasting and gelation, using Rapid Visco Analyser (RVA). At 50 °C, starch granules maintained their morphology with low viscosity. As the temperature increased to 95 °C, helical and crystal structures were destroyed, leading to granule swelling, distortion and porosity, as identified by Wide Angle X-ray Scattering and Fourier Transforms Infrared measurements at 90% moisture. This resulted in increased viscosity and the formation of a loose gel network structure. Subsequently, maintaining the temperature at 95 °C caused a decrease in viscosity as most granules disappeared, forming a reorganized flaky gel structure with larger pores. As the temperature decreased, gel porosity reduced. In high amylose content starch, the viscosity remained low and granules were partially gelatinized since the heating temperature was below the gelatinization temperature. This study is the first to detail starch multilevel structural dynamics during RVA gelatinization.

The typically low solubility and gelation capacity of plant proteins can impose challenges in the design of high-quality plant-based foods. The acid used during the precipitation step of plant protein isolate extraction can influence protein functionality. Here, acetic acid and citric acid were used to extract quinoa protein isolate (QPI) from quinoa flour, as these acids are more kosmotropic than the commonly used HCl, promoting the stabilisation of the native protein structure. While proximate analysis showed that total protein was similar for the three isolates, precipitation with kosmotropic acids increased soluble protein, which correlated positively with gel strength. Microstructure analysis revealed that these gels contained a less porous protein network with lipid droplet inclusions. This study shows that the choice of precipitation acid offers an opportunity to tailor the properties of quinoa protein isolate for application, a strategy that is likely applicable to other plant protein isolates.

Energy and environmental issues have increasingly garnered significant attention for sustainable development. Flexible and shape-stable phase change materials display great potential in regulation of environmental temperature for energy saving and human comfort. Here, inspired by the water absorption behavior of salt-tolerant animals and plants in salinity environment and the Hofmeister theory, highly stable phase change salogels (PCSGs) are fabricated through in situ polymerization of hydrophilic monomers in molten salt hydrates, which can serve multiple functions including thermal management patches, smart windows, and ice blocking coatings. The gelation principles of the polymer in high ion concentration solution are explored through the density functional theory simulation and verified the feasibility of four types of salt hydrates. The high concentration chaotropic ions strongly interacted with polymer chains and promoted the gelation at low polymer concentrations which derive highly-stable and ultra-moisturizing PCSGs with high latent heat (> 200 J g-1). The synergistic adhesion and transparency switching abilities accompanied with phase transition enable their smart thermal management. The study resolves the melting leakage and thermal cycling stability of salt hydrates, and open an avenue to fabricate flexible PCM of low cost, high latent heat, and long-term durability for energy-saving, ice-blocking, and thermal management.

Mung bean is an increasingly cultivated legume. This study compared mung bean varieties \'KPS2\' from Thailand (Th) and \'Imara\' from Tanzania (T) with a focus on protein composition, allergenicity, and techno-functional properties. Two rounds alkaline-acid extraction were performed to produce mung bean protein isolate (MBPI - Th1/T1 and Th2/T2), supernatant (S) and protein-poor residue (PPR). Mass spectrometric analysis revealed high abundance of 8 s-vicilin and 11 s-legumin in MBPI and S. Extraction removed considerable amounts of the seed albumin allergen but increased the relative abundance of cupins in MBPI. Higher vicilin levels were found in Th1 samples, contributed to increased protein solubility above pH 6.5. Th formed stronger gels which were more stable at higher frequencies. In contrast, T proteins were structurally more flexible, leading to its improved foaming ability. This study provides the knowledge and methods for appropriate selection of mung bean varieties for various food applications.

OBJECTIVE: Elucidation of the micro-mechanisms of sol-gel transition of gelling glucans with different glycosidic linkages is crucial for understanding their structure-property relationship and for various applications. Glucans with distinct molecular chain structures exhibit unique gelation behaviors. The disparate gelation phenomena observed in two methylated glucans, methylated (1,3)-β-d-glucan of curdlan (MECD) and methylated (1,4)-β-d-glucan of cellulose (MC), notwithstanding their equivalent degrees of substitution, are intricately linked to their unique molecular architectures and interactions between glucan and water.
METHODS: Density functional theory and molecular dynamics simulations focused on the electronic property distinctions between MECD and MC, alongside conformational variations during thermal gelation. Inline attenuated total reflection Fourier transform infrared spectroscopy tracked secondary structure alterations in MECD and MC. To corroborate the simulation results, additional analyses including circular dichroism, rheology, and micro-differential scanning calorimetry were performed.
RESULTS: Despite having similar thermally induced gel networks, MECD and MC display distinct physical gelation patterns and molecular-level conformational changes during gelation. The network of MC gel was formed via a \"coil-to-ring\" transition, followed by ring stacking. In contrast, the MECD gel comprised compact irregular helices accompanied by notable volume shrinkage. These variations in gelation behavior are ascribed to heightened hydrophobic interactions and diminished hydrogen bonding in both systems upon heating, resulting in gelation. These findings provide valuable insights into the microstructural changes during gelation and the thermo-gelation mechanisms of structurally similar polysaccharides.

Chicken egg white (EW) proteins possess various useful techno-functionalities, including foaming, gelling or coagulating, and emulsifying. The gelling property is one of the most important functionalities of EW proteins, affecting their versatile applications in the food and pharmaceutical industries. However, it is challenging to develop high-quality gelled foods and innovative nutraceutical supplements using native EW and its proteins. This review describes the gelling properties of EW proteins. It discusses the development and action mechanism of the physical, chemical, and biological methods and exogenous substances used in the modification of EW gels. Two main applications of EW gels, i.e., gelling agents in foods and gel-type carriers for nutraceutical delivery, are systematically summarized and discussed. In addition, the research and technological gaps between modified EW gels and their applications are highlighted. By reviewing the new modification strategies and application trends of EW gels, this paper provides insights into the development of EW gel-derived products with new and functional features.

HPAM/PEI gel is a promising material for conformance control in hydrocarbon reservoirs. However, its use in low-permeability reservoirs is limited by the high polymer concentrations present. In this study, the gelation performance of an HPAM/PEI system with HPAM < 2.0 wt.% was systematically investigated. The gelation time for HPAM concentrations ranging from 0.4 to 2.0 wt.% varied from less than 1 h to 23 days, with the highest gel strength identified as grade H. The hydrodynamic radius manifested the primary effect of HPAM on the gelation performance. Branched PEI provided superior gelation performance over linear PEI, and the gelation performance was only affected when the molecular weight of the PEI varied significantly. The optimal number ratio of the PEI-provided imine groups and the HPAM-provided carboxylic acid functional groups was approximately 1.6:1~5:1. Regarding the reservoir conditions, the temperature had a crucial effect on the hydrodynamic radius of HPAM. Salts delayed the gelation process, and the order of ionic influence was Ca2+ > Na+ > K+. The pH controlled the crosslinking reaction, primarily due to the protonation degree of PEI and the hydrolysis degree of HPAM, and the most suitable pH was approximately 10.5. Plugging experiments based on a through-type fracture showed that multi-slug plugging could significantly improve the plugging performance of the system, being favorable for its application in fractured low-permeability reservoirs.

Polymeric foamed materials are among the most widely utilized technologies for oil spill accidents and releases of oil-contaminated wastewater oil due to their porosity to absorb and separate oil/water effectively. However, a major limitation of traditional polymeric foams is their reliance on an ad/absorption mechanism as the sole method of oil capture, leading to potential oil leakage once their saturation point is exceeded. Tri-block polymer styrene-ethylene-butylene-styrene (SEBS) is a fascinating absorbent material that can bypass this limitation by both capturing oil and providing a sealing mechanism via gelation to prevent oil leakage due to its unique chemical structure. SEBS foams are produced via simultaneous crosslinking and foaming that results in an impressive expansion ratio of up to 15.2 with over 93% porosity. Most importantly, the SEBS foams show great potential as oil absorbents in spill remediation, demonstrating rapid and efficient oil absorption coupled with superhydrophobic properties. Moreover, the unique interaction between the oil and SEBS enables the formation of a physical gel, acting as an effective barrier against oil leakage. These findings indicate the potential for commercializing SEBS foam as a viable option for geotextiles to mitigate oil spill concerns from infrastructures.

Limited proteolysis, CaCl2 and carboxymethyl cellulose (CMC) have individually demonstrated ability to increase the gel strength of laboratory-extracted plant proteins. However, the syneresis effects of their combination on the gelling capacity of commercial plant protein remains unclear. This was investigated by measuring the rheological property, microstructure and protein-protein interactions of gels formed from Alcalase hydrolyzed or intact pea proteins in the presence of 0.1 % CMC and 0-25 mM CaCl2. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed the molecular weight of pea protein in the mixture were < 15 kDa after hydrolysis. The hydrolysates showed higher intrinsic fluorescence intensity and lower surface hydrophobicity than the intact proteins. Rheology showed that the storage modulus (G\') of hydrolyzed pea protein (PPH)-based gels sightly decreased compared to those of native proteins. 5-15 mM CaCl2 increased the G\' for both PP and PPH-based gels and decreased the strain in the creep-recovery test. Scanning electron microscopy (SEM) showed the presence of smaller protein aggregates in the PPH-based gels compared to PP gels and the gel network became denser, and more compact and heterogenous in the presence of 15 and 25 mM CaCl2. The gel dissociation assay revealed that hydrophobic interactions and hydrogen bonds were the dominant forces to maintain the gel structure. In vitro digestion showed that the soluble protein content in PPH-based gels was 10 ∼ 30 % higher compared to those of the PP counterpart. CaCl2 addition reduced protein digestibility with a concentration dependent behavior. The results obtained show contrasting effects of limited proteolysis and CaCl2 on the gelling capacity and digestibility of commercial pea proteins. These findings offer practical guidelines for developing pea protein-based food products with a balanced texture and protein nutrition through formulation and enzymatic pre-treatment.

The structure and functional properties of protein fibrils are closely related to environmental factors in fibrillation. Herein, soy protein isolate fibrils (SPIFs, 22 mg/mL) were prepared under acid-heating conditions in the presence of 100 mM metal ions (K+, Na+, Ca2+, Mg2+, and Fe3+). Except for Fe3+, fibrillation and subsequent larger fibril aggregates were promoted, ultimately leading to gel formation. Compared with K+ or Na+, the addition of Ca2+ or Mg2+ resulted in more organized SPIF structures with increased β-sheet contents and higher ThT fluorescence intensities. Furthermore, both of them resulted in longer fibrils with an average contour length of 700-800 nm, which significantly enhanced the storage modulus. However, the presence of Fe3+ accelerated protein hydrolysis and inhibited SPIF formation, resulting in samples consistently exhibited liquid behavior. These findings provide a foundation for understanding the influence of metal ions on regulating the fibrillation and gelling properties of SPIFs.