Your browser doesn't support javascript.
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 1.117
Filtrar
1.
J Agric Food Chem ; 68(4): 1051-1063, 2020 Jan 29.
Artigo em Inglês | MEDLINE | ID: mdl-31910005

RESUMO

Glycyrrhizic acid (GA) and GA nanofibrils (GN) have been shown to be efficient natural emulsifiers for formation and stabilization of food emulsions. In this work, the emulsion properties of GN in the presence of soy protein isolate-pectin complex nanoparticles (SPNPs) were studied to understand the impact of the nanofibril-nanoparticle interactions on emulsion stabilization. In the presence of low GN concentrations (0.1-0.5 wt %), the synergy in reducing the interfacial tension was observed due to SPNPs-GN complexation in the bulk and at the interface by hydrogen bonding, endowing the prepared emulsions with an overall smaller droplet size. However, obvious flocculation and clustering of oil droplets occurred in these emulsions (especially at 0.25 and 0.5 wt % GN), which are probably induced by a depletion mechanism. At high GN concentrations (1-2 wt %), due to the preferential adsorption, the GN mainly dominated the interface and the subsequent formation and properties of emulsions. Accordingly, the self-standing emulsion gels were obtained, showing a small droplet size with d32 of about 1.0-1.5 µm, homogeneous appearance and microstructure, and encouraging rheological properties including high gel strength, shear sensitivity, and good thixotropic recovery. This is mainly attributed to the formation of a fibrillar hydrogel network in the continuous phase as well as around the droplet surfaces.


Assuntos
Ácido Glicirrízico/química , Nanofibras/química , Nanopartículas/química , Pectinas/química , Proteínas de Soja/química , Adsorção , Emulsões/química , Géis/química , Tamanho da Partícula
2.
Food Chem ; 313: 126125, 2020 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-31923872

RESUMO

The effect of Mesona blumes polysaccharide (MBP) on the microstructure and gel properties of glucono-delta-lactone-induced soy protein isolate (SPI) gels was evaluated by texture, water holding capacity, rheology, and microstructure analysis. The results showed that the apparent viscosities and storage modulus (G') of the SPI-MBP gels were increased as the MBP concentration increased. The addition of MBP promoted the water holding capacity (WHC) and gel strength of SPI-MBP gels. Scanning electron microscopy (SEM) showed that, in the presence of MBP, the surface of mixed gels became smooth and the structure became dense. Additionally, the zeta potential and interactions results indicated that electrostatic and hydrophobic interactions played an important role in maintaining the three-dimensional structure of SPI-MBP gels. In conclusion, the results of this study suggest that MBP is desirable for SPI-MBP gels as a gelling agent.


Assuntos
Géis/química , Lamiaceae/metabolismo , Polissacarídeos/química , Proteínas de Soja/química , Gluconatos/química , Interações Hidrofóbicas e Hidrofílicas , Lactonas/química , Tamanho da Partícula , Reologia , Eletricidade Estática , Viscosidade , Água/química
3.
Spectrochim Acta A Mol Biomol Spectrosc ; 224: 117400, 2020 Jan 05.
Artigo em Inglês | MEDLINE | ID: mdl-31437763

RESUMO

Water soluble protein content (WSPC) is a parameter of great significance to the soybean food industry. So far, genetic studies and breeding practices have been limited by the lack of a rapid technique for the evaluation of WSPC. Near-infrared reflectance spectroscopy (NIRS) is widely applied for rapid quantification of many traits, including moisture, protein and oil content, and dietary fiber. The present study aimed to establish and evaluate a NIRS regression model for the rapid prediction of WSPC in soybean. Results showed that seed coat color had a profound impact on the accuracy of protein content prediction, whereas the seed coat itself deeply influenced protein determination. We established a partial least squares (PLS) regression model with 167 soybean samples whose seed coat had been removed. Based on multiplicative scatter correction and Savitsky-Golay transformation, the highest determination coefficient (R2) was 0.831, and the relative predictive determinant was 2.417. Further analysis showed that seed roundness correlated negatively with WSPC (r=-0.59, P<0.001) and greatly impacted PLS regression model prediction accuracy. The PLS model was suitable only for intact seeds whose coat had been peeled off, but not for broken seeds, soy powder, and green cotyledon soybean seeds. This study highlights the effect the seed coat has on soybean composition determination by NIRS. Moreover, the established PLS model for soybean WSPC determination could facilitate genetic studies and breeding.


Assuntos
Sementes/química , Proteínas de Soja/análise , Proteínas de Soja/química , Soja/química , Espectroscopia de Luz Próxima ao Infravermelho/métodos , Análise dos Mínimos Quadrados , Reprodutibilidade dos Testes , Água
4.
Food Chem ; 309: 125501, 2020 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-31677451

RESUMO

In this study, we selected two most commonly-available commercial pectin, i.e. citrus pectin and apple pectin as the grafting polysaccharides to prepare soy protein isolate-pectin conjugates. Despite the similar degrees of methoxylation and acetylation for two pectin samples, apple pectin showed much more complex structures compared to citrus pectin, with a 2.20-fold higher molecular weight and large numbers of side chains. The conjugates were prepared under controlled dry-heating conditions and achieved the degree of graft of 25.00% and 21.85% for citrus and apple pectin, respectively. Formation of the conjugates was further confirmed by SDS-PAGE gel electrophoresis and IR spectra. Attributed to the strong steric-hindrance effect of pectin, the fluorescence intensity and surface hydrophobicity of the soy protein isolate were significantly decreased after Maillard reaction. However, both solubility and emulsifying properties of the conjugates were significantly improved. Results indicated that both pectin samples played favorable roles in protein modification.


Assuntos
Citrus/química , Malus/química , Pectinas/química , Proteínas de Soja/química , Emulsões , Calefação , Interações Hidrofóbicas e Hidrofílicas , Reação de Maillard , Solubilidade
5.
Food Chem ; 309: 125718, 2020 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-31753688

RESUMO

The present study was aimed to investigate the effects of non-covalent and covalent interactions between soy protein isolate (SPI) and different concentrations (1, 2 and 5 mM) of (-)-epigallocatechin gallate (EGCG) regarding the structural and functional properties of the complex. The combination with EGCG caused changes in the secondary structure of SPI. The covalent complexes formed at low concentrations of EGCG tended to form a network structure. Compared with the SPI-EGCG non-covalent complexes, the covalent complexes exhibited higher thermal stability and oxidation resistance and a polyphenol-protective effect. In addition, the corresponding anti-digestive ability of the covalent complexes was strong and would therefore be more stable in the intestinal tract. The findings of this study provide a theoretical reference and research basis for the use of different SPI-polyphenol complexes as functional food ingredients or as bioactive materials.


Assuntos
Catequina/análogos & derivados , Proteínas de Soja/química , Antioxidantes/química , Catequina/química , Catequina/metabolismo , Oxirredução , Tamanho da Partícula , Polifenóis/análise , Estabilidade Proteica , Estrutura Secundária de Proteína , Proteínas de Soja/metabolismo , Temperatura Ambiente
6.
Food Chem ; 306: 125593, 2020 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-31610327

RESUMO

The heat-induced aggregation of edible proteins has been regarded as one of the critical challenges for their application in protein-enriched beverages. Therefore, the formulation of thermal stable proteins to improve the stability of these beverages upon heating is highly desired. In this study, soy proteins (SPs) with enhanced heat stability were obtained by low-concentration-preheating (LCPH). Results from reheating of the above samples showed that pretreatment of SPs at low concentrations (≤1.0%, w/v) increased their resistance against aggregation. Additionally, when the suspensions of the particles were reheated at 10% (w/v) protein concentration, no gelation was found for samples prepared by LCPH, indicating collapsed protein-protein interactions, whereas gelled suspensions were obtained for native SPs and samples prepared by preheating at higher protein concentrations (≥2.0%, w/v). Furthermore, suspensions of particles prepared at lower protein concentration showed lower viscosities and higher flow behavior index values before and after reheat treatment. These findings highlighted that LCPH would provide fundamental information on the application of SPs in high protein beverages.


Assuntos
Proteínas de Soja/química , Géis/química , Temperatura Alta , Concentração de Íons de Hidrogênio , Estabilidade Proteica , Viscosidade
7.
Food Chem ; 309: 125579, 2020 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-31683149

RESUMO

The development of functional foods requires a detailed understanding of the behavior of lipophilic protein (LP) in the presence of emulsion stabilizers at different pH conditions. In this study, we examined the interaction between hydroxypropyl methylcellulose (hypromellose, HPMC) and soybean lipophilic protein. To that end, we examined the stabilities of LP-HPMC emulsions at pH 3, 5, and 7, as well as the oil-release behavior of LP-HPMC emulsions during digestion. Fluorescence data showed that HPMC binds to LP with quenching at a single binding site that did not change with pH. Atomic-force microscopy, emulsification, and oxidation-stability analyses showed that HPMC improves the pH stability of the LP-HPMC emulsions, while simulated in-vitro digestion experiments showed that added HPMC delayed the release of lipids to varying degrees. The results of this study will aid in the development of emulsion-based functional foods, pharmaceutical carriers with controlled-release or sustained-release functional ingredients.


Assuntos
Derivados da Hipromelose/química , Proteínas de Soja/química , Emulsões/química , Concentração de Íons de Hidrogênio
8.
Carbohydr Polym ; 228: 115373, 2020 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-31635735

RESUMO

Type of sugar and gelling agents used in confectionery formulations have vital importance since they directly influence physicochemical properties during storage. In this study, the effect of a non-caloric rare sugar, D-allulose (formerly called D-psicose) on the starch based confectionery gels were investigated in the presence and absence of soy protein isolate (SPI) using different experimental techniques for 28 days. For characterization of the formulized gel systems, common techniques were used (SEM, DSC, XRD, moisture content, water activity, hardness and color). Time Domain Nuclear Magnetic Resonance (TD-NMR) technique was also employed to explain dynamics in the systems. Sugar type was found to be a very significant factor affecting gel characteristics and retrogradation. Results showed that D-allulose containing formulations were less prone to retrogradation and showed smaller changes upon storage by supporting presence of better gel network. According to X-ray results, sucrose containing formulations were more susceptible to crystallization. T2 relaxation spectra obtained from NMR experiments showed that number of distinct peaks reduced with the addition of SPI while relaxation times of peaks changed when different type of sugar.


Assuntos
Doces , Armazenamento de Alimentos , Frutose/química , Géis/química , Proteínas de Soja/química , Amido/química , Dureza , Água/química
9.
J Agric Food Chem ; 67(50): 13978-13985, 2019 Dec 18.
Artigo em Inglês | MEDLINE | ID: mdl-31757126

RESUMO

Protein oxidation results in structural modification which affects its digestion. The objective of this work was to investigate the influence of lipoxygenases (LOX) catalyzed linoleic acid (LA) oxidation on the structure and in vitro gastric digests of soybean protein isolate (SPI). Fluorescence recovery after photobleaching (FRAP) was used to evaluate the relationship between pepsin diffusion and gastric digestion. Results indicated that oxidation induced carbonyl formation and loss of free sulfhydryl. Increased surface hydrophobicity and zeta-potential verified the protein unfolding and thus resulted in a small particle size and low fluorescence intensity. Fourier transform infrared spectroscopy (FTIR) showed that oxidation caused the increases in ß-sheets mostly at the expense of α-helix and random coils. Fluorescein isothiocyanate (FITC)-pepsin in SPI solution modified with 3 mL LA showed a faster diffusion rate with 80.51 µm2/s as well as a higher DH value of 9.11%, showing that pepsin diffusivity might play an important role in protein gastric digestion.


Assuntos
Mucosa Gástrica/metabolismo , Ácido Linoleico/metabolismo , Lipoxigenase/metabolismo , Proteínas de Soja/química , Proteínas de Soja/metabolismo , Digestão , Humanos , Interações Hidrofóbicas e Hidrofílicas , Ácido Linoleico/química , Lipoxigenase/química , Modelos Biológicos , Oxirredução , Pepsina A/química , Pepsina A/metabolismo , Dobramento de Proteína , Espectroscopia de Infravermelho com Transformada de Fourier
10.
J Oleo Sci ; 68(11): 1113-1123, 2019 Nov 07.
Artigo em Inglês | MEDLINE | ID: mdl-31611517

RESUMO

This study investigated the impact of ultrasonic modification at various ultrasonic power extents on the freeze-thaw stability of soy protein isolate (SPI) gel. The freeze-thaw stability of the gel was evaluated by examining the changes in texture, water holding capacity, microstructure and soluble protein content during the process of 5 freeze-thaw cycles. In addition, effects on particle size, surface hydrophobicity and structure were also explored. The results showed that within a certain range, the average particle size of the protein gradually decreased, and the particle size distribution was narrower with ultrasonic intensity, it may be due to the high shear and cavitation effects of sonication that reduce the degree of protein aggregation. Furthermore, we also detected that treated proteins had lower fluorescence intensity, higher surface hydrophobicity and more flexible molecular structure with the reduction of α-helical structure as well as the rise of random coil. In terms of gel freeze-thaw stability, moderate ultrasound treatment made the water holding capacity and soluble protein content of SPI gel reduce by 38.27% and 3.58%, whereas the hardness and elasticity increased by 510.23g and 0.06mm after 5 FTC. The corresponding changes of indexes of the control group were 75.05%, 51%, 1062.75g and 0.11mm, respectively. It can be observed that the change range of treated SPI gel properties was smaller than that of natural SPI gel, indicating that ultrasonic treatment can remarkably improve the freeze-thaw stability of the gel which might have something to do with changes of protein structure.


Assuntos
Congelamento , Estabilidade Proteica , Proteínas de Soja/química , Ultrassom , Elasticidade , Géis , Dureza , Interações Hidrofóbicas e Hidrofílicas , Estrutura Molecular , Agregados Proteicos
11.
Molecules ; 24(20)2019 Oct 09.
Artigo em Inglês | MEDLINE | ID: mdl-31600956

RESUMO

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.


Assuntos
Ablação por Ultrassom Focalizado de Alta Intensidade , Estrutura Molecular , Hidrolisados de Proteína/química , Proteínas de Soja/química , Ablação por Ultrassom Focalizado de Alta Intensidade/métodos , Hidrólise , Hidrolisados de Proteína/ultraestrutura , Proteínas de Soja/ultraestrutura , Espectroscopia de Infravermelho com Transformada de Fourier , Relação Estrutura-Atividade
12.
Molecules ; 24(19)2019 Oct 04.
Artigo em Inglês | MEDLINE | ID: mdl-31590314

RESUMO

Proteinaceous materials have numerous structures, many of which aid in the roles they perform. Some need to impart strength while others need elasticity or toughness. This study is the first to investigate the modification of both globular and fibrous protein, namely, zein, soy protein and gelatin, using deep eutectic solvents (DES) to form bioplastics, which may have application in drug delivery systems. The effects of DES content on the thermal and mechanical properties of the material were determined. Zein and soy are globular proteins, which both showed a significant change in the properties by the addition of DES. Both of these materials were, however, weaker and less ductile than the starch based materials previously reported in the literature. The material made from gelatin, a fibrous protein, showed variable properties depending on how long they were in contact with each other before pressing. Conductivity and NMR measurements indicate the existence of a continuous liquid phase, which are useful in the demonstrated application of transdermal drug delivery systems. It is shown that pharmaceutical DESs can be gelled with gelatin and this method is three times faster at delivering a pharmaceutical active ingredient across the skin barrier than from a corresponding solid formulation.


Assuntos
Preparações Farmacêuticas/síntese química , Escleroproteínas/química , Solventes/química , Sistemas de Liberação de Medicamentos , Gelatina/química , Preparações Farmacêuticas/química , Conformação Proteica , Solubilidade , Proteínas de Soja/química , Zeína/química
13.
J Food Sci ; 84(11): 3140-3146, 2019 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-31613008

RESUMO

The interactions between black soybean protein isolate (B-SPI) and cyanidin 3-O-glucoside (C3G), anthocyanin extracted from black soybean coat was investigated under neutral conditions. The fluorescence spectra showed that C3G had fluorescence quenching effects on B-SPI. Thermodynamic parameters showed that ∆G < 0, which demonstrated that the binding was a spontaneous reaction. Since ΔH > 0 and ΔS > 0, the interactions between C3G and B-SPI was mainly hydrophobic interactions. Fourier infrared spectroscopy results suggested that the contents of α-helix and ß-sheet structure showed an increasing trend, whereas the ß-angle content displayed a decreasing trend. The degradation of C3G followed first-order kinetics at 85 °C and 100 °C. After the interactions with B-SPI, the degradation rate constant was decreased and the half-life of C3G was prolonged from 70.25 ± 0.90 min to 175.64 ± 38.04 min at 85 °C, from 62.68 ± 1.1 min to 72.51 ± 2.5 min at 100 °C (p < 0.05). The results indicated that the interactions of B-SPI and C3G improved the thermal stability of C3G under heating conditions.


Assuntos
Antocianinas/química , Glucosídeos/química , Proteínas de Soja/química , Soja/química , Antocianinas/isolamento & purificação , Estabilidade de Medicamentos , Glucosídeos/isolamento & purificação , Temperatura Alta , Estrutura Secundária de Proteína , Proteínas de Soja/isolamento & purificação , Espectrometria de Fluorescência , Espectroscopia de Infravermelho com Transformada de Fourier
14.
J Food Sci ; 84(10): 2820-2830, 2019 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-31518457

RESUMO

This investigation aimed to extract and characterize the GCSM proteins, determine their solubility potential at two different temperatures and different solvents, and explore their functional properties. During the extraction, no water- or ethanol-soluble protein was found. Most of the protein was extracted with KOH solution. GCSM showed major protein bands between 13,273 and 56,564 Da with an isoelectric point of 5.1. The results showed that extraction temperature and solvent affected the amount of protein extracted from GCSM. The highest protein yield (63.4%) was obtained with KOH at 55 °C. Fat content negatively affected the protein solubility. The highest protein purity (99.9%) was obtained with 6% of fat content and the lowest one with 19% of fat content. GCSM has a high glutamic acid content, followed by arginine and aspartic acid compared to the other amino acids. The essential amino acids make up about 30.0% of the total amino acid concentration in KOH-soluble fractions. The results showed a denaturation temperature of GCSM protein ranging from 61.4 to 63.6 °C. Scanning electron microscopy reveals a microglobular protein structure. GCSM protein isolate showed lower (P < 0.05) water-holding and oil-holding capacity but similar gelation properties as soy protein. GCSM protein shows a high foaming capacity at high pH values and high emulsion stability. PRACTICAL APPLICATION: The results of this investigation have a direct impact on the plant protein processing industry. This paper presents a new source of plant protein with a high foaming capacity in alkaline conditions with potential applications for human consumption and feed for aquaculture and animals. The results of this research may impact the cotton producers who can increase their income, and the aquaculture industry will have a cheaper source of protein that can partially substitute the expensive fishmeal. Cottonseed protein can be used to develop high protein extruded snacks and other functional foods, such as plant protein-based food products.


Assuntos
Gossypium/química , Proteínas de Plantas/química , Sementes/química , Sequência de Aminoácidos , Eletroforese , Emulsões/química , Solubilidade , Proteínas de Soja/química , Temperatura Ambiente
15.
Eur J Histochem ; 63(3)2019 Sep 11.
Artigo em Inglês | MEDLINE | ID: mdl-31505925

RESUMO

In mammals, the alveolarization process develops predominantly after birth. Airway cells display a complex assemblage of glycans on their surface. These glycans, particularly terminal glycan extensions, are important effective carriers of information that change during the differentiation process. Nevertheless, few systematic data are reported about the cell surface sugar residue content during post-natal lung development. In the present work, we aimed to identify and semi-quantify N-acetylgalactosamine (GalNAc)/galactose (Gal) residues on the bronchioloalveolar cell surface in rat lung sections from 1-, 4-, 8- day old and adult animals and link these data with the lung glycocalyx composition. Horseradish peroxidase-conjugated lectin from Glycine max (soybean agglutinin, SBA) was used, and light microscopy methodologies were performed. SBA labelling intensity was studied before and after sialidase pre-treatment, at one-, four- and eight-day-old animals and adult animals. For semi-quantitative evaluation of SBA binding intensity, two investigators performed the analysis independently, blinded to the type of experiment. Reactivity of the lectin was assessed in bronchiolar and respiratory portion/alveolar epithelial cell surfaces. We evidenced a stronger positive reaction when lung sections were pre-treated with neuraminidase before incubation with the lectin in one- and four-day-old animals and adult animals. These results were not so manifest in eight-day-old animals. This binding pattern, generally points towards the presence of terminal but mainly sub-terminal GalNAc/Gal residues probably capped by sialic acids on the rat bronchiolar/respiratory tract epithelial cells. As this glycan extension is common in O- and N-glycans, our results suggest that these glycan classes can be present in bronchioloalveolar cells immediately after birth and exist during the postnatal period. The results observed in eight-day-old rat lung sections may be due to the dramatic lung morphologic changes and the possible underlying biological mechanisms that occur during this age-moment.


Assuntos
Acetilgalactosamina/metabolismo , Brônquios/citologia , Células Epiteliais/metabolismo , Galactose/metabolismo , Alvéolos Pulmonares/citologia , Animais , Brônquios/crescimento & desenvolvimento , Feminino , Histocitoquímica/métodos , Peroxidase do Rábano Silvestre/química , Neuraminidase/química , Lectinas de Plantas/química , Gravidez , Alvéolos Pulmonares/crescimento & desenvolvimento , Ratos Wistar , Proteínas de Soja/química
16.
J Oleo Sci ; 68(10): 959-965, 2019 Oct 03.
Artigo em Inglês | MEDLINE | ID: mdl-31511465

RESUMO

Protein hydrolysis on the freeze-thaw stability of emulsions prepared with soy protein - dextran conjugates were investigated. Soy protein isolate-dextran (SPI-D) and soy protein hydrolysates-dextran (SPH-D) conjugates with different degree of hydrolysis (DH) were formed by Maillard reaction. The formation of protein-polysaccharide conjugates between SPI/SPH and dextran molecules was confirmed by SDS-PAGE; this finding was consistent with the degree of glycation and the browning index. The freeze-thaw emulsion stability was investigated. The results confirmed that the SPH3-D (DH at 3%) emulsion with 3% DH of SPI exhibited the lowest creaming index after experiencing 1, 2, and 3 freeze-thaw cycles , with results of 7.69%, 20.74% and 31.30%, respectively. The SPH3-D emulsion had a significantly lower average particle size, which was reduced by 48.28% compared to the SPI-D emulsion. Meanwhile, the SPH3-D solution had low interfacial tension. The confocal laser scanning microscopy analysis indicated that the SPH3-D emulsions were strongly stable against the freeze-thaw treatment and could be used as effective emulsifiers in frozen foods.


Assuntos
Anticoagulantes/química , Dextranos/química , Congelamento , Proteínas de Soja/química , Emulsões , Hidrólise , Estabilidade Proteica , Proteínas de Soja/isolamento & purificação
17.
Int J Mol Sci ; 20(19)2019 Sep 23.
Artigo em Inglês | MEDLINE | ID: mdl-31547569

RESUMO

The development of natural phospholipids for nanostructured drug delivery systems has attracted much attention in the past decades. Lecithin that was derived from naturally occurring in soybeans (SL) has introduced some auspicious accomplishments to the drug carrying aspect, like effectual encapsulation, controlled release, and successful delivery of the curative factors to intracellular regions in which they procure these properties from their flexible physicochemical and biophysical properties, such as large aqueous center and biocompatible lipid, self-assembly, tunable properties, and high loading capacity. Despite the almost perfect properties as a drug carrier, liposome is known to be quite quickly eliminated from the body systems. The surface modification of liposomes has been investigated in many studies to overcome this drawback. In this review, we intensively discussed the surface-modified liposomes that enhancing the targeting, cellular uptake, and therapeutic response. Moreover, the recent applications of soy lecithin-derived liposome, focusing on cancer treatment, brain targeting, and vaccinology, are also summarized.


Assuntos
Antineoplásicos/uso terapêutico , Encéfalo , Neoplasias , Lectinas de Plantas/uso terapêutico , Proteínas de Soja/uso terapêutico , Vacinas/uso terapêutico , Animais , Antineoplásicos/química , Encéfalo/metabolismo , Encéfalo/patologia , Humanos , Lipossomos , Neoplasias/tratamento farmacológico , Neoplasias/metabolismo , Neoplasias/patologia , Lectinas de Plantas/química , Proteínas de Soja/química , Propriedades de Superfície , Vacinas/química
18.
J Oleo Sci ; 68(9): 863-871, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31484902

RESUMO

The variations in average particle size, zeta potential, free fatty acids (FFA) release rate, and the bioavailability of menthol under in vitro simulated digestion conditions of peppermint oil nanoemulsion were investigated. 3D confocal laser scanning microscopy and Cryo-scanning electron microscopy were used to observe the microstructure characteristics of peppermint oil nanoemulsion, which indicated that soybean protein was completely adsorbed at the oil-water interface of the nanoemulsion and presented a core shell structure. And the results indicated that FFA release rate and menthol bioavailability of peppermint oil nanoemulsion prepared by using high-pressure homogenization were much higher. In the simulated gastric digestion phase, the average particle size and the zeta potential of the nanoemulsion increased, and droplet polymerization appeared. After the simulated intestinal, the interfacial protein of nanoemulsion was hydrolyzed, and the oil droplets were digested, which resulted in the decreased particle size and increased absolute value of zeta potential.


Assuntos
Emulsões/química , Nanopartículas/química , Óleos Vegetais/química , Disponibilidade Biológica , Liberação Controlada de Fármacos , Mentha piperita/química , Mentol/farmacocinética , Nanopartículas/ultraestrutura , Tamanho da Partícula , Proteínas de Soja/química , Soja/química
19.
Food Funct ; 10(9): 5485-5497, 2019 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-31411222

RESUMO

Microbial transglutaminase (MTGase) has been developed as a new tofu coagulant in recent years due to its good hydrophilicity, high catalytic activity, and strong thermal stability. This study aimed to investigate the effect of MTGase on the physicochemical properties and immunoreactivity of tofu relative to conventional coagulants [brine and glucono-δ-lactone (GDL)]. Structural changes of the MTGase cross-linked soymilk protein were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), circular dichroism (CD) spectroscopy, ultraviolet (UV) absorption spectroscopy, and fluorescence spectroscopy. The IgE-binding capacity of MTGase cross-linked proteins was tested by enzyme-linked immunosorbent assay (ELISA). The physicochemical properties, quality characteristics, and surface microstructures of five different types of tofu were determined by the Kjeldahl nitrogen method, texture analysis, and scanning electron microscopy (SEM). The digestibility of tofu was evaluated in vitro by simulated gastrointestinal (GIS) digestion. A cell sensitization experiment was performed in vitro to evaluate the capability of tofu digestion products to induce the release of bioactive mediators from human basophil leukemia (KU812) cells. Results indicated that MTGase significantly changed the advanced structure of the soymilk protein. Compared with tofu without MTGase, the composite coagulant tofu containing MTGase exhibited better quality. MTGase improved the water-holding capacity (WHC) of the internal mesh structure and increased the yield of tofu. The digestion products of the composite coagulant tofu, especially the GDL plus MTGase tofu, induced KU812 cells to release fewer bioactive mediators compared with those of MTGase-free tofu. MTGase can not only improve the quality of conventional coagulant tofu but also reduce the potential allergenicity of tofu to a certain extent.


Assuntos
Proteínas de Bactérias/química , Alimentos de Soja/análise , Proteínas de Soja/química , Proteínas de Soja/imunologia , Soja/imunologia , Transglutaminases/química , Alérgenos , Basófilos/imunologia , Biocatálise , Humanos , Soja/química
20.
J Agric Food Chem ; 67(34): 9591-9600, 2019 Aug 28.
Artigo em Inglês | MEDLINE | ID: mdl-31414795

RESUMO

Process conditions that are applied to make structured soy-protein-based food commonly include high temperatures. Those conditions can induce protein oxidation, leading to a decrease in their susceptibility to proteolysis by digestive enzymes. We aimed to investigate the effects of thermomechanical processing on oxidation and in vitro gastric digestion of commercial soy protein ingredients. Samples were sheared at 100 to 140 °C and characterized for acid uptake, carbonyl content, electrophoresis, and surface hydrophobicity. The enzymatic hydrolysis was determined in simulated gastric conditions. Protein ingredients were already oxidized and showed higher surface hydrophobicity and hydrolysis rate compared with those of the processed matrices. However, no clear correlation between the level of carbonyls and the hydrolysis rate was found. Therefore, we conclude that gastric digestion is mostly driven by the matrix structure and composition and the available contact area between the substrate and proteolytic enzymes.


Assuntos
Digestão , Mucosa Gástrica/metabolismo , Proteínas de Soja/metabolismo , Mucosa Gástrica/enzimologia , Humanos , Concentração de Íons de Hidrogênio , Hidrólise , Interações Hidrofóbicas e Hidrofílicas , Modelos Biológicos , Oxirredução , Proteínas de Soja/química
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA