Together, the contributions describe changes involving protein organization, cell-wall permeability, pectin networks, rheology, yield, and texture. The editorial frames plant-based food as a dynamic soft-matter system whose functional properties emerge from a hierarchy extending from individual molecules to intermediate networks and, ultimately, macroscopic behavior. Plant proteins and polysaccharides can have rigid structures, limited solubility, undesirable off-flavors, and poor texturization under conventional thermal processing.

Replacing animal-derived proteins and fats with plant sources therefore presents scientific difficulties as well as sustainability goals. The proposed alternative is to connect physical changes at one scale with observable properties at another, including mouthfeel, firmness, stability, and texture, rather than treating food processing as a collection of unrelated steps. One review examines ultrasound-assisted structural modification in plant proteins at the molecular and macro-organizational levels.

Its mechanism centers on acoustic cavitation, which generates localized shear forces, microjets, and transient temperature spikes. These effects can disrupt non-covalent interactions, partially unfurl folded polypeptide chains, and expose previously hidden hydrophobic regions. The editorial reports that this molecular realignment can improve solubility, emulsification, and gelation performance.

A second review addresses a wider processing continuum, beginning with the extraction of components from plant biomass and extending to the texturization of the resulting ingredients. It considers the integration of ultrasound with complementary electro-physical technologies in what the editorial describes as multi-technology, green processing cascades. The purpose is to connect the physical principles involved in isolation with the production of ingredients whose structures and techno-functional properties are retained or improved.

Rather than treating ultrasound and other electro-physical methods as isolated alternatives to heat, this perspective places them within coordinated processing lines and considers how multiple physical mechanisms can contribute at successive stages. The collection’s mini-review offers a more focused multiscale analysis of tomato-based matrices subjected to ultrasound or pulsed electric fields. According to the editorial, both approaches can modify cell-wall permeability and interactions within pectin networks without the thermal degradation associated with heating.

These microscopic modifications can affect macroscopic rheological properties and are reported in the tomato work to enhance lycopene bioaccessibility. The contribution therefore illustrates how targeted physical stress can be connected to process efficiency, potential nutritional value, and sensory quality in the same matrix. Its evidence is specific to tomato-based systems, however, and the editorial does not demonstrate that every response observed in those systems will occur at the same level in other plant foods.

The topic’s original research examines a finished plant-based product: tofu. In that study, the authors use multivariate modeling to evaluate the combined effects of thermosonication and coagulant type on tofu matrices. The editorial describes the analysis as a mapping of relationships among physical processing inputs, coagulant chemistry, product yield, and textural profiles.

Because the study evaluates several variables together, it seeks to clarify how processing mechanics and coagulation conditions relate to the formation and performance of a protein network. Its central methodological message is that structural optimization in plant-based foods should not rely only on empirical trial and error, but should instead use an integrated account of interacting physical and chemical inputs. Across these contributions, ultrasound and electro-physical processing are presented as distinct but complementary sources of physical stress.

Ultrasound acts through cavitation-associated mechanical effects, including shear forces and microjets, whereas pulsed electric fields impose localized electrical stress on plant material. In tomato matrices, these treatments are considered together because both can influence cell and network organization. In plant proteins, ultrasound is associated with changes to folded molecular structures and non-covalent interactions.

The soft-matter framework allows researchers to relate these molecular or cellular events to the behavior of gels, emulsions, and other organized structures, and then to properties such as solubility, stability, rheology, and texture. The editorial also places the research topic within the wider push toward sustainable food systems and connects it to the United Nations Sustainable Development Goals on zero hunger and responsible consumption and production. Its argument is that replacing animal-derived food matrices with plant-based alternatives requires more than a change in ingredients; the structures within those ingredients must also be engineered deliberately.

Non-thermal physical methods offer tools for controlling selected features without relying solely on conventional heating. Nevertheless, the editorial is a synthesis of research contributions rather than a clinical, consumer, or industrial performance study, and it does not report human health outcomes, consumer acceptance results, or large-scale manufacturing validation. The strongest conclusion is methodological: improving the texture and function of plant-based foods requires researchers to connect mechanisms across scales and model the interactions among processing variables.

Ultrasound-assisted protein modification, electric-field treatment of plant cells, combined electro-physical processing, and multivariate optimization of tofu demonstrate how this approach can be applied to different structural levels and product systems. The research topic does not establish universal gains in nutritional value, yield, sensory quality, or texture.

Subject of Research: Multiscale modification of plant-food structures using ultrasound and electro-physical processing

Article Title: Editorial: Multiscale analysis of ultrasound-assisted and electro-physical methods for modifying structure–property relationships in plant-based foods

Article References: Lamas, D. L., Lin, Y.-W., & Huang, P.-H. (2026). Editorial: Multiscale analysis of ultrasound-assisted and electro-physical methods for modifying structure–property relationships in plant-based foods. Frontiers in Soft Matter, 6, Article 2019319. https://doi.org/10.3389/frsfm.2026.2019319

Image Credits: AI Generated

DOI: 10.3389/frsfm.2026.2019319

Keywords: plant-based foods, ultrasound processing, pulsed electric fields, food structure, plant proteins, soft matter, tofu texture, tomato matrices, food engineering, Editorial, Multiscale, analysis

The aquafaba was prepared from chickpeas soaked for 24 hours and then pressure-cooked for 120 minutes. The cooking liquid was separated from the chickpeas, and its pH was measured at 6.15 ± 0.01 before being adjusted to approximately 5 with lemon juice. Its protein concentration was 1.12% on a wet basis and 17.42% on a dry basis, compared with 9.24% and 73.002% for egg white.

Aquafaba also contained less total material: its total solid content was 6.42%, compared with 12.69% for egg white. These compositional differences were consistent with the aquafaba’s lower ability to expand and stabilize foam in the study’s standardized whipping test. That test produced a marked difference between the two foaming ingredients.

After whisking, egg white reached 781.66% foaming capacity, meaning a much larger volume relative to the initial sample, while aquafaba reached 326.66%. Foam stability after 30 minutes was 97.22% for egg white and 84.03% for aquafaba. Aquafaba is not a single-component foaming agent: the study describes it as a mixture containing soluble proteins, saponins, carbohydrates, polysaccharides and fibrous components.

Proteins and saponins can contribute at interfaces, while soluble carbohydrates and polysaccharides influence the continuous phase. The measured gap nevertheless showed that the chickpea cooking liquid could foam, but did not match the expansion or persistence of egg white under the tested conditions. The researchers selected meringue as a relatively simple model of a foam and pancakes as a more complex fluid system containing starch granules, proteins and lipids.

For pancakes, the control contained 100 g of wheat flour, 40 g of egg white, 20 g of sugar, 2 g of salt, 4.5 g of baking powder and 108.5 g of water. The 50% formulation replaced 20 g of egg white with 20 g of aquafaba, while the 100% formulation replaced all 40 g of egg white with 40 g of aquafaba. For meringue, the formulations contained 250 g of powdered sugar and either 250 g of egg white, 125 g each of egg white and aquafaba, or 250 g of aquafaba.

All formulations were produced in three independent batches, with triplicate analyses and three technical replicates per production replicate. Replacing egg white lowered the density of both product types, a measured indication that the mixtures incorporated more air. Pancake batter density declined from 1.123 ± 0.003 g/mL in the egg-white control to 1.077 ± 0.03 g/mL at 50% substitution and 1.049 ± 0.03 g/mL at full substitution.

Meringue foam density fell from 0.156 ± 0.001 g/mL in the control to 0.138 ± 0.002 g/mL with 50% aquafaba and 0.123 ± 0.001 g/mL with complete replacement. These differences were significant at p < 0.05. Aquafaba therefore generated aerated systems, but the decrease in density did not translate into a stronger final structure.

Rheological measurements were conducted at 25°C and 1 Hz, equivalent to 6.28 radians per second, with strain amplitudes from 0.01% to 200%. In the linear viscoelastic region, the elastic modulus, G′, exceeded the viscous modulus, G″ for all pancake and meringue samples, indicating predominantly elastic, solid-like behavior. The egg-white controls had the highest modulus values.

Aquafaba reduced the elastic response, particularly in meringue, whose G′ values ranged from 0 to 1,600 Pa, compared with a G″ range of 0 to 400 Pa. Pancake G′ and G″ values ranged from 0 to 200 Pa and 0 to 100 Pa, respectively. Aquafaba also shifted the G′–G″ crossover in meringue to lower strain, showing that the substituted foams entered nonlinear behavior earlier.

The nonlinear response also differed by product. Meringues exhibited Type III weak strain overshoot: as strain increased, G′ declined and G″ rose before G″ decreased at the highest strains, a pattern associated with irreversible deformation and flow. At 200% strain, the pancake systems returned to strain softening after earlier strain stiffening, while the meringues shifted from shear thickening to shear thinning.

Chebyshev harmonic analysis gave the same broad distinction: pancakes showed positive third-to-first elastic coefficients and negative viscous coefficients in the nonlinear region, whereas meringues initially showed positive ratios for both before the viscous response became negative at 200% strain. Large-amplitude Lissajous–Bowditch curves separated the elastic and viscous parts of each stress cycle and showed that aquafaba reduced both stored and dissipated energy. The effect was especially pronounced in meringue made with 100% aquafaba.

Wider elastic stress loops in aquafaba-containing pancake samples indicated greater irreversible structural breakdown during flow, while narrower viscous loops and a more fluid-like response in fully substituted meringue indicated altered energy dissipation. The large-strain-to-minimum-strain elastic modulus and viscosity ratios also described the shift from linear to nonlinear behavior. Together, these observations indicated lower mechanical resistance in aquafaba-containing systems, even though the overall types of nonlinear response remained similar across the formulations.

Texture analysis confirmed that the baked products became softer as the replacement level increased. Control pancakes had a hardness of 47.49 ± 0.51 N, compared with 43.42 ± 0.52 N for the 50% formulation and 38.26 ± 2.03 N for the 100% formulation. Springiness, gumminess, chewiness and elasticity also generally decreased with more aquafaba.

For meringue, hardness fell from 69.37 ± 2.28 N in the control to 51.34 ± 1.93 N at 50% replacement and 43.28 ± 1.18 N at full replacement. Meringue fracturability declined from 60.09 ± 1.86 N to 47.67 ± 1.46 N and 42.68 ± 1.59 N, respectively. The texture measurements were consistent with the lower density, modulus and energy responses observed in the rheological analysis.

Scanning electron microscopy and cross-sectional images showed structural changes associated with the lower mechanical resistance. Pancakes containing higher proportions of aquafaba displayed fewer visible pores, while aquafaba-based meringues developed more layered and fragile structures. The images support the interpretation that the mixtures initially incorporated air but were less effective at retaining that aerated architecture during baking.

Color also changed with substitution. In pancakes, increasing aquafaba raised crumb brightness but lowered crust brightness; the highest redness values for both crumb and crust occurred in the 50% formulation. The authors associated the crust differences with the sugars and polysaccharides in aquafaba and their possible influence on Maillard browning and caramelization.

Overall, the study shows that aquafaba can perform useful foaming and structural functions in pancakes and meringues, but it does not reproduce the mechanical resistance of egg white. Its use produced lower-density, softer products with less capacity to withstand large deformation, and microscopy indicated less effective retention of incorporated air during baking. The authors identified several limitations and directions for further work: composition can vary with chickpea cultivar, genotype and preparation conditions, so future studies should test how protein, saponin, starch and soluble-carbohydrate contents affect air incorporation, deformation resistance and structural retention.

The same large-amplitude rheological approach could also be applied to other plant-based, high-shear foods. Sensory assessment, consumer acceptance and shelf-life studies would be needed before the practical performance of the most promising formulations could be fully evaluated.

Subject of Research: Laboratory assessment of aquafaba as an egg-white substitute in pancake batter and meringue foam

Article Title: Investigation of the Effects of Aquafaba Used Egg Replacers on Pancake Batter and Meringue Foam Rheology and Products Properties

Article References: Özyiğit, E., Erkoç, S., Özcan, İ., Kumcuoglu, S., & Tavman, Ş. (2026). Investigation of the Effects of Aquafaba Used Egg Replacers on Pancake Batter and Meringue Foam Rheology and Products Properties. Food Science & Nutrition, 14(10), Article e72392. https://doi.org/10.1002/fsn3.72392

Image Credits: AI Generated

DOI: 10.1002/fsn3.72392

Keywords: aquafaba, egg replacement, pancake batter, meringue foam, food rheology, large-amplitude shear, food texture, chickpea cooking water, plant-based foods, scanning electron microscopy, Investigation, Effects

The core of the review’s argument rests on two protein families that dominate oilseed meals: globulins and albumins. Globulins, the salt-soluble storage proteins that include the well-characterized 7S and 11S fractions of soybean, and albumins, the water-soluble fraction, possess exactly the technofunctional properties that food formulators crave. They stabilize emulsions, whip into foams and form gels—the three pillars of texture in everything from plant-based yogurts to meat analogues. Recent work highlighted in the review shows that the ratio between these fractions matters enormously: soybean varieties with different 11S/7S globulin ratios display markedly different structural and functional behavior, meaning breeders and processors can, in principle, tune raw material quality at the source. Similar fraction-specific behavior has been documented in rice bran, where enzymatic hydrolysis of albumin and globulin fractions alters their emulsification performance in distinct ways.

Getting those proteins out of the meal, however, is where the engineering gets interesting. Traditional alkaline extraction followed by isoelectric precipitation works, but it can damage protein structure and leave behind antinutritional compounds. The review identifies a clear trend toward non-conventional extraction technologies that are gentler, faster and often more scalable. Ultrasound-assisted extraction uses cavitation bubbles to rupture cell walls and loosen protein matrices, boosting yields from pumpkin seed press cake and chickpea flour alike. Microwave pretreatment accelerates solvent penetration and has been optimized for perilla meal protein using response surface methodology. Pulsed electric fields permeabilize seed tissue through electroporation, improving the alkaline extraction of valuable compounds from perilla seed meal, while high-pressure homogenization and dynamic high-pressure microfluidization physically shear protein aggregates—flaxseed protein isolates treated this way show reduced aggregation and enhanced functional properties.

Perhaps the most chemically inventive approaches involve alternative solvent systems. Reverse micelle extraction, in which proteins are solubilized inside surfactant-stabilized nanodroplets within an organic phase, has been applied to hemp protein isolate, with the defatting process itself influencing protein structure, functionality and aromatic profile. Deep eutectic solvents—designer mixtures of hydrogen bond donors and acceptors that behave like ionic liquids but are far less toxic—have emerged as green media for protein extraction, and molecular dynamics simulations are now revealing exactly how natural deep eutectic solvents act on rapeseed proteins at the atomic level. In cottonseed processing, deep eutectic solvents have even been used to integrate protein extraction with detoxification, simultaneously pulling out protein and removing gossypol, the toxic phenolic pigment that has historically limited cottonseed’s food use. Ultrasonic-aided extraction combined with degossypolization has similarly produced cottonseed meal protein with improved functional traits and modified molecular structure.

Once extracted, whole proteins are only half the story. The second act of the review concerns bioactive peptides: short amino acid chains, typically two to twenty residues, released when proteins are cleaved by enzymes. Enzymatic hydrolysis with proteases such as alcalase and pepsin liberates sequences that can do far more than nourish. The catalogue of activities reported for oilseed-derived peptides is striking: antioxidant effects that protect cells from oxidative damage, inhibition of angiotensin-converting enzyme (ACE) linked to blood pressure reduction, blockade of dipeptidyl peptidase-IV (DPP-IV) and α-glucosidase relevant to diabetes management, anti-inflammatory signaling in human cell lines, cholesterol-lowering effects, and antimicrobial action. Cottonseed protein hydrolysates, for example, have demonstrated antioxidant, antimicrobial and ACE-inhibitory activity, while peanut protein hydrolyzed by alcalase inhibits both ACE and renin. Pumpkin seed meal hydrolysates have yielded novel ACE-inhibitory peptides that also upregulate ACE2, and sunflower seed peptide fractions separated by ultrafiltration show hypocholesterolemic and antidiabetic potential.

Some of the most compelling evidence comes from precisely identified peptide sequences. Hempseed peptides WVSPLAGRT and IGFLIIWV have been shown to exert anti-inflammatory activity in LPS-stimulated human hepatic cells, and the same IGFLIIWV sequence—dubbed peptide H3—lowers cholesterol in a human hepatic cell line. A flaxseed-derived peptide called IPPF inhibits intestinal cholesterol absorption in Caco-2 cells and hepatic cholesterol synthesis in HepG2 cells. Novel antioxidant peptides purified from peanut meal protect liver cells against hydrogen peroxide-induced oxidative damage, and a soybean meal peptide has been shown to alleviate oxidative stress through the Keap1-Nrf2-HO-1 signaling pathway. Sunflower seed-derived peptides have progressed all the way from in silico simulation to animal models, showing antioxidant and anti-inflammatory activity in vivo—a critical step beyond test-tube chemistry.

What makes the current moment different, the authors emphasize, is the arrival of computational discovery. Rather than hydrolyzing proteins and screening the resulting soup laboriously, researchers now combine enzymatic hydrolysis with artificial intelligence-assisted peptide screening tools, molecular docking and machine learning classifiers. Deep learning frameworks for antioxidant peptide discovery, updated machine learning tools for predicting anticancer peptides, and improved toxicity predictors such as ToxinPred 3.0 allow scientists to mine protein sequences in silico, rank candidate peptides by likely activity and safety, and then validate only the most promising ones experimentally. Machine learning is also transforming antimicrobial peptide identification and design, a field where rational design has long been hampered by the complexity of structure–activity relationships. This computational pipeline dramatically compresses the discovery timeline, turning oilseed proteomes into searchable databases of therapeutic potential.

The food applications flowing from this research are already tangible. Rapeseed meal protein isolate has been tested as a supplement in texture-modified foods for the elderly, addressing a genuine clinical need for protein-dense, easy-to-swallow nutrition. Sesame seed press cake protein has been formulated into meatball analogues, and hydrolyzed sesame meal protein, free and encapsulated, has been incorporated into chitosan-based coatings that extend the shelf life of ostrich fillets. Pumpkin seed protein-based hydrogels are being used as gelatin mimics and edible inks in 3D-printed foods, while pumpkin seed protein serves as a carrier that stabilizes astaxanthin, a notoriously unstable carotenoid. Plant proteins are fortifying oat yogurt with improved storage stability and bioactivity, and hempseed protein emulsions are being stabilized through carefully chosen enzymatic treatments that modify the interfacial adsorption layer. Even the residual fiber left after rapeseed protein extraction is being characterized as a functional ingredient, and flaxseed oil cake hydrolysates have found a surprising second life as media supplements in CHO cell culture for biopharmaceutical manufacturing.

The review is candid about the obstacles standing between laboratory promise and supermarket shelves. Bioavailability remains the central question: a peptide that inhibits ACE in a assay must survive stomach acid, digestive enzymes and the intestinal barrier to have any chance of acting in the body, and simulated digestion studies show that activity can change substantially along the way. Bitterness is a persistent sensory problem, since hydrophobic peptides—the very sequences often responsible for bioactivity—also activate bitter taste receptors, and bioinformatics is increasingly deployed to understand and predict peptide bitterness. Storage stability within real food matrices, the effects of processing and fortification on peptide integrity, allergenicity concerns that hydrolysis can either mitigate or complicate, regulatory pathways for novel food ingredients, and the sheer economics of commercialization all demand attention before oilseed peptides become mainstream functional ingredients.

Still, the trajectory is unmistakable. With the global population projected to approach nearly ten billion by mid-century and demand for sustainable protein intensifying, the review positions oilseed byproducts as a resource the food industry can no longer afford to discard. The convergence of green extraction technologies, precision enzymology, AI-driven peptide discovery and a growing body of in vivo validation suggests that the defatted cake sitting in an oil mill today could become tomorrow’s emulsifier in a plant-based cheese, the antihypertensive ingredient in a functional beverage, or the bioactive payload in a nutraceutical capsule. What was once waste, the authors argue, is now a strategic raw material—and the science of unlocking it is advancing on every front at once.

Subject of Research: Functional proteins and bioactive peptides from oilseed processing byproducts

Article Title: Oilseed processing byproducts as sources of functional proteins and bioactive peptides: extraction technologies, enzymatic hydrolysis, and food applications

Article References: Thoe, Y. Y. W., Yap, P.-G., Gan, C.-Y., Setyawan, H. Y., & Huda, N. (2026). Oilseed processing byproducts as sources of functional proteins and bioactive peptides: extraction technologies, enzymatic hydrolysis, and food applications. Food Science and Biotechnology. https://doi.org/10.1007/s10068-026-02333-3

Image Credits: AI Generated

DOI: 10.1007/s10068-026-02333-3

Keywords: oilseed byproducts, bioactive peptides, functional proteins, protein extraction, enzymatic hydrolysis, ultrasound-assisted extraction, deep eutectic solvents, ACE-inhibitory peptides, plant-based foods, food science, artificial intelligence, sustainability

The research team, led by Yong Liang, Wei Wang, Kai Huang, Zhengxing Chen, and Tao Wang, began from a well-known obstacle. Rice proteins are nutritionally attractive because they offer a balanced profile of essential amino acids and low allergenicity, but as foam stabilizers they are notoriously difficult. They are largely insoluble in water and prone to severe aggregation, which prevents them from diffusing quickly to the air-water interface and forming a coherent film. Foams stabilized by plant protein particles alone often collapse within seconds or minutes, because these proteins tend to sit more comfortably in the air phase than in the liquid phase, leaving the foam vulnerable to rapid water drainage. Enhancing the water retention capacity of the interfacial film therefore became the central design goal of the work.

To solve the solubility problem, the researchers co-assembled rice proteins with soy protein isolates using a pathway of alkali solvation followed by acid precipitation. Both proteins were first unfolded at high pH, allowed to interact, and then refolded together into uniform, water-dispersible nanoparticles. Transmission electron microscopy showed that while rice proteins alone formed aggregates of roughly thirty-nanometer elementary particles, the co-assembled rice-soy protein nanoparticles, prepared at a one-to-one mass ratio, emerged as monodisperse particles of about forty nanometers. Zeta potential measurements revealed something unexpected: the complexes carried stronger surface charges than either protein alone, while their surface hydrophobicity was lower than that of either parent protein. This indicated that the hydrophobic groups of both proteins had been buried inside the co-assembled structures while the charged groups were exposed outward, a rearrangement driven by hydrophobic interactions, electrostatic attraction, and hydrogen bonding.

These nanoparticles already improved foaming. Soy protein isolates alone could generate foams filling seventy-five percent of the initial dispersion volume, but only five percent survived thirty minutes. The co-assembled rice-soy nanoparticles at optimal ratios reached one hundred percent foaming ability and pushed thirty-minute stability to roughly fifteen percent at higher concentrations, plateauing at fifty percent survival once the interface became saturated. That was progress, but more than eighty-five percent of the foam still vanished within half an hour. The team then turned to starch nanocrystals, rigid platelets produced by hydrolyzing waxy corn starch in sulfuric acid for seven days. These crystals carry abundant hydroxyl groups on their surfaces, making them strongly hydrophilic and mechanically robust, but they also aggregate heavily through hydrogen bonding between their faces.

When the protein nanoparticles and starch nanocrystals were simply mixed together, the two components associated into hybrid complexes the researchers call RSP@SNCs. Atomic force microscopy revealed that the aggregated starch crystals disaggregated and reappeared as sheet-like hybrid nanoparticles of one hundred to two hundred nanometers, a morphology distinct from either component. Intrinsic fluorescence spectroscopy provided quantitative evidence of close association: as starch nanocrystal concentration increased, the fluorescence of the protein’s aromatic amino acid residues was progressively quenched, following an apparent Stern-Volmer-type relationship with a mass-based quenching coefficient of 1.896 milliliters per milligram and a correlation coefficient of 0.9677. Fourier transform infrared spectroscopy showed no new absorption bands or significant shifts, confirming that the binding was non-covalent.

The molecular glue holding the complexes together turned out to be hydrogen bonding. In a clever chemical blocking experiment, the team repeated the complexation in the presence of sodium chloride, sodium dodecyl sulfate, or thiourea, which selectively disrupt ionic forces, hydrophobic attractions, and hydrogen bonding respectively. Thiourea dramatically weakened the protein-starch interactions and restored fluorescence, while the salt and surfactant had only minor effects. Because the starch nanocrystals self-aggregate primarily through hydrogen bonds between their hydroxyl groups, competition from protein-starch hydrogen bonding appears to reduce the surface energy of the crystals, suppressing their self-aggregation and yielding dispersed hybrids with balanced amphiphilic character, exactly what is needed to anchor at an air-water interface.

The foaming results were striking. Adding starch nanocrystals doubled the initial foam formation of the protein nanoparticles at the highest tested ratio of 1.2, while optical microscopy showed that bubbles became smaller and more homogeneous as the starch proportion rose. Confocal laser scanning microscopy, with proteins and starch labeled in different fluorescent colors, revealed that both components were jointly trapped at the air-water interface, forming a thick physical barrier around each bubble. In foams stabilized by protein alone, bubbles approached a millimeter in size with thin, patchy coverage; with the hybrids at a ratio of 0.8, bubble sizes dropped to hundreds of micrometers and the liquid-filled spaces between adjacent bubbles widened, reducing direct bubble contact and hindering coalescence.

The stabilization mechanism operates on three coupled fronts. First, the interfacial film itself: contact angle measurements showed starch nanocrystals are highly hydrophilic at forty degrees while rice-soy protein nanoparticles are more hydrophobic at seventy-nine degrees, and the hybrids strike a balance that wets both phases, lowers interfacial tension, and satisfies the Gibbs stability criterion against coarsening. Second, the bulk viscosity: shear rheology demonstrated that viscosity of the stabilizer dispersions increased with starch content, and cryo-scanning electron microscopy performed at minus 145 degrees Celsius revealed ordered hybrid structures arranged throughout the continuous phase, not just at the interface. These ordered microstructures elevated system viscosity, slowing bubble disproportionation and liquid drainage. Notably, the dispersions showed shear-thinning behavior, meaning that during the violence of whipping the mixture temporarily thins, allowing particles to race to the interface, after which viscosity rebuilds to lock the structure in place. Third, water retention: the hydrophilic starch crystals trap water in the interstitial spaces between bubbles, deterring the gravity-driven drainage that kills most foams.

The practical implications extend well beyond the laboratory. The authors point to applications in milky tea, lattes, and other foamed beverages where stability over hours rather than minutes would transform product quality, particularly for delivery and takeaway markets. Because every ingredient is edible and plant-derived, the system sidesteps the limitation of surfactant crystals, which can produce extraordinarily stable foams but are not food-grade. The work also demonstrates a broader design principle: rather than searching for a single miracle stabilizer, combining a diffusion-competent protein nanoparticle with a mechanically strong, hydrophilic nanocrystal produces synergy that neither component achieves alone. As demand grows for plant-based, low-calorie foods with indulgent textures, engineering the air-water interface with hybrid biocolloids may become a standard tool in the food engineer’s repertoire, turning one of the most fragile structures in cuisine into one of the most durable.

Subject of Research: Stabilization of aqueous food foams using rice and soy protein nanoparticles reinforced with starch nanocrystals

Article Title: Starch nanocrystals reinforce rice/soy protein-structured air-water interface to stabilize aqueous foams

Article References: Liang, Y., Wang, W., Huang, K., Chen, Z., & Wang, T. (2026). Starch nanocrystals reinforce rice/soy protein-structured air-water interface to stabilize aqueous foams. Journal of Agriculture and Food Research, Article 103352. https://doi.org/10.1016/j.jafr.2026.103352

Image Credits: AI Generated

DOI: 10.1016/j.jafr.2026.103352

Keywords: aqueous foams, starch nanocrystals, rice protein, soy protein isolate, food colloids, air-water interface, hydrogen bonding, foam stability, plant-based foods, Pickering stabilization, interfacial tension, food engineering

A research team led by Shaoning Cui and Han Du set out to test whether cellulose nanocrystals, or CNCs, could slow the retrogradation of pea starch. CNCs are rigid, rod-like crystalline fragments of cellulose, typically 100 to 500 nanometers long and 10 to 50 nanometers wide, produced by dissolving away the amorphous portions of microcrystalline cellulose with sulfuric acid. Unlike flexible polysaccharides such as chitosan or alginate, which behave like soft polymer chains, CNCs behave more like microscopic reinforcing bars. Their surfaces are studded with hydroxyl groups that can form hydrogen bonds with neighboring molecules, and their stiff geometry prevents them from tangling with one another. The team hypothesized that these rods would fight retrogradation in two ways at once: by competitively binding water that starch chains need to mobilize, and by physically blocking the realignment of amylose and amylopectin chains as the gel ages.

To test the idea, the researchers hydrolyzed wheat-straw-derived microcrystalline cellulose with 65 percent sulfuric acid under sonication, then purified the resulting rods by repeated centrifugation and dialysis. Transmission electron microscopy confirmed the classic whisker morphology, while dynamic light scattering revealed a zeta potential of −36.9 millivolts, a negative surface charge imparted by sulfate ester groups that keeps the particles stably dispersed in water. X-ray diffraction showed that the acid treatment had stripped out the disordered regions of the parent cellulose, raising the crystallinity index from 62.26 percent to 88.71 percent. These intrinsic properties—a high aspect ratio, strong surface charge, and near-perfect crystallinity—turned out to be critical to everything that followed.

The team then blended CNCs into pea starch at concentrations ranging from 2 to 8 percent by weight and subjected the mixtures to a battery of analytical tests spanning seven orders of magnitude in scale, from molecular vibrations to whole-gel texture. Rapid viscosity analysis showed that even small doses of CNCs changed how the starch behaved during cooking. At 4 percent CNCs, the peak viscosity of the paste dropped from 505 to 487 pascal-seconds, a sign that the nanorods were crowding the swelling granules and competing for water. More tellingly, the setback viscosity—a measure of how much the paste thickens as it cools and the chains begin to reassociate—fell steadily from 187 pascal-seconds in the pure starch to 159 pascal-seconds at 8 percent CNCs, indicating that the nanorods were already interfering with the earliest stages of chain reordering.

The most visually striking evidence came from simple refrigeration experiments. When gels were stored at 4 degrees Celsius for five and seven days, the untreated pea starch gel expelled progressively more water, a phenomenon called syneresis that anyone who has opened a container of old pudding will recognize. By day seven, the control gel had lost 30.63 percent of its weight as expelled water. The gel fortified with 8 percent CNCs lost only 27.49 percent, a reduction of more than three percentage points, and the effect grew stronger with increasing CNC loading. Low-field nuclear magnetic resonance revealed what was happening at the molecular level: the fraction of free, mobile water in the gels fell dose-dependently from 33.09 percent in the control to 27.79 percent at 8 percent CNCs after a week of storage, while the relaxation time of weakly bound water shortened, showing that the nanorods were literally pinning water molecules in place within the gel network.

Scanning electron microscopy provided the structural explanation. In the freeze-dried retrograded gels, the CNCs appeared as rigid rods uniformly distributed throughout the starch matrix, bridging adjacent fragments and pore walls like tiny struts in a scaffold. Gels containing the nanorods showed thickened fragment walls, smoother surfaces, and more homogeneous pore distributions than the untreated control, forming what the authors describe as a concrete-like supportive framework. The hydroxyl-rich surfaces of the rods competitively bind water while simultaneously forming hydrogen bonds with amylose and amylopectin chains, reinforcing the three-dimensional network and denying the starch chains the mobility they need to crystallize.

Spectroscopic and thermal measurements confirmed that the interaction is non-covalent but powerful. Fourier transform infrared spectroscopy showed no new absorption peaks and no peak shifts, only a pronounced broadening of the hydroxyl stretching band near 3300 wavenumbers—a fingerprint of extensive hydrogen bonding between the nanorods and the starch chains. Differential scanning calorimetry quantified the energetic consequence: after seven days of refrigeration, the retrogradation enthalpy of pure pea starch was 1.46 joules per gram, but only 0.60 joules per gram at 8 percent CNCs, cutting the degree of retrogradation nearly in half, from 14.07 percent to 7.23 percent. X-ray diffraction delivered perhaps the most dramatic number of all: the relative crystallinity of the stored gels fell from 34 percent to 16 percent across the CNC range, a 52.94 percent reduction, while the characteristic B-type crystal polymorph of the starch remained unchanged, confirming that the nanorods suppressed crystal growth without altering its fundamental nature.

Texture analysis tied the physics back to the eating experience. After a week of cold storage, the untreated pea starch gel had hardened to 93.76 grams of resistance, while every CNC-fortified gel was measurably softer, with springiness preserved near 1.0 throughout. Interestingly, the relationship between CNC concentration and gel properties was not strictly linear. The inhibitory effect rose with loading and then plateaued between 6 and 8 percent, and above that threshold the nanorods began to agglomerate, losing their ability to disperse and undermining the very interfacial contact on which the mechanism depends. This non-linear, dispersion-governed behavior distinguishes rigid rod-like CNCs from both flexible hydrocolloids and spherical nanoparticles, and it establishes a practical formulation window for food developers.

The implications reach beyond the laboratory. Because CNCs are derived from abundant agricultural byproducts and work through physical rather than chemical modification, they sidestep the toxicity concerns of chemical starch additives and the limited controllability of enzymatic treatments. A dosing guideline of 6 to 8 percent CNCs could extend the refrigerated shelf life of pea-based noodles, jellies, and meat analogues without any synthetic preservatives. The authors caution that their study covered only one week of storage at 4 degrees Celsius, leaving room-temperature stability, freeze-thaw cycling, digestibility, and real-food matrices for future work. But the core message stands: the answer to keeping plant-based foods fresh may lie in scattering billions of impossibly small cellulose rods through the gel, where they lock up water, brace the network, and quietly stop starch from turning back against itself.

Subject of Research: Using cellulose nanocrystals to inhibit the retrogradation of high-amylose pea starch in food gels

Article Title: Effects of cellulose nanocrystals on the physicochemical and retrogradation properties of pea starch

Article References: Cui, S., Cui, S., Xie, W., Li, H., Li, F., Ge, S., Fu, Z., & Du, H. (2026). Effects of cellulose nanocrystals on the physicochemical and retrogradation properties of pea starch. Food Chemistry: X, Article 104569. https://doi.org/10.1016/j.fochx.2026.104569

Image Credits: AI Generated

DOI: 10.1016/j.fochx.2026.104569

Keywords: pea starch, cellulose nanocrystals, starch retrogradation, food chemistry, amylose, syneresis, nanomaterials, gelatinization, X-ray diffraction, LF-NMR, plant-based foods, shelf life