Structural Properties Of Proteins Research Articles

Impact of non‐thermal plasma generated using air and nitrogen on functional properties of milk protein dispersions

AbstractThis study focuses on improving the functionalities of milk protein concentrate (MPC) using a nonthermal plasma jet and plasma‐activated water (PAW) with atmospheric air and nitrogen as source gases. The 5% and 10% MPC dispersions were directly treated with a plasma jet, and PAW was used to make the MPC dispersions. The dispersions were analyzed for changes in protein structure and functional properties. The treatment altered the secondary structure of MPC protein structure by increasing β‐components and changing the order of random coils. The solubility of the PAW‐treated 5% protein dispersions doubled due to plasma‐induced modification of hydrophilic and covalent bonds of the protein, but this increase was not significant for the 10% dispersions due to less hydration. Emulsifying capacity increases by around 7% for plasma jet and PAW with air, owing to hydrophobicity on the particle surface. The gelation capacity and heat coagulation time rise by almost twice; however, foaming capacity decreases, indicating protein structural modifications and aggregations caused by plasma exposure. The viscosity of the 5% dispersions decreased due to high solubility, while that of the 10% dispersions increased due to less hydration. Principle component analysis was used to correlate the change in functionality with different operating parameters. In conclusion, this study illustrates that the functional properties of MPC can be significantly modified through plasma treatment. The observed changes depend on several factors, including the mode of plasma exposure, the source gas used to generate the plasma, and the concentration of the protein solution.Practical applicationsMilk protein concentrate (MPC) is a promising ingredient in food products such as cheese, cultured dairy items, nutritional goods, infant milk formulas, ice cream, dairy‐based drinks, sports beverages, and a variety of health‐focused products. However, the application is profoundly hindered due to its poor solubility and solubility‐related functional properties. MPC powders lose functionalities during manufacturing and gradually lose them again during processing and storage. This study explores the potential of non‐thermal plasma to improve the functional properties of proteins. This study explores the potential of two different discharges: plasma jet and plasma‐activated water (PAW), using atmospheric air and nitrogen as source gases. The findings of this study would also help to understand the types of plasma discharge (jet vs PAW) and types of sources of gases that can be used in industrial applications. Some optimization parameters of this study can be used for scaling up the plasma processing of milk or dairy products. In addition, PAW is being very well studied to improve food safety, and this study would provide information on the physicochemical properties of MPC. Therefore, it would also help to understand how to apply non‐thermal plasma to achieve both microbial and physical effects.

MechanoProDB: a web-based database for exploring the mechanical properties of proteins.

The mechanical stability of proteins is crucial for biological processes. To understand the mechanical functions of proteins, it is important to know the protein structure and mechanical properties. Protein mechanics is usually investigated through force spectroscopy experiments and simulations that probe the forces required to unfold the protein of interest. While there is a wealth of data in the literature on force spectroscopy experiments and steered molecular dynamics simulations of forced protein unfolding, this information is spread and difficult to access by non-experts. Here, we introduce MechanoProDB, a novel web-based database resource for collecting and mining data obtained from experimental and computational works. MechanoProDB provides a curated repository for a wide range of proteins, including muscle proteins, adhesion molecules and membrane proteins. The database incorporates relevant parameters that provide insights into the mechanical stability of proteins and their conformational stability such as the unfolding forces, energy landscape parameters and contour lengths of unfolding steps. Additionally, it provides intuitive annotations of the unfolding pathways of each protein, allowing users to explore the individual steps during mechanical unfolding. The user-friendly interface of MechanoProDB allows researchers to efficiently navigate, search and download data pertaining to specific protein folds or experimental conditions. Users can visualize protein structures using interactive tools integrated within the database, such as Mol*, and plot available data through integrated plotting tools. To ensure data quality and reliability, we have carefully manually verified and curated the data currently available on MechanoProDB. Furthermore, the database also features an interface that enables users to contribute new data and annotations, promoting community-driven comprehensiveness. The freely available MechanoProDB aims to streamline and accelerate research in the field of mechanobiology and biophysics by offering a unique platform for data sharing and analysis. MechanoProDB is freely available at https://mechanoprodb.ibdm.univ-amu.fr.

Research progress and latest application of ultrasonic treatment on protein extraction and modification

SummaryThe advancement of the modern food industry has prompted a shift away from traditional protein extraction methods due to their inherent limitations. As a result, there is a growing interest in exploring alternative methods for protein extraction and modification such as ultrasonic (US) treatment. This shift towards more sustainable and efficient protein extraction methods is a key research focus in obtaining safe proteins in an environmentally friendly manner. Furthermore, enhancing the functional properties of proteins through modification can expand their application. This paper reviews recent research progress and applications of US treatment on protein extraction and modification as well as the impact on protein structure and functional properties. In addition, the latest applications of ultrasound‐modified‐proteins, including nano‐proteins, 3D printing and interactions between proteins and other food components, are reviewed. This review may provide some inspiration for the potential application of US technologies in food fields.

Insights into the starch and proteins molecular structure changes of foxtail millet sourdough: Effect of fermentation from grains of cereal to pre-meal

This study investigated the effects of foxtail millet sourdough fermentation time (0, 8, 16, and 24 h) on the protein structural properties, thermomechanical, fermentation, dynamic rheological, starch granules crystalline regions molecular mobility, and starch microstructural characteristics. The fermentation led to a significant increase in the concentration of free amino acids from protein hydrolysis. Fourier transform infrared spectroscopy (FTIR) revealed changes in protein secondary structure and the presence of functional groups of different bioactive compounds. The result of thermomechanical properties showed a significant increase in the stability (0.70–0.79 min) and anti-retrogradation ability (2.29–3.14 Nm) of lactic acid bacteria (LAB) sourdough compared to the control dough, showing a wider processing applicability with radar profiler index. In contrast, sourdoughs with lower tan δ values had higher elasticity and strength. Scanning electron microscopy showed that the surface of the starch appeared from smooth to uneven with patchy shapes and cavities, which declined the crystallinity from 34.00 % to 21.57 %, 23.64 %, 25.09 %, and 26.34 % respectively. Fermentation changed the To, Tp, Tc, and ΔH of the starch. The results of the study will have great potential for application in the whole grain sourdough industry.

CASTpFold: Computed Atlas of Surface Topography of the universe of protein Folds.

Geometric and topological properties of protein structures, including surface pockets, interior cavitiesand cross channels, are of fundamental importance for proteins to carry out their functions. Computed Atlas of Surface Topography of proteins(CASTp) is a widely used web server for locating, delineating, and measuring these geometric and topological properties of protein structures. Recent developments in AI-based protein structure prediction such as AlphaFold2 (AF2) have significantly expanded our knowledge on protein structures. Here we present CASTpFold, a continuation of CASTp that provides accurate and comprehensive identifications and quantifications of protein topography. It now provides (i) results on an expanded database of proteins, including the Protein Data Bank(PDB) and non-singleton representative structures of AlphaFold2 structures, covering 183 million AF2 structures; (ii) functional pockets prediction with corresponding Gene Ontology (GO) terms or Enzyme Commission (EC) numbers for AF2-predicted structuresand (iii) pocket similarity search function for surface and protein-protein interface pockets. The CASTpFold web server is freely accessible at https://cfold.bme.uic.edu/castpfold/.

Comparative analysis of folding and unfolding dynamics and free-energy landscapes in homologous cold shock proteins with variable thermal stabilities

Cold shock proteins from the mesophilic organism (BsCSP), the thermophilic organism (BcCSP), and the hyperthermophilic organism (TmCSP) are homologous proteins with similar native structure but quite different thermal stabilities, which makes them promising candidates for investigating the general and specific aspects the folding and unfolding dynamics of proteins and free-energy landscapes. In this study, we employed magnetic tweezers to explore the force-dependent folding and unfolding rates of BsCSP, BcCSP, and TmCSP at forces from several pN to tens of pN. Our results indicate similar force-dependent folding rates for these three proteins, while the unfolding rate of BsCSP, BcCSP, and TmCSP decreases sequentially, consistent with previous biochemical findings. Comparing with TmCSP, BcCSP shows lower but sufficient stability with folding free energy of 8.0 kBT, and its force-dependent unfolding rates exhibit tremendous nonlinear behavior deviated from Bell's model like TmCSP. BsCSP has very low stability with folding free energy of only 3.9 kBT, and its force-dependent unfolding rates at 3–10 pN exhibit almost linear behavior. Comprehensive free-energy landscapes are constructed, revealing common barriers that governs folding and unfolding dynamics for BcCSP and TmCSP but a wide merged barrier for BsCSP. Our findings provide valuable insights into the folding and unfolding mechanisms of these CSPs, shedding light on the relationship between protein structure, stability, and mechanical properties. Published by the American Physical Society 2024

Preparation of a curcumin oil bodies delivery system based on pH-Shift treatment: Physicochemical properties, protein structure, and digestive properties

Curcumin (Cur) was encapsulated in oil bodies (OBs) using pH-shift treatment. The physicochemical properties, surface protein structure, stability, and in vitro digestion of the prepared composite emulsion (COB) were characterized. The results showed a fading of Cur crystallization peak in COB. Besides, the highest encapsulation rate, largest particle size and zeta potential were observed at pH 0.5. Compared to OBs, the hydrophilic groups of COB surface proteins were unfolded and the central hydrophobic region remained relatively stable, with reduced COB storage stability and good oxidative stability. In vitro simulated digestion revealed that Cur was released in a sustained manner. The highest bioaccessibility (57.5%) and stability (67.3%) of COB were observed at pH 0.5. The present study suggested that pH-shift treatment is a viable method for the preparation of COB carriers. This information may provide new ideas for the preparation of lipophilic polyphenol delivery systems such as Cur, which can contribute to the application of OBs in a variety of food processing applications, including plant-based milk, fortified foods, etc.

Insight into the effects of pulsed electric field on the structure, aggregation characteristics and functional properties of whey proteins

The effects of pulsed electric field (PEF) under different electric field intensities (EFIs, 5–20 kV/cm) and treatment times (2–8 ms) on the structural properties, aggregation/dissociation, and rheological characteristics of whey proteins (WPs) were investigated. An increase of visual turbidity and particle size measurements in 5 and 10 kV/cm PEF treatment groups indicated the formation of larger, insoluble aggregates dominated by disulfide bonds cross-linking and enhanced surface hydrophobicity. However, with the augmentation of EFI reaching a pivotal level (15 and 20 kV/cm), the decrease of hydrophobic interaction coupled with the increased electrostatic repulsion due to increased helix structure can dissociate the aggregates in response to blue-shifted particle size and thin irregular cavern-like structure, causing the solubility increased by 5.24% (20 kV/cm treatment for 8 ms). Furthermore, WPs oxidation played an important role in aggregates disintegration and liberation of peptides due to protein polarization and attack of reactive radicals produced by electrochemical reaction. Rheological analysis showed that higher solubility and diminished particle size after 15 and 20 kV/cm treatments improved the emulsifying capacity and decreased viscosity and interfacial tension of WPs dispersion. Conclusively, structural modification and preeminent functional properties were prompted by the extension of EFI and treatment time. Therefore, an effective theoretical basis may be proposed for PEF used as a promising technology to modify the functional characteristics of WPs.

Effects of glycation reactions on the structure and immunological properties of sesame proteins

SummarySesame has been included in the top eight food allergens, and therefore reduction of sesame allergen potency is of great practical significance. Glycation reactions are extensively researched for their role in regulating the allergic properties of food allergens due to their distinct benefits. This study involved the glycation of sesame proteins with three different reducing sugars to generate reaction products. The structure of the reaction products was characterized by the use of spectroscopic and chromatographic techniques. The impact of glycation on the allergenic properties of sesame proteins was explored by in vitro simulated digestion tests combined with immunological techniques. The study results indicated that all three reducing sugars underwent glycation with sesame proteins, with D‐ribose showing the most significant level of glycation. During the glycation reaction of sesame proteins in this study, the proteins underwent precipitation as well as structural changes, leading to reduced immunoglobulin G (IgG) binding capacity. Glycation alters the digestive stability of sesame proteins and further reduces the ability to bind to IgG. Overall, glycation modification shows promise in decreasing the allergenicity of sesame.

Unraveling the impacts of fermentation methods on the protein structural, foaming and air-water interfacial properties of buckwheat steamed bread dough liquor

Liquid lamella has crucial impacts on stabilizing gas cells and buckwheat steamed bread (BSB) quality due to the high fiber content and lack of gluten protein in buckwheat. The liquid lamella was collected by ultracentrifugation as the dough liquor (DL). This study explored the composition, foaming and interfacial properties of DL from lactic acid bacteria (LAB), yeast, LAB and yeast cooperate (LAB-yeast), and chemical acidified and yeast (CA-yeast) fermented buckwheat dough, as well as the unfermented buckwheat dough. Compared with the unfermented dough, the DL yield of LAB-yeast, yeast, and CA-yeast fermented dough decreased by 4.09%, 3.93%, and 7.67%, respectively. The protein molecular weight and surface hydrophobicity of DL were dramatically reduced by LAB, LAB-yeast, and CA-yeast fermentation as compared to unfermented DL. Among all DL samples, the unfermented and yeast DL showed the highest protein surface hydrophobicity and surface activity, resulting in the greatest foam stability. The protein in CA-yeast DL displayed the fastest interface diffusion because its DL had the highest amount of low molecular weight protein, the lowest viscosity and protein content. Compared with the unfermented dough, the LAB and LAB-yeast fermentation decreased, while the CA-yeast fermentation increased the strain hardening index (SHI) of the dough. This enhanced strain hardening behavior contributed to a decrease in the average cell area and an increase in cell density, making the crumb structure of CA-yeast fermented BSB homogeneous and dense.

Influence of the processing on composition, protein structure and techno-functional properties of mealworm protein concentrates produced by isoelectric precipitation and ultrafiltration/diafiltration

Edible insects represent a great alternative protein source but food neophobia remains the main barrier to consumption. However, the incorporation of insects as protein-rich ingredients, such as protein concentrates, could increase acceptance. In this study, two methods, isoelectric precipitation and ultrafiltration-diafiltration, were applied to produce mealworm protein concentrates, which were compared in terms of composition, protein structure and techno-functional properties. The results showed that the protein content of the isoelectric precipitation concentrate was higher than ultrafiltration-diafiltration (80 versus 72%) but ash (1.91 versus 3.82%) and soluble sugar (1.43 versus 8.22%) contents were lower. Moreover, the protein structure was affected by the processing method, where the ultrafiltration-diafiltration concentrate exhibited a higher surface hydrophobicity (493.5 versus 106.78 a.u) and a lower denaturation temperature (161.32 versus 181.44 °C). Finally, the ultrafiltration-diafiltration concentrate exhibited higher solubility (87 versus 41%) and emulsifying properties at pH 7 compared to the concentrate obtained by isoelectric precipitation.

Supercritical CO2 Treatment to Modify Techno-Functional Properties of Proteins Extracted from Tomato Seeds.

Tomato seeds are a rich source of protein that can be utilized for various industrial food purposes. This study delves into the effects of using supercritical CO2 (scCO2) on the structure and techno-functional properties of proteins extracted from defatted tomato seeds. The defatted meal was obtained using hexane (TSMH) and scCO2 (TSMC), and proteins were extracted using water (PEWH and PEWC) and saline solution (PESH and PESC). The results showed that scCO2 treatment significantly improved the techno-functional properties of protein extracts, such as oil-holding capacity and foaming capacity (especially for PEWC). Moreover, emulsifying capacity and stability were enhanced for PEWC and PESC, ranging between 4.8 and 46.7% and 11.3 and 96.3%, respectively. This was made possible by the changes in helix structure content induced by scCO2 treatment, which increased for PEWC (5.2%) and decreased for PESC (8.0%). Additionally, 2D electrophoresis revealed that scCO2 hydrolyzed alkaline proteins in the extracts. These findings demonstrate the potential of scCO2 treatment in producing modified proteins for food applications.

Unlocking the potential of waxworm (Galleria mellonella) proteins: Extraction, fractionation, and protein quality assessment

Edible insects are increasingly recognized as an alternative and sustainable protein source to meet future protein demands. Owing to its significant protein content (33.43%), the edible insect Waxworm (Galleria mellonella) was characterized in this study for its protein extractability, structural properties, and protein quality. Protein extractability under various pH levels and ionic strengths was evaluated. Subsequently, Osborne fractionation was employed to characterize protein fractions based on their preferential solubilities. The extracted proteins and their respective fractions were visualized by SDS-PAGE, and the most intense bands were excised for proteomics data analysis. Secondary structure, pI, molecular mass, and denaturation temperature were also examined. The quality of waxworm protein was assessed by determining the IVPD, PDCAAS, and amino acid profile. Waxworm proteins exhibited greater stability in alkaline conditions compared to acidic environments. These might also be more sensitive to ionic strength than other alternative proteins, such as those derived from plants. The allergen tropomyosin was identified by SDS-PAGE with an approximate molecular weight of ∼32.5 kDa; however, it can be selectively removed by salt extraction. The secondary structures of waxworm proteins, extracted under various conditions, appeared stable, with α-helix and β-conformation being the predominant conformation. Among the protein fractions, prolamins displayed an α-helix conformation, while albumins, globulins, and glutelins predominantly adopted a β-sheet structure. It was observed that structural features could influence the overall quality of the protein. As for the protein quality, globulins are the protein fraction recommended as these showed the highest EAAI% (924.02), PDCAAS (0.84) and IVPD (76.33%) values.

Pro-Hemorrhagic Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy Associated with NOTCH3 p.R75P Mutation with Low Vascular NOTCH3 Aggregation Property.

Intracerebral hemorrhage (ICH) and cerebral microbleeds (CMB) in cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy are more common in East Asian populations than in people of white European ancestry. We hypothesized that the ethnic difference is explained by the East Asian-specific NOTCH3 p.R75P mutation. This retrospective observational study included 118 patients with cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy in Japanese and Korean cohorts. We investigated whether the p.R75P mutation is associated with symptomatic ICH and multiple CMB (>5) using quasi-Poisson regression models. We predicted the NOTCH3 extracellular domain protein structures in silico and graded NOTCH3 extracellular domain immunostaining in skin vessels of some patients, with subsequent comparisons between p.R75P and other conventional mutations. Among 63 Japanese patients (median age 55 years; 56% men), 15 had a p.R75P mutation, significantly associated with symptomatic ICH (adjusted relative risk 9.56, 95% CI 2.45-37.31), multiple CMB (3.00, 1.34-6.71), and absence of temporopolar lesions (4.91, 2.29-10.52) after adjustment for age, sex, hypertension, and antithrombotics. In the Korean cohort (n = 55; median age 55 years; 51% men), the p.R75P mutation (n = 13) was also associated with symptomatic ICH (8.11, 1.83-35.89), multiple CMB (1.90, 1.01-3.56), and absence of temporopolar lesions (2.32, 1.08-4.97). Structural analysis revealed solvent-exposed free cysteine thiols in conventional mutations, directly causing aggregation, whereas a stereochemically incompatible proline residue structure in p.R75P lowers correct disulfide bond formation probability, indirectly causing aggregation. Pathologically, the p.R75P mutation resulted in less vascular NOTCH3 extracellular domain accumulation than the other conventional mutations. NOTCH3 p.R75P mutation is associated with hemorrhagic presentations, milder temporopolar lesions, and distinct mutant protein structure properties. ANN NEUROL 2024;95:1040-1054.

Effects of fibrillation combined with glycation by different chain length sugars on structural and functional properties of soybean protein

The key objective of this study was to investigate the effects of fibrillation combined with glycation of soybean protein isolate (SPI) on the protein structure and functional properties. SPI fibrils alone, glycated proteins and glycated fibrils with different chain lengths (glucose–G, maltose–M and dextran–D) were prepared and characterized by spectroscopy and microscopy methods. The results of the O-phthalaldehyde assay, ultraviolet–visible spectroscopy and fluorescent advanced glycation endproducts indicated the degree of glycation. The thioflavin T fluorescence assay, transmission electron microscopy (TEM) and Fourier-transform infrared (FTIR) spectroscopy results demonstrated that the fibril morphology improved, and more flexible and aggregated fibrils were produced after glycation, further improving the protein functional properties. With EAI and ESI values of 37.31 m2/g and 33.80%, respectively, the emulsifying properties of SPI fibrils glycated by dextran were higher than the others. Foam properties and antioxidant activity were highest for the fibrils glycated by glucose. These results are of scientific significance for in-depth understanding and reasonable regulation of protein functional properties for industrial production in a complex food system.

Effects of high-pressure homogenization and ultrasound on the composition, structure, and physicochemical properties of proteins extracted from Nannochloropsis Oceania

This study examined the effects of high-pressure homogenization (HPH) and ultrasonication pre-treatment on the structural and physicochemical properties of proteins extracted from defatted Nannochloropsis Oceania biomass (DNOB). HPH treatment was found to enhance the solubility of protein extracted from DNOB compared to ultrasound, where samples pretreated with three passes (3P) of HPH exhibited lower solubility than two passes (2P). The morphology of extracted samples was visualized by scanning electron microscopy, which HPH pre-treatment, especially with more passes, were able to breakdown DNOB into fragments. Alternatively, more holes were displayed on the surface of the extracts pretreated with ultrasound especially when higher amplitude applied. The particle size of extracts from HPH3P (129.5 µm) significant dropped from HPH2P (314.25 µm), where samples pretreated with ultrasound at 20 % amplitude (US20) also decreased in particle size compared to 40 % amplitude (US40), from 115.25 µm to 78.22 µm. Protein flexibility of DNOB extracts were enhanced by both HPH2P and HPH3P but decreased for ultrasound samples. β-sheets were found to be the most abundant protein secondary structure for all samples, where samples treated with HPH3P contained the highest percentage of β-sheets (72 %) than control, HPH2P, ultrasonication at 20 and 40 % amplitude (52–62 %). The high percentage of β-sheets found in HPH3P sample also contributed to its outstanding emulsifying properties which stood out among all, especially at concentrations over 1 mg/ml. Results obtained from this study helped to direct the application of DNOB extracts as functional food ingredient for future food innovation.

High Hydrostatic Pressure: Influences on Allergenicity, Bioactivities, and Structural and Functional Properties of Proteins from Diverse Food Sources.

High hydrostatic pressure (HHP) has gained prominence in the food processing industry over the last decade. In addition to the effectiveness of microbial and enzymatic inactivation, HHP directly impacts protein structures and properties. Accordingly, this review article aims to consolidate relevant research findings elucidating the effects of HHP on protein structure, allergenicity, bioactivities, and functional properties across diverse protein sources. They encompass cereals, legumes, nuts, meat, poultry products, milk, eggs, seafood, algae, insects, seeds, and vegetables. This review provides insights into the consistent trends of HHP effects on each protein source. In conclusion, HHP induces alterations in non-covalent bonds within protein structures, leading to the unfolding of their interior regions and consequential changes in their properties. Remarkably, the allergenicity of cereals, legumes, and nuts decreases while their bioactivities and digestibility escalate. The disruption of non-covalent bonds during HHP results in the exposure of the interior hydrophobic regions to the surface microenvironment, thereby enhancing the surface hydrophobicity of proteins, particularly those derived from seeds and vegetables. HHP weakens the allergenicity and elevates the foaming properties of proteins from dairy products, including improving the gelling properties and antioxidant activities of egg proteins. Texture profiles of meat and poultry, particularly hardness, are enhanced. Furthermore, HHP demonstrates the potential to diminish the allergenicity of seafood proteins and augment insect protein bioactivities. Lastly, HHP enhances the extraction of algal bioactive components, improving their nutritional quality.

FvMYB108, a MYB Gene from Fragaria vesca, Positively Regulates Cold and Salt Tolerance of Arabidopsis.

MYB (myoblast) protein comes in large quantities and a wide variety of types and plays a role in most eukaryotes in the form of transcription factors (TFs). One of its important functions is to regulate plant responses to various stresses. However, the role of MYB TFs in regulating stress tolerance in strawberries is not yet well understood. Therefore, in order to investigate the response of MYB family members to abiotic stress in strawberries, a new MYB TF gene was cloned from Fragaria vesca (a diploid strawberry) and named FvMYB108 based on its structural characteristics and evolutionary relationships. After a bioinformatics analysis, it was determined that the gene belongs to the R2R3-MYB subfamily, and its conserved domain, phylogenetic relationships, predicted protein structure and physicochemical properties, subcellular localization, etc. were analyzed. After qPCR analysis of the expression level of FvMYB108 in organs, such as the roots, stems, and leaves of strawberries, it was found that this gene is more easily expressed in young leaves and roots. After multiple stress treatments, it was found that the target gene in young leaves and roots is more sensitive to low temperatures and salt stimulation. After these two stress treatments, various physiological and biochemical indicators related to stress in transgenic Arabidopsis showed corresponding changes, indicating that FvMYB108 may be involved in regulating the plant's ability to cope with cold and high-salt stress. Further research has found that the overexpression of this gene can upregulate the expression of AtCBF1, AtCOR47, AtERD10, and AtDREB1A related to low-temperature stress, as well as AtCCA1, AtRD29a, AtP5CS1, and AtSnRK2.4 related to salt stress, enhancing the ability of overexpressed plants to cope with stress.

Steam cooking drives alterations of proteomics, protein structural and functional properties in rice (Oryza sativa l.)

Rice, as an important staple food consumed by people, is gradually becoming a concern for many consumers in terms of its eating quality. Many studies have found that protein is an important factor to determine the edible quality of rice. However, the protein changes during rice cooking have not been compared and studied in detail. In this study, the structural and functional characteristics of rice proteins before and after steaming were comprehensively compared. Meanwhile, proteomic strategies were also applied to analyze changes in protein composition and expression. Steaming promoted the aggregation of cooked rice proteins, resulting in a more compact structure and a significant increase in particle size (raw rice, 304.33 nm; cooked rice, 565.17 nm). Compared with raw rice protein (43.33%; 133.91%), the solubility (22.29%) and foaming capacity (119.53%) of cooked rice protein were significantly reduced, while emulsion activity was slightly improved. The differential abundance proteins were found to be predominantly down-regulated after steaming (238 proteins) and mostly enriched in metabolic pathways. The steaming process of rice mainly involves oxidative phosphorylation, thiamine metabolism, ether lipid metabolism, glycerophospholipid metabolism, multiple amino acid metabolism and other metabolic pathways, and they are closely related to each other. This study deepens the understanding of proteomic changes and structural/functional properties of rice proteins during steaming.

Modular Protein Fibers with Outstanding High-Strength and Acid-Resistance Performance Mediated by Copper Ion Binding and Imine Networking.

Engineered protein fibers are promising biomaterials with diverse applications due to their tunable protein structure and outstanding mechanical properties. However, it remains challenging at the molecular level to achieve satisfied mechanical properties and environmental tolerance simultaneously, especially under extreme acid conditions. Herein, the construction of artificial fibers comprising chimeric proteins made of rigid amyloid peptide and flexible cationic elastin-like protein (ELP) module is reported. The amyloid peptide readily assembles into highly organized β-sheet structures that can be further strengthened by the coordination of Cu2+, while the flexible ELP module allows the formation of imine-based crosslinking networks. These double networks synergistically enhance the mechanical properties of the fibers, leading to a high tensile strength and toughness, overwhelming many reported recombinant spidroin fibers. Notably, the coordination of Cu2+ with serine residues could stabilize β-sheet structures in the fibers under acidic conditions, which makes the fibers robust against acid, thus enabling their successful utilization in gastric perforation suturing. This work highlights the customization of double networks at the molecular level to create tailored high-performance protein fibers for various application scenarios.