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1.
Adv Colloid Interface Sci ; 326: 103124, 2024 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-38461766

RESUMO

Nanomedicine has a profound impact on various research domains including drug delivery, diagnostics, theranostics, and regenerative medicine. Nevertheless, the clinical translation of nanomedicines for solid cancer remains limited due to the abundant physiological and pathological barriers in tumor that hinder the intratumoral penetration and distribution of these nanomedicines. In this article, we review the dynamic remodeling of tumor extracellular matrix during the tumor progression, discuss the impact of biophysical obstacles within tumors on the penetration and distribution of nanomedicines within the solid tumor and collect innovative approaches to surmount these obstacles for improving the penetration and accumulation of nanomedicines in tumor. Furthermore, we dissect the challenges and opportunities of the respective approaches, and propose potential avenues for future investigations. The purpose of this review is to provide a perspective guideline on how to effectively enhance the penetration of nanomedicines within tumors using promising methods.


Assuntos
Antineoplásicos , Nanopartículas , Neoplasias , Humanos , Nanomedicina , Neoplasias/tratamento farmacológico , Neoplasias/patologia , Sistemas de Liberação de Medicamentos , Matriz Extracelular/patologia , Antineoplásicos/farmacologia , Antineoplásicos/uso terapêutico
2.
Ultrason Sonochem ; 104: 106843, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38471387

RESUMO

The primary significance of this work is that the commercial yeast proteins particles were successfully used to characterize the high internal phase Pickering emulsions (HIPPEs). The different sonication time (0,3,7,11,15 min) was used to modulate the structure and interface characteristics of yeast proteins (YPs) that as Pickering particles. Immediately afterward, the influence of YPs particles prepared at different sonication time on the rheological behavior and coalescence mechanism of HIPPEs was investigated. The results indicate that the YPs sonicated for 7 min exhibited a more relaxed molecular structures and conformation, the smallest particle size, the highest H0 and optimal amphiphilicity (the three-phase contact (θ) was 88.91°). The transition from extended to compact conformations of YPs occurred when the sonication time exceeded 7 min, resulting in an augmentation of size of YPs particles, a reduction in surface hydrophobicity (H0), and an elevation in hydrophilicity. The HIPPEs stabilized by YPs particles sonicated for 7 min exhibited the highest adsorption interface protein percentage and a more homogeneous three-dimensional (3D) protein network, resulting in the smallest droplet size and the highest storage (G'). The HIPPEs sample that stabilized by YPs particles sonicated for 15 min showed the lowest adsorption protein percentage. This caused a reduction in the thickness of its interface protein layer and an enlargement in the droplet diameter (D [3,2]). It was prone to droplet coalescence according to the equation used to evaluate the coalescence probability of droplets (Eq (2)). And the non-adsorbed YPs particles form larger aggregation structures in the continuous phase and act as "structural agents" in 3D protein network. Therefore, mechanistically, the interface protein layer formed by YPs particles sonicated 7 min contributed more to HIPPEs stability. Whereas the "structural agents" contributed more to HIPPEs stability when the sonication time exceeded 7 min. The present results shed important new light on the application of commercial YPs in the functional food fields, acting as an available and effective alternative protein.


Assuntos
Proteínas Fúngicas , Sonicação , Emulsões/química , Interações Hidrofóbicas e Hidrofílicas , Tamanho da Partícula
3.
Gels ; 10(3)2024 Mar 18.
Artigo em Inglês | MEDLINE | ID: mdl-38534623

RESUMO

In this study, the purpose was to investigate the effects with different concentrations of carrageenan (CG, 0-0.30%) on the gel properties and freeze-thaw stability of soy protein isolate (SPI, 8%) cold-set gels. LF-NMR, MRI, and rheology revealed that CG promoted the formation of SPI-CG cold-set gel dense three-dimensional network structures and increased gel network cross-linking sites. As visually demonstrated by microstructure observations, CG contributed to the formation of stable SPI-CG cold-set gels with uniform and compact network structures. The dense gel network formation was caused when the proportion of disulfide bonds in the intermolecular interaction of SPI-CG cold-set gels increased, and the particle size and zeta potential of SPI-CG aggregates increased. SG20 (0.20% CG) had the densest gel network in all samples. It effectively hindered the migration and flow of water, which decreased the damage of freezing to the gel network. Therefore, SG20 exhibited excellent gel strength, water holding capacity, freeze-thaw stability, and steaming stability. This was beneficial for the gel having a good quality after freeze-thaw, which provided a valuable reference for the development of freeze-thaw-resistant SPI cold-set gel products.

4.
Food Chem ; 444: 138601, 2024 Jun 30.
Artigo em Inglês | MEDLINE | ID: mdl-38325083

RESUMO

Recently, MLCTs have attracted considerable attention as a potential alternative to traditional oils due to their suppressive effect on fat accumulation and insulin sensitivity. In this study, the microcapsules of MLCTs with superior performance were fabricated through different homogenization processes to overcome the limitations of ω-3 medium- and long- chain triacylglycerols (MLCTs), including poor stability and prone oxidation. Additionally, the impact of various homogenization techniques, namely, high-pressure, ultrasound, and cavitation jet, on the particle structure, encapsulation efficiency, and oxidation stability of microcapsules (MLCTs) was investigated. The MLCTs microcapsules fabricated through high-pressure homogenization had a smaller particle size of 295.12 nm, lower PDI of 0.24, and a higher zeta-potential absolute value of 32.65, which significantly improved their dispersion and encapsulation efficiency, reaching 94.56 % after the spray-drying process. Furthermore, the low moisture content and superior storage stability of MLCTs microcapsules have the potential to serve as carriers of liposoluble actives.


Assuntos
Ácidos Graxos Ômega-3 , Proteínas de Soja , Cápsulas/química , Ácidos Graxos Ômega-3/química , Oxirredução , Triglicerídeos
5.
Int J Biol Macromol ; 260(Pt 1): 129480, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38237823

RESUMO

Exopolysaccharides (EPS) yield and added concentration of lactic acid bacteria can greatly affect the processing characteristics of fermented milk. In order to investigate the effects and mechanisms of EPS yield and added concentration on fermented milk, researchers extracted EPS from 50 strains of Lactobacillus helvedicus (L. helvedicus) and selected the two strains with the largest difference in EPS yield (L. helvedicus LH18 and L. helvetigus LH33) for subsequent experiments. The physicochemical properties of EPS-LH18 and EPS-LH33 were analyzed. The gel characteristics and protein conformation of fermented milk were studied by means of texture analyzer, rheometer, scanning electron microscopy, nuclear magnetic resonance machine, fluorescence spectrophotometer and circular dichroism. The results indicate that the monosaccharide compositions of EPS-LH18 and EPS-LH33 are the same and have good thermal stability. The texture and rheological properties of L. helveticus LH18 fermented milk are significantly superior to other fermented milk. The reason is that L. helveticus LH18 EPS has the highest yield, which leads to a denser gel structure, lower surface hydrophobicity and free sulfhydryl content of its fermented milk. According to circular dichroism analysis, ß- sheet and random coil are the internal factors leading to the difference in fermented milk gel. In addition, the fermented milk improved even more favorably as the concentration of the two EPS additions increased. As described above, L. helveticus LH18 has the potential to be an excellent yogurt starter, and both of the above EPS can be used as probiotic stabilizer alternatives for fermented dairy products.


Assuntos
Produtos Fermentados do Leite , Lactobacillus helveticus , Probióticos , Animais , Leite/química , Lactobacillus helveticus/metabolismo , Fermentação , Produtos Fermentados do Leite/microbiologia , Iogurte/microbiologia
6.
Food Chem X ; 21: 101066, 2024 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-38268843

RESUMO

At present, there have been many research articles reporting that plant-based protein Pickering particles from different sources are used to stabilize Pickering emulsions, but the reports of corresponding review articles are still far from sufficient. This study focuses on the research hotspots and related progress on plant-based protein Pickering particles in the past five years. First, the article describes the mechanism by which Pickering emulsions are stabilized by different types of plant-based protein Pickering particles. Then, the extraction, preparation, and modification methods of various plant-based protein Pickering particles are highlighted to provide a reference for the development of greener and more efficient plant-based protein Pickering particles. The article also introduces some of the most promising applications of Pickering emulsions stabilized by plant-based protein Pickering particles in the food field. Finally, the paper also discusses the potential applications and challenges of plant-based protein Pickering particles in the food industry.

7.
Int J Biol Macromol ; 256(Pt 1): 128381, 2024 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-38000596

RESUMO

The interactions between carboxymethyl cellulose sodium and proteins can regulate the interfacial and rheological properties of HIPEs, which plays a leading role in the stabilities of HIPEs. This article prepared various ratios of soluble soy protein isolate/carboxymethyl cellulose sodium (SPI/CMC) complexes in different proportions and examined the impact of various ratios of complexes on the structure and interface properties of complexes systems. Additionally, it explored the co-emulsification mechanism of HIPEs using SPI and CMC. At appropriate ratios of SPI/CMC, SPI and CMC mainly combine through non covalent binding and form complexes with smaller particle sizes and stronger electrostatic repulsion. The interfacial properties indicated that adding appropriate CMC increased the pliability and reduced the interfacial tension, while also enhancing the wettability of SPI/CMC complexes. At the ratio of 2:1, the SPI/CMC complexes-stabilized HIPPEs exhibited smaller oil droplets size, tighter droplet packing, and thicker interfacial film through the bridging of droplets and the generation of stronger gel-like network structures to prevent the coalescence/flocculation of droplets. These results suggested that the appropriate ratios of SPI/CMC can improve the physical stability of HIPEs by changing the structure and interface characteristics of the SPI/CMC complexes. This work provided theoretical support for stable HIPEs formed with protein-polysaccharide complexes.


Assuntos
Carboximetilcelulose Sódica , Proteínas de Soja , Proteínas de Soja/química , Emulsões/química , Molhabilidade , Tamanho da Partícula , Sódio
8.
Food Chem X ; 19: 100861, 2023 Oct 30.
Artigo em Inglês | MEDLINE | ID: mdl-37780258

RESUMO

This research explored microwave treatment impact on the structuro-functional aspects of oxidized soy protein aggregates (OSPI). Data showed that oxidative treatment promoted the formation of high molecular weight aggregates through hydrophobic interactions, thereby disrupting the structure of natural soy protein isolates (SPI). Microwave treatment for an appropriate time (≤30 s) caused the molecular structure of OSPI to open up and reduction in molecular weight and disulfide bond content, while absolute zeta potential increased. These modifications increased emulsifying capacity of OSPI, as well as the interfacial adsorption of protein. Longer microwave treatment times (>30 s) caused OSPI to exhibit a tendency to aggregate in TEM and CLSM images. It indicated the appropriate microwave electromagnetic field effect and microwave heating effect could coordinatively regulate soy protein functional properties by modifying their aggregation behavior. The results provided new ideas for reducing resource waste, and further expanding soy protein application in the food industry.

9.
Ultrason Sonochem ; 96: 106421, 2023 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-37137245

RESUMO

The protein conformation of soymilk is the key to affecting the instant solubility of soymilk flour. This study aimed to evaluate the effect of cavitation jet treatment time (0, 2, 4, 6, and 8 min) on the instant solubility of soymilk flour based on the conformational changes of protein in soymilk. The results showed that the cavitation jet treatment for 0-4 min significantly unfolded the protein structure of soymilk and increased the content of soluble protein, which reduced the particle size and increased the electrostaticrepulsion and the viscosity of soymilk. This was beneficial for soymilk droplets fully atomized and repolymerized in the spray drying tower, forming soymilk flour particles with large size, smooth surface, and uniform distribution. When the cavitation jet treatment time was 4 min, the wettability (from 127.3 ± 2.5 s to 84.7 ± 2.1 s), dispersibility (from 70.0 ± 2.0 s to 55.7 ± 2.1 s), and solubility (from 56.54% to 78.10%) of soymilk flour were significantly improved. However, when the time of the cavitation jet treatment was extended to 8 min, the protein of soymilk aggregated and the stability of soymilk decreased, which reduced the particle size and hurt the surfacecharacteristics of soymilk flour after spraydrying. It resulted in a decrease in the instant solubility of soymilk flour. Therefore, the cavitationjet treatment with proper time increases the instant solubility of soymilk flour by improving the protein conformation of soymilk.


Assuntos
Farinha , Leite de Soja , Solubilidade , Fenômenos Químicos , Leite de Soja/química , Conformação Proteica
10.
Foods ; 12(10)2023 May 13.
Artigo em Inglês | MEDLINE | ID: mdl-37238801

RESUMO

Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, and the gel properties of soy protein isolate (SPI) in myofibril protein (MP) was evaluated. The study found that four industrial modifications did not influence the subunit composition of SPI. However, the four industrial modifications altered SPI's secondary structure and disulfide bond conformation content. A-SPI exhibits the highest surface hydrophobicity and I850/830 ratio but the lowest thermal stability. G-SPI exhibits the highest disulfide bond content and the best gel properties. Compared with MP gel, the addition of H-SPI, A-SPI, G-SPI, and O-SPI components significantly improved the properties of the gel. Additionally, MP-ASPI gel exhibits the best properties and microstructure. Overall, the four industrial modification effects may impact SPI's structure and gel properties in different ways. A-SPI could be a potential functionality-enhanced soy protein ingredient in comminuted meat products. The present study results will provide a theoretical basis for the industrialized production of SPI.

11.
Microbiol Spectr ; 11(3): e0081423, 2023 06 15.
Artigo em Inglês | MEDLINE | ID: mdl-37074200

RESUMO

A simple model of alternative microbiota in the developing intestinal environment has been highly desirable for the study of health and disease in the gut. The pattern of antibiotic depletion of natural gut microbes is necessary for this model. However, the effects and loci of antibiotic deletion of gut microbes remain unclear. In this study, a mixture of three proven broad-spectrum antibiotics was selected to study their effects on microbial deletions in the jejunum, ileum, and colon of mice. The 16S rRNA sequencing results showed that antibiotics significantly reduced colonic microbial diversity, with limited effects on the jejunum and ileum. At the level of microbial genera, only 93.38% of Burkholderia-Caballeronia-Paraburkholderia and 5.89% of Enterorhabdus were present in the colon after antibiotic treatment. However, such changes were not observed in the microbial composition of the jejunum and ileum. Our results suggest that the antibiotics depleted intestinal microorganisms by acting primarily in the colon and not in the small intestine (jejunum and ileum). IMPORTANCE Many studies have applied antibiotics to delete intestinal microbes to shape pseudosterile mouse models and further used for fecal microbial transplantation. However, few studies have explored the spatial location of antibiotic action in the intestine. This study shows that the selected antibiotics effectively deleted microbiota in the colon of mice, with limited effects on microbes in the jejunum and ileum. Our study provides guidance for the application of a mouse model of antibiotic deletion of intestinal microbes.


Assuntos
Antibacterianos , Microbioma Gastrointestinal , Animais , Camundongos , Antibacterianos/farmacologia , RNA Ribossômico 16S/genética , Intestino Delgado , Colo
12.
Foods ; 12(5)2023 Feb 21.
Artigo em Inglês | MEDLINE | ID: mdl-36900426

RESUMO

A cavitation jet can enhance food proteins' functionalities by regulating solvable oxidized soybean protein accumulates (SOSPI). We investigated the impacts of cavitation jet treatment on the emulsifying, structural and interfacial features of soluble soybean protein oxidation accumulate. Findings have shown that radicals in an oxidative environment not only induce proteins to form insoluble oxidative aggregates with a large particle size and high molecular weight, but also attack the protein side chains to form soluble small molecular weight protein aggregates. Emulsion prepared by SOSPI shows worse interface properties than OSPI. A cavitation jet at a short treating time (<6 min) has been shown to break the core aggregation skeleton of soybean protein insoluble aggregates, and insoluble aggregates into soluble aggregates resulting in an increase of emulsion activity (EAI) and constancy (ESI), and a decrease of interfacial tension from 25.15 to 20.19 mN/m. However, a cavitation jet at a long treating time (>6 min) would cause soluble oxidized aggregates to reaggregate through an anti-parallel intermolecular ß-sheet, which resulted in lower EAI and ESI, and a higher interfacial tension (22.44 mN/m). The results showed that suitable cavitation jet treatment could adjust the structural and functional features of SOSPI by targeted regulated transformation between the soluble and insoluble components.

13.
Foods ; 12(5)2023 Mar 05.
Artigo em Inglês | MEDLINE | ID: mdl-36900624

RESUMO

The impacts of industrial phosphorylation on the structural changes, microstructure, functional, and rheological features of soybean protein isolate (SPI) were spotlighted. The findings implied that the spatial structure and functional features of the SPI changed significantly after treatment with the two phosphates. Sodium hexametaphosphate (SHMP) promoted aggregation of SPI with a larger particle size; sodium tripolyphosphate (STP) modified SPI with smaller particle size. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) results showed insignificant alterations in the structure of SPI subunits. Fourier transform infrared (FTIR) and endogenous fluorescence noted a decline in α-helix quantity, an amplification in ß-fold quantity, and an increase in protein stretching and disorder, indicating that phosphorylation treatment fluctuated the spatial structure of the SPI. Functional characterization studies showed that the solubility and emulsion properties of the SPI increased to varying degrees after phosphorylation, with a maximum solubility of 94.64% for SHMP-SPI and 97.09% for STP-SPI. Emulsifying activity index (EAI) and emulsifying steadiness index (ESI) results for STP-SPI were better than those for SHMP-SPI. Rheological results showed that the modulus of G' and G″ increased and the emulsion exhibited significant elastic behavior. This affords a theoretical core for expanding the industrial production applications of soybean isolates in the food and various industries.

14.
Food Chem ; 410: 135413, 2023 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-36623461

RESUMO

The gut microbiota plays an evolutionarily conserved role in host metabolism, which is influenced by diet. Here, we investigated differences in shaping the gut microbiota and regulating metabolism in cow milk-based infant formula, goat milk-based infant formula, and mix milk-based infant formula compared with pasteurized human milk. 16S rRNA results showed that goat milk-based infant formula selectively increased the relative abundance of Blautia, Roseburia, Alistites and Muribaculum in the gut compared to other infant formulas. Metabolomics identification indicated that goat milk-based infant formula mainly emphasized bile acid biosynthesis, arachidonic acid metabolism and steroid biosynthesis metabolic pathways. Metabolites associated with these metabolic pathways were positively associated with increased microorganisms in goat milk-based infant formula, particularly Alistipes. Furthermore, we found a deficiency of Akkermansia abundance in three infant formula-fed compared to pasteurizedhuman milk-fed. This study presents new insights into the improvement and application of goat milk-based infant formulas in terms of intestinal microecology.


Assuntos
Microbioma Gastrointestinal , Fórmulas Infantis , Bovinos , Feminino , Humanos , Animais , Lactente , Camundongos , Microbioma Gastrointestinal/fisiologia , RNA Ribossômico 16S/genética , Leite Humano , Fezes , Cabras/genética
15.
Front Nutr ; 9: 1054326, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-36505251

RESUMO

This paper investigates the effect on the physicochemical and functional properties of soybean protein concentrate (SPC) by using Alcalase protease and high-pressure homogenization (HPH) (0, 20, 40, 60, 80, and 100 MPa) for the combined modification. The results showed that the degree of hydrolysis of SPC was 4.1% and the antigen protein was degraded after Alcalase hydrolysis, when the homogenization pressure (HP) was 6 0Mpa, the particle size of the SPC was the smallest, the zate potential absolute value up to 33.45 mV, the secondary structure has the lowest ß-sheet content, the highest random coil content, and the highest surface hydrophobicity (H0), the size of protein fragments on the microstructure surface is the smallest, the lowest denaturation temperature (T d ) and enthalpy (△H) are 72.59°C and 1.35 J/g, the highest solubility is 80.54%, and the highest water and oil holding capacities are 7.73 g/g and 6.51 g/g, respectively. The best emulsifying activity and emulsifying stability were 43.46 m2/g and 190.35 min, the most even distribution of emulsion droplets. This indicates that the HPH treatment destroys the structure of enzymatic hydrolyzed SPC, changes its physicochemical properties, and improves its functional properties. In this study, SPC was modified by HPH and enzyme combined treatment, in order to improve the functionality and application range of SPC, and provide a theoretical basis for its high-value utilization in the food field.

16.
Front Microbiol ; 13: 1028919, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-36274719

RESUMO

Ulcerative colitis (UC) is challenging to treat and severely impacts patients and families. A previous study reported immunomodulatory and reduction of pro-inflammatory properties for the Lactiplantibacillus plantarum L15. This study aimed to analyze the preventive properties and mechanistic actions in an in vivo colitis model. The histopathological alteration, inflammation cytokines, and intestinal barrier function were analyzed. Subsequently, the cecal gut microbiota contents and products from different groups were detected. Finally, gene expressions related to the NF-κB signaling process were evaluated. L. plantarum L15 significantly decreased disease activity index (DAI), myeloperoxidase activity (MPO), pro-inflammatory cytokine (TNF-α, IL-1ß, and IL-6) level, and increased weight change, colon length, and production of inflammation-suppressing cytokines. Furthermore, this strain supplementation substantially increased ZO-1, Occludin, and Claudin-1, and MUC2 mRNA expression levels with a corresponding decrease in serum lipopolysaccharide and D-lactic acid contents. In addition, L. plantarum L15 improved gut microbiota composition and increased short-chain fatty acid (SCFAs) in the colon content, which significantly reduced the transfer of NF-κB p65 to the nucleus. Our findings provide a theoretical basis for L. plantarum L15 as a preventive candidate for UC.

17.
Food Chem X ; 15: 100382, 2022 Oct 30.
Artigo em Inglês | MEDLINE | ID: mdl-36211760

RESUMO

The emulsifying activity of soy protein would decrease after long-term storage, which caused huge economic losses to food processing plants. This study explored the temporal evolution mechanism of oxidation on the structure and function of soy protein aggregates, which would improve the application of soy protein in food industry. Decreased α-helix and increased random coil were observed at the initial oxidation stage (0-4 h), which induced increases in hydrophobicity and disulfide bond content. In addition, emulsibility increased significantly. However, when the oxidation time extended to 6-12 h, the soluble aggregates transformed into insoluble aggregates with large particle size, low solubility, and molecular flexibility. Surface hydrophobicity and emulsifying activity were reduced, resulting in bridging flocculation of emulsion droplets. Mutual transformation between components is affected by factors that include spatial conformation and intermolecular forces, which eventually lead to functional changes in the protein molecules.

18.
Ultrason Sonochem ; 88: 106075, 2022 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-35753139

RESUMO

The combination of protein and flavonoids can ameliorate the problems of poor solubility and stability of flavonoids in utilization. In this study, soybean protein isolate pretreated by ultrasonication was selected as the embedding wall material, which was combined with luteolin to form a soybean protein isolate-luteolin nanodelivery system. The complexation effect and structural changes of soybean protein isolate (SPI) and ultrasonic pretreatment (100 W, 200 W, 300 W, 400 W and 500 W) of soybean protein isolate with luteolin (LUT) were compared, as well as the changes in digestion characteristics and antioxidant activity in vitro. The results showed that proper ultrasonic pretreatment increased the encapsulation efficacy, loading amount and solubility to 89.72%, 2.51 µg/mg and 90.56%. Appropriate ultrasonic pretreatment could make the particle size and the absolute value of ζ-potential of SPI-LUT nanodelivery system decrease and increase respectively. The FTIR and fluorescence results show that appropriate ultrasonic pretreatment could reduce α-helix, ß-sheet and random coil, increase ß-turn, and enhance fluorescence quenching. The thermodynamic evaluation results indicate that the ΔG < 0, ΔH > 0 and ΔS > 0, so the interaction of LUT with the protein was spontaneous and mostly governed by hydrophobic interactions. The XRD results show that the LUT was amorphous and completely wrapped by SPI. The DSC results showed that ultrasonic pretreatment could improve the thermal stability of SPI-LUT nanodelivery system to 112.66 ± 1.69 °C. Digestion and antioxidant analysis showed that appropriate ultrasonic pretreatment increased the LUT release rate and DPPH clearance rate of SPI-LUT nanodelivery system to 89.40 % and 55.63 % respectively. This study is a preliminary source for the construction of an SPI nanodelivery system with ultrasound pretreatment and the deep processing and utilization of fat-soluble active substances.


Assuntos
Luteolina , Proteínas de Soja , Disponibilidade Biológica , Solubilidade , Proteínas de Soja/química , Ultrassom
19.
Foods ; 11(10)2022 May 16.
Artigo em Inglês | MEDLINE | ID: mdl-35627001

RESUMO

In this study, pea residue reserve insoluble diet fiber (hereinafter referred to as pea fiber) was used as a raw material. The effects of γ-irradiation doses (0, 0.5, 1, 2, 3, and 5 kGy) on the structural properties (main composition, particle size and specific surface area, scanning electron microscope (SEM) microstructure, Fourier transform infrared spectroscopy, and X-ray diffraction) and functional properties (oil-holding capacity, swelling and water-holding capacity, and adsorption properties) of pea fiber were explored. The results show that, when the γ-irradiation dose was 2 kGy, compared with the untreated sample, the contents of cellulose, hemicellulose and lignin in pea fiber decreased by 1.34 ± 0.42%, 2.56 ± 0.03% and 2.02 ± 0.05%, respectively, and the volume particle size of pea fiber decreased by 17.43 ± 2.35 µm. The specific surface area increased by 23.70 ± 2.24 m2/kg and the crystallinity decreased by 7.65%. Pore and irregular particles appeared on the microstructure surface of the pea fiber treated with γ-irradiation. The results of the infrared spectrum showed that the hemicellulose and lignin in pea fiber were destroyed by γ-irradiation. These results indicate that γ-irradiation can significantly affect the structural properties of pea fiber. When the γ-irradiation dose was 2 kGy, the highest oil-holding capacity, swelling capacity and water-holding capacity of pea fiber were 8.12 ± 0.12 g/g, 19.75 ± 0.37 mL/g and 8.35 ± 0.18 g/g, respectively, and the adsorption capacities of sodium nitre, cholesterol and glucose were also the strongest. These results indicate that the functional properties of pea fiber are improved by γ-irradiation. In this study, γ-irradiation technology was used as pretreatment to provide a theoretical basis for the application of pea fiber in food processing.

20.
Ultrason Sonochem ; 87: 106046, 2022 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-35636156

RESUMO

Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean protein aggregates (OSPI). The results showed that oxidative treatment could disrupt the native soy protein (SPI) structure by promoting the formation of oxidized aggregates with ß1-sheet structures through hydrophobic interactions. These changes led to a decrease in the solubility, emulsification ability and interfacial activity of soybean protein. After low-power ultrasound (100 W, 200 W) treatment, the relative contents of ß1-sheets, ß2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute ζ-potential value and free sulfhydryl content decreased. Moreover, protein aggregates with larger particle sizes and poor solubility were formed. The emulsions prepared using the OSPI showed bridging flocculation and decreased protein adsorption and interfacial tension. After applying medium-power ultrasound (300 W, 400 W, and 500 W) treatments, the OSPI solubility increased and particle size decreased. The α-helix and ß-turn contents, surface hydrophobicity and absolute ζ-potential value increased, the structure unfolded, and the disulfide bond content decreased. These changes improved the emulsification activity and emulsion state of the OSPI and increased the protein adsorption capacity and interfacial tension of the emulsion. However, after a high-power ultrasound (600 W) treatment, the OSPI showed a tendency to reaggregate, which had a certain negative effect on the emulsification activity and interfacial activity. The results showed that UT at an appropriate power could depolymerize OSPI and improve the emulsification and interfacial activity of soybean protein.


Assuntos
Agregados Proteicos , Proteínas de Soja , Dissulfetos/química , Emulsificantes/química , Emulsões/química , Interações Hidrofóbicas e Hidrofílicas , Proteínas de Soja/química
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