Development and Characterization of Pickering Emulsion Stabilized by Walnut Protein Isolate Nanoparticles.

This study was conducted to prepare walnut protein isolate nanoparticles (nano-WalPI) by pH-cycling, combined with the ultrasound method, to investigate the impact of various nano-WalPI concentrations (0.5~2.5%) and oil volume fractions (20~70%) on the stability of Pickering emulsion, and to improve the comprehensive utilization of walnut residue. The nano-WalPI was uniform in size (average size of 108 nm) with good emulsification properties (emulsifying activity index and stability index of 32.79 m2/g and 1423.94 min, respectively), and it could form a stable O/W-type Pickering emulsion. When the nano-WalPI concentration was 2.0% and the oil volume fraction was 60%, the best stability of Pickering emulsions was achieved with an average size of 3.33 µm, and an elastic weak gel network structure with good thermal stability and storage stability was formed. In addition, the emulsion creaming index value of the Pickering emulsion was 4.67% after 15 days of storage. This study provides unique ideas and a practical framework for the development and application of stabilizers for food-grade Pickering emulsions.

Effect of Protein-Glutaminase on Calcium Sulphate-Induced Gels of SPI with Different Thermal Treatments.

The effects of protein-glutaminase (PG) on calcium sulphate (CaSO4)-induced gels of soy protein isolate (SPI) with different heat treatment levels were investigated. The time-dependent degree of deamidation showed that the mild denaturation of the protein favored the deamidation. The particle size distribution showed that the heat treatment increased the SPI particle size, and the particle size distribution of the SPI shifted to the right or increased the proportion of the large particle size component as the degree of deamidation increased for each sample. Rheological analysis showed that the deamidation substantially pushed up the gel temperature and decreased the value of G'. The gel strength and water-holding capacity showed that the higher the amount of enzyme added, the more significant the decrease in gel strength, while the gel water-holding capacity increased. In summary, the deamidation of PG and heat treatment can affect the gel properties of SPI synergistically.

Solubilization mechanism of self-assembled walnut protein nanoparticles and curcumin encapsulation.

BACKGROUND: Native walnut protein is an alkali-soluble protein that seriously limits the application of walnut protein. The pH-shifting method could improve the solubility of walnut proteins and enable the encapsulation of active ingredients. The present study aimed to prepare water-soluble nanoparticles of curcumin using walnut protein and evaluate the process of walnut protein self-assembly, interaction between walnut protein and curcumin, encapsulation properties, and stability of nanoparticles. RESULTS: The solubility of native walnut protein was poor, but the solubility of walnut protein nanoparticles (WPNP) formed by walnut protein after pH-shifting significantly improved to 91.5 ± 1.2%. This is because, during the process of pH changing from 7 to 12 and back to 7, walnut protein first unfolded under alkaline conditions and then refolded under pH drive, finally forming an internal hydrophobic and external hydrophilic shell-core structures. The quenching type of walnut protein and curcumin was static quenching, and the quenching constant was 2.0 × 1014 mol-1 L-1 s-1 , indicating that the interaction between walnut protein and curcumin was non-covalent. Adding curcumin resulted in the formation of nanoparticles with small particle size compared with the no-load. The loading capacity of curcumin-loaded walnut protein nanoparticles (WPNP-C) was 222 mg g-1 walnut protein isolate. Under the same mass, the curcumin equivalent concentration in aqueous solution of WPNP-C was 17 000 times higher than that of the native curcumin. CONCLUSION: The solubility of the self-assembled WPNP significantly increased after pH-shifting treatment. The walnut protein carrier could improve the stability of the encapsulated curcumin. Therefore, walnut proteins could be used as water-soluble carriers for hydrophobic drugs. © 2023 Society of Chemical Industry.

Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment.

This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (p < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (p < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.

Functional Properties of Rice Bran Proteins Extracted from Low-Heat-Treated Defatted Rice Bran.

Rice bran is rich in proteins with high nutritional values. However, current protein extraction methods from rice bran are greatly limited by their low yield. Therefore, in this study, we aimed to develop a feasible method to extract rice bran protein (RBP) of high purity and quality. We prepared RBP using low-heat-treated defatted rice bran (LDRB) and analyzed its functional properties. The protein solubility of LDRB increased from 25.4% to 56% upon increasing the pH level and was more than double that of heat-stabilized defatted rice bran. RBP prepared from LDRB had good functional properties, comparable to those of soy proteins. The emulsifying capacities of RBP were 424 ± 14 mL/g at pH 4 and 530 ± 21 mL/g at pH 7.0. Under acidic conditions, RBP showed a better emulsifying capacity than soy proteins (262 ± 1 mL/g at pH 4). RPB showed water-binding and oil-absorption capacities of 270 ± 35 g/100 g and 268 ± 30 g/100 g, respectively. Moreover, RBP showed better foaming capacity (610% vs. 590%) and foam stability (83% vs. 4%) than soy proteins; however, it lacked gelling properties. This study demonstrated that RBP is a potential new protein source in the food industry.

Chickpea protein ingredients: A review of composition, functionality, and applications.

Chickpea (Cicer arietinum L.) is a pulse consumed all over the world, representing a good source of protein, as well as fat, fiber, and other carbohydrates. As a result of the growing global population the demand for the protein component of this pulse is increasing and various approaches have been proposed and developed to extract same. In this review the composition, functionality, and applications of chickpea protein ingredients are described. Moreover, methods to enhance protein quality have been identified, as well as applications of the coproducts resulting from protein extraction and processing. The principal dry and wet protein enrichment approaches, resulting in protein concentrates and isolates, include air classification, alkaline/acid extraction, salt extraction, isoelectric precipitation, and membrane filtration. Chickpea proteins exhibit good functional properties such as solubility, water and oil absorption capacity, emulsifying, foaming, and gelling. During protein enrichment, the functionality of protein can be enhanced in addition to primary processing (e.g., germination and dehulling, fermentation, enzymatic treatments). Different applications of chickpea protein ingredients, and their coproducts, have been identified in research, highlighting the potential of these ingredients for novel product development and improvement of the nutritional profile of existing food products. Formulations to meet consumer needs in terms of healthy and sustainable foods have been investigated in the literature and can be further explored. Future research may be useful to improve applications of the specific coproducts that result from the extraction of chickpea proteins, thereby leading to more sustainable processes.

Soy protein isolates: A review of their composition, aggregation, and gelation.

Considering that a series of complex issues such as environmental problems, sustainable development, animal welfare, and human health are on a global scale, the development of vegetable protein-based meat substitutes provides a potential solution to the disparity between meat consumption demand and supply. The research and development of vegetable protein-based meat substitutes have become a major commercial activity, and the market is expanding to meet the growing consumer demand. Soy protein isolates (SPI) are often used as a raw material for vegetable meat substitutes because of their potential to form fiber structures. Although significant initial success has been achieved, it is still a challenge to explain how the composition and aggregation of SPI influence gel properties and the mechanism(s) involved. This article reviews the latest research about SPI. The relationship between the composition, aggregation, and gelation properties of SPI is based on a through literature search. It focused on the application of SPI in heat- and cold-induced gels, given the diversified market demands. The research on cold gel has helped expand the market. The methods to improve the properties of SPI gels, including physical, chemical, and biological properties, are reviewed to provide insights on its role in the properties of SPI gels. To achieve environmentally friendly and efficient ways for the food industry to use SPI gel properties, the research prospects and development trends of the gel properties of SPI are summarized. New developments and practical applications in the production technology, such as for ultrasound, microwave and high pressure, are reviewed. The potential and challenges for practical applications of cold plasma technology for SPI gel properties are also discussed. There is a need to transfer the laboratory technology to actual food production efficiently and safely.

Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study.

Sonicated protein isolates were recovered from Chenopodium quinua, Phaseoulus vulgaris and Lens culinaris to develop a functional matrix by assessing the physicochemical and functional properties. The plant protein isolates were prepared from powdered materials followed by sonication in alkaline medium using a Box-Behnken design. pH (6-10), a buffer-to-material ratio (5:1 to 15:1) and sonication time (0-20 min) were taken as independent variables, whereas protein yield was taken as the dependent variable. A pH of 9, 20 min treatment, and a buffer-to-material ratio of 5:1 were the optimal extraction conditions for quinoa and black beans, whereas a 1:10 ratio was suitable for lentils. Sonication in alkaline medium caused partial protein unfolding and these isolates; in turn, the molecular weight affected the emulsifying activity and stability. Moreover, sonication had a strong effect on the gelation temperature, emulsifying activity, the water, and oil sorption. Sonication improved protein yield and exposed amino acids such as glutamic acid, aspartic acid, leucine and glycine. In turn, thiol groups were responsible for the increased in gelation temperature. The better gelling property coupled with high emulsifying property of these proteins show potential application as protein emulsifiers in the production of gels, sausages, and pet foods.

Study of tobacco-derived proteins in paper coatings.

Replacing synthetic polymers with renewable alternatives is a critical challenge for the packaging industry. This research investigated the use of leaf-based proteins as a sustainable co-binder in the coating formulations for paper-based packaging and other applications. Protein isolates from tobacco leaf and alfalfa concentrates were characterized using the Pierce protein assay, Kjeldahl nitrogen, and gel electrophoresis. The proteins were tested as co-binders in a typical latex-based paper coating formulation. The rheology and water retention properties of the wet coating and the surface, optical, structural, and strength properties of coated papers were measured. The coating performance was affected by the purity, solubility, and molecular weight of the tobacco protein and exhibited a shear-thinning behavior with lower water retention than soy protein. Analysis by scanning electron microscopy and time of flight secondary ion mass spectroscopy on the dried coating layer containing tobacco protein showed enhanced porosity (advantageous for package glueability) relative to the control latex coating. The tobacco protein offers adequate coverage and coating pigment distribution, indicating that this protein can be a suitable option in coatings for packaging applications.

Canola/rapeseed protein - nutritional value, functionality and food application: a review.

Plant-based diet and plant proteins specifically are predestined to meet nutritional requirements of growing population of humans and simultaneously reduce negative effects of food production on the environment. While searching for new sources of proteins, special emphasis should be placed on oilseeds of Brassica family comprising varieties of rapeseed and canola as they contain nutritionally valuable proteins, which have potential to be used in food, but are now rarely or not used as food components. The purpose of the present work is to provide a comprehensive review of main canola/rapeseed proteins: cruciferin and napin, with the focus on their nutritional and functional features, putting special emphasis on their possible applications in food. Technological challenges to obtain rapeseed protein products that are free from anti-nutritional factors are also addressed. As molecular structure of cruciferin and napin differs, they exhibit distinct features, such as solubility, emulsifying, foaming or gelling properties. Potential allergenic effect of 2S napin has to be taken under consideration. Overall, rapeseed proteins demonstrate beneficial nutritional value and functional properties and are deemed to play important roles both in food, as well as, non-food and non-feed applications.

Effects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Walnut Protein Isolate.

The purpose of this paper was to investigate the effect of high-intensity ultrasonication (HIU) pretreatment before enzymolysis on structural conformations of walnut protein isolate (WPI) and antioxidant activity of its hydrolysates. Aqueous WPI suspensions were subjected to ultrasonic processing at different power levels (600-2000 W) and times (5-30 min), and then changes in the particle size, zeta (ζ) potential, and structure of WPI were investigated, and antioxidant activity of its hydrolysates was determined. The particle size of the particles of aqueous WPI suspensions was decreased after ultrasound, indicating that sonication destroyed protein aggregates. The ζ-potential values of a protein solution significantly changed after sonication, demonstrating that the original dense structure of the protein was destroyed. Fourier transform infrared spectroscopy indicated a change in the secondary structure of WPI after sonication, with a decrease in ß-turn and an increase in α-helix, ß-sheet, and random coil content. Two absorption peaks of WPI were generated, and the fluorescence emission intensity of the proteins decreased after ultrasonic treatment, indicating that the changes in protein tertiary structure occurred. Moreover, the degree of hydrolysis and the antioxidant activity of the WPI hydrolysates increased after sonication. These results suggest that HIU pretreatment is a potential tool for improving the functional properties of walnut proteins.

Recent advances in protein derived bionanocomposites for food packaging applications.

This review article critically presents a comprehensive overview of the current advances in the research and development of proteins derived bionanocomposites used in food packaging applications. The recent interest in protein-based biomaterials is due to sustainability, renewability, biodegradability and low carbon footprint. The inherent drawbacks of proteins-based materials for food packaging applications are their low mechanical strength, poor thermal, barrier and inferior physicochemical properties. The nanoreinforced bio-based polymers called bionanocomposites provide an opportunity to overcome these issues and have ability to supersede non-biodegradable food packaging plastics produced from petroleum resources. So far, most studied protein derived bionanocomposites suitable for food packaging are soy protein isolates (SPI) and gelatin proteins. Layered silicates are the most promising nanofillers used to increase strength, improve heat resistance and enhance barrier properties of proteins derived materials while montmorillonites (MMT) is the most commonly used silicate nanofiller. This review emphases on the processing strategies used for proteins-based biomaterials, their mechanical and moisture barrier properties for food packaging applications. Different proteins and nanofillers that have been studied to date in proteins derived food packaging applications are also discussed in detail.

Encapsulation of Bacillus salmalaya 139SI using double coating biopolymer technique.

Sustainable crop production for a rapidly growing human population is one of the current challenges faced by the agricultural sector. However, many of the chemical agents used in agriculture can be hazardous to humans, non-targeted organism and environment. Plant growth promoting rhizobacteria have demonstrated a role in promoting plant growth and health under various stress conditions including disease. Unfortunately, bacterial viability degrades due to temperature and other environmental factors (Bashan et al., Plant Soil 378: 1-33, 2014). Encapsulation of bacteria into core-shell biopolymers is one of the promising techniques to overcome the problem. This study deals with the encapsulation of Bacillus salmalaya 139SI using simple double coating biopolymer technique which consist of brown rice protein/alginate and 0·5% low molecular weight chitosan of pH 4 and 6. The influence of biopolymer to bacteria mass ratio and the chitosan pH on the encapsulation process, physic-chemical, morphology and bioactivity properties of encapsulated B. salmalaya 139SI have been studied systematically. Based on the analysis of physico-chemical, morphology and bioactivity properties, B. salmalaya 139S1 encapsulated using double coating encapsulation technology has promising viability pre- and postfreeze-drying with excellent encapsulation yields of 99·7 and 89·3% respectively. SIGNIFICANCE AND IMPACT OF THE STUDY: The need of a simple yet effective way of encapsulating plant growth promoting rhizobacteria is crucial to further improve their benefits to global sustainable agriculture practice. Effective encapsulation allows for protection, controlled release and function of the micro-organism, as well as providing a longer shelf life for the product. This research report offers an innovative yet simple way of encapsulating using double coating technology with environmentally friendly biopolymers that could degrade and provide nutrients when in soil. Importantly, the bioactivity of the bacteria is maintained upon encapsulation.

Effects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Soy Protein Isolate.

The objective of this study was to investigate the effects of different high-intensity ultrasonication (HIU) pretreatment on the structure and properties of soybean protein isolate (SPI) as well as enzymatic hydrolysis of SPI by bromelain and antioxidant activity of hydrolysates. The HIU-treated SPI fractions showed a decrease in the proportion of α-helices and ß-turns and an increase in the content of ß-sheets and random coils based on Fourier-transform infrared spectroscopy. Near-infrared spectra and fluorescence spectra analyses provided support for the changes in secondary and tertiary structures of SPI after ultrasound treatment. The particle size of SPI decreased from 217.20 nm to 141.23 nm and the absolute zeta potential increased. Scanning electron microscopy showed that HIU treatment changed apparent morphology. Dynamic and static light scattering of ultrasonicated samples showed that SPI structure had changed from hard-sphere to hollow-sphere or polydisperse and monodisperse gaussian coils. HIU pretreatment significantly increased the hydroxyl-radical scavenging and the degree of hydrolysis of the SPI hydrolysates.

Overcoming current challenges in commercial applications of fish protein isolates in food and feed systems: a review.

Over the past 2 decades, the number of scientific papers on properties of fish proteins recovered from various aquatic resources, including the rest raw materials obtained from seafood processing have grown dramatically. Whereas the fish protein isolate (FPI) is a new source of animal protein that can be used to develop value-added food products as well as animal feed enrichment. But to date, very few practical studies have been done on the application of FPI in food and feed systems, and it may have caused the lack of commercial development of this product. Therefore, in order to optimal utilization of aquatic and raw materials in addition to the fight against malnutrition and protein deficiency in poor countries more attention to this technology will be caused this product commercialized. However, for realizing this potential in FPI, several challenges have to be solved. Therefore, this article explores in depth the researches into the use of FPI in food systems and discusses the challenges that this protein source is faced in developing food products. The authors believe that in order to overcome the current challenges in commercial applications of protein isolates in food systems, the following issues should be paying attention and further researches being carried out based on them: industrial process scale-up, production costs, choosing the optimum pH for protein extraction, solubility of proteins, lipid and protein oxidation, the ratio of FPI in food systems, storage stability, sensory defects of FPI, marketing, and economic aspects and future trends of the use of FPI.

Characterization of a soy protein hydrolyzate for the development of a functional ingredient.

Argentina is a leading country in biodiesel production from soy. Extruded soy is a low-cost byproduct of the soybean oil industry, from which animal feeds are prepared as well as flour for human consumption. Soy proteins can be isolated from flours and digested with enzymes in order to obtain bioactive fractions. In this work, a commercial soy isolate (PRO-FAM 974) was characterized. Maximal solubility was achieved at a concentration of 90 mg/mL. Protein profiles obtained by SDS-PAGE showed that the isolate was constituted mostly by globulins. Conformational and thermal analyses (differential scanning calorimetry) showed that proteins were almost completely denatured. The isolate was hydrolyzed with a commercially available enzyme (COROLASE 7089). The peptide profile (MALDI-TOF) showed peptides ranging from 800 to 10,000 Daltons. We conclude that the product obtained has the potential to be used as functional ingredient for the development of functional foodstuffs, giving the opportunity to add value to the byproducts of the soybean oil industry.

Characterizing the Structural and Functional Properties of Soybean Protein Extracted from Full-Fat Soybean Flakes after Low-Temperature Dry Extrusion.

The soy protein isolates (SPI) extracted from different extruded full-fat soybean flakes (FFSF), and their conformational and functional properties were characterized. Overall, the free thiol (SH) content of SPI increased when the extrusion temperature was below 80 °C and decreased at higher temperatures. Soy glycinin (11S) showed higher stability than ß-conglycinin (7S) during extrusion. Results also indicated that the increase in some hydrophobic groups was due to the movement of hydrophobic groups from the interior to the surface of the SPI molecules at extrusion temperatures from 60 to 80 °C. However, the aggregation of SPI molecules occurred at extrusion temperatures of 90 and 100 °C, with decreasing levels of hydrophobic groups. The extrusion temperature negatively affected the emulsifying activity index (EAI); on the other side, it positively affected the emulsifying stability index (ESI), compared to unextruded SPI.

Effects of Limited Hydrolysis and High-Pressure Homogenization on Functional Properties of Oyster Protein Isolates.

In this study, the effects of limited hydrolysis and/or high-pressure homogenization (HPH) treatment in acid conditions on the functional properties of oyster protein isolates (OPI) were studied. Protein solubility, surface hydrophobicity, particle size distribution, zeta potential, foaming, and emulsifying properties were evaluated. The results showed that acid treatment led to the dissociation and unfolding of OPI. Subsequent treatment such as limited proteolysis, HPH, and their combination remarkably improved the functional properties of OPI. Acid treatment produced flexible aggregates, as well as reduced particle size and solubility. On the contrary, limited hydrolysis increased the solubility of OPI. Furthermore, HPH enhanced the effectiveness of the above treatments. The emulsifying and foaming properties of acid- or hydrolysis-treated OPI significantly improved. In conclusion, a combination of acid treatment, limited proteolysis, and HPH improved the functional properties of OPI. The improvements in the functional properties of OPI could potentiate the use of oyster protein and its hydrolysates in the food industry.

High-Pressure Homogenization Pretreatment before Enzymolysis of Soy Protein Isolate: the Effect of Pressure Level on Aggregation and Structural Conformations of the Protein.

The high-pressure homogenization (HPH) treatment of soybean protein isolate (SPI) before enzymatic hydrolysis using bromelain was investigated. Homogenization pressure and cycle effects were evaluated on the enzymatic degree of hydrolysis and the antioxidant activity of the hydrolysates generated. The antioxidant activity of SPI hydrolysates was analyzed by 1,1-dipheny-2-picrylhydrazyl (DPPH). The sizes and structures of the SPI-soluble aggregate after HPH treatment were analyzed using dynamic and static laser light scattering. The changes in the secondary structure, as measured by Fourier transform infrared spectroscopy (FTIR) and the macromorphology of SPI, were measured by scanning electron microscope (SEM). These results suggested that the HPH treatment (66.65%) could increase the antioxidant activities of the SPI hydrolysates compared with the control (54.18%). SPI hydrolysates treated at 20 MPa for four cycles obtained higher DPPH radical-scavenging activity than other samples. The control was predicted to be a hard sphere, and SPI treatment at 10 MPa was speculated to be Gaussian coil, polydisperse, and then the high-pressure treated SPI became a hollow sphere. Changes in the secondary structures showed protein aggregate formation and rearrangements. The image of SPI varied from a globular to a clump structure, as observed by the SEM. In conclusion, combining HPH treatment and enzymolysis could be an effective way to improve the antioxidant activity of the SPI.

The Potential of Combined Emulsification and Spray Drying Techniques for Encapsulation of Polyphenols from Rosemary (Rosmarinus officinalis L.) Leaves.

The present study evaluates the potential of encapsulation of polyphenolic antioxidants from rosemary (Rosmarinus officinalis L.) leaves by combining emulsification and spray drying techniques. To stabilize the emulsions and prepare samples suitable for use in dry products, double emulsions encapsulating rosemary polyphenolic extract and containing polyglycerol polyricinoleate (4%), whey protein isolates (2 and 4%) as emulsifiers, and maltodextrins (MDE 10 and 21) as enhancing coatings were subjected to spray drying. The obtained results show insignificant (p>0.05) effect of used maltodextrin type and protein content on mean particle size of double emulsions containing rosemary polyphenols. Morphology analyses showed that double emulsions were successfully prepared, spherical microcapsules were obtained after spray drying of double emulsions and double emulsion form was still preserved after rehydration of spray-dried microcapsules. Regardless of used maltodextrins, significantly (p>0.05) higher encapsulation efficiencies (EE) of total polyphenols (39.57 and 42.83%) in rehydrated samples were achieved when higher protein content (4% whey protein isolate) was used, indicating the major impact of protein content on EE of rosemary polyphenols. Also, using HPLC analysis, rosmarinic and caffeic acids, apigenin and luteolin derivatives were detected among specific polyphenols, where rosmarinic acid had notable encapsulation efficiency ranging from 62.15 to 67.43%. In this way, the obtained microcapsules encapsulating rosemary polyphenols could be easily blended with various dry mixtures, and serve for delivery in different functional products.