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1.
The potential of utilizing interfacial complexes, formed through the electrostatic interactions of proteins and polysaccharides at oil-water interfaces, to stabilize model beverage cloud emulsions has been examined. These interfacial complexes were formed by mixing charged polysaccharides with oil-in-water emulsions containing oppositely charged protein-coated oil droplets. Model beverage emulsions were prepared that consisted of 0.1 wt % corn oil droplets coated by beta-lactoglobulin (beta-Lg), beta-Lg/alginate, beta-Lg/iota-carrageenan, or beta-Lg/gum arabic interfacial layers (pH 3 or 4). Stable emulsions were formed when the polysaccharide concentration was sufficient to saturate the protein-coated droplets. The emulsions were subjected to variations in pH (from 3 to 7), ionic strength (from 0 to 250 mM NaCl), and thermal processing (from 30 or 90 degrees C), and the influence on their stability was determined. The emulsions containing alginate and carrageenan had the best stability to ionic strength and thermal processing. This study shows that the controlled formation of protein-polysaccharide complexes at droplet surfaces may be used to produce stable beverage emulsions, which may have important implications for industrial applications.  相似文献   

2.
Intermolecular disulfide bond formation in pure beta-lactoglobulin (beta-Lg) B and in its 1:1 mixture with alpha-lactalbumin (alpha-La), heated at 85 degrees C for 10 min in solutions of low and high (100 mM NaCl) ionic strength and pH 6.0, was studied by reverse-phase HPLC and MALDI-TOF mass spectrometry. Disulfide bonding between beta-Lg monomers was more extensive than reported in the literature for a temperature of 68.5 degrees C, including formation of trimers connected by two of the three adjacent cysteines, C106/C119/C121. The participation of the different thiol groups in disulfide bonds appeared to depend on their location in the native structure, with surface-located cysteines more involved than internally located ones. This also applied to alpha-La-beta-Lg interactions, where the predominant participants were the surface-located alphaC111, alphaC120, alphaC61, and alphaC6. The least active participant was alphaC28, suggesting that it becomes sterically inaccessible during unfolding of the protein. High ionic strength apparently promoted disulfide bonding. The order of cysteine participation at the high ionic strength was similar to that at low ionic strength, with fewer native-location bonds observed and a lower activity of some groups, such as beta-C106/C119/C121 and alphaC61.  相似文献   

3.
The physical aggregation of commercial whey protein isolate (WPI) and purified beta-lactoglobulin was studied by ultrasound spectroscopy. Protein samples were dialyzed to achieve constant ionic strength backgrounds of 0.01 and 0.1 NaCl, and gelation was induced in situ at constant temperatures (from 50 to 75 degrees C) or with a temperature ramp from 20 to 85 degrees C. Changes in the ultrasonic properties were shown in the early stages of heating, at temperatures below those reported for protein denaturation. During heating, the relative ultrasound velocity (defined as the difference between sample velocity and reference velocity) decreased continuously with temperature, indicating a rearrangement of the hydration layer of the protein and an increase in compressibility of the protein shell. At temperatures <50 degrees C the ultrasonic attenuation decreased, and <65 degrees C both velocity and attenuation differentials showed increasing values. A sharp decrease in the relative velocity and an increase in the attenuation at 70 degrees C were indications of "classical" protein denaturation and the formation of a gel network. Values of attenuation were significantly different between samples prepared with 0.01 and 0.1 M NaCl, although no difference was shown in the overall ultrasonic behavior. WPI and beta-lactoglobulin showed similar ultrasonic properties during heating, but some differences were noted in the values of attenuation of WPI solutions, which may relate to a less homogeneous distribution of aggregates caused by the presence of alpha-lactalbumin and other minor proteins in WPI.  相似文献   

4.
The aggregation behavior during heating of a solution containing soy protein and whey protein isolate (WPI) was studied using rheology, confocal microscopy, gel filtration, and electrophoresis. Soy/WPI mixtures formed gels at 6% total protein concentration with a high elastic modulus (G') and no apparent phase separation. The ratio of soy to WPI was fundamental in determining the type of network formed. Systems containing a high soy to WPI ratio (>70% soy protein) showed a different evolution of the elastic modulus during heat treatment, with two apparent stages of network development. Whey proteins formed disulfide bridges with soy proteins during heating, and at low ratios of soy/WPI, the aggregates seemed to be predominantly formed by 7S, the basic subunits of 11S and beta-lactoglobulin. Size exclusion chromatography indicated the presence of high molecular weight soluble complexes in mixtures containing high soy/WPI ratios. Results presented are the first evidence of interactions between soy proteins and whey proteins and show the potential for the creation of a new group of functional ingredients.  相似文献   

5.
1H NMR was used to study the effect of high pressure on changes in the structure of beta-lactoglobulin (beta-Lg), particularly the strongly bonded regions, the "core". beta-Lg was exposed to pressures ranging from 100 to 400 MPa at neutral pH. After depressurization and acidification to pH 2.0, (1)H NMR spectra were taken. Pressure-induced unfolding was studied by deuterium exchange. Refolding was also evaluated. Our results showed that the core was unaltered at 100 MPa but increased its conformational flexibility at >/=200 MPa. Even though the core was highly flexible at 400 MPa, its structure was found to be identical to the native structure after equilibration back to atmospheric pressure. It is suggested that pressure-induced aggregates are formed by beta-Lg molecules maintaining most of their structure, and the intermolecular -SS- bonds, formed by -SH/-SS- exchange reaction, are likely to involve C(66)-C(160) rather than C(106)-C(119). In addition, the beta-Lg variants A and B could be distinguished in a (1)H NMR spectrum from a solution made with the AB mixed variant, by the differences in chemical shifts of M(107) and C(106); structural implications are discussed. Under pressure, the core of beta-Lg A seemed to unfold faster than that of beta-LgB. The structural recovery of the core was full for both variants.  相似文献   

6.
Thermal denaturation, rheological, and microstructural properties of gels prepared from native beta-lactoglobulin (beta-LG) and preheated or heat-denatured beta-LG (HDLG) aggregates were compared. The HDLG was prepared by heating solutions of 4% beta-LG in deionized water, pH 7.0, at 80 degrees C for 30 min and then diluted to the desired concentration in 0.6 M NaCl and 0.05 M phosphate buffer at pH 6.0, 6.5, and 7.0. When reheated to 71 degrees C, HDLG formed a gel at a concentration of 2% protein. At pH 7.0, 3% HDLG gelled at 52.5 degrees C and had a storage modulus (G') of 2200 Pa after cooling. beta-LG (3%) in 0.6 M NaCl and 0.05 M phosphate buffer, pH 7.0, did not gel when heated to 71 degrees C. The gel point of 3% HDLG decreased by 10.5 degrees C and the G' did not change when the pH was decreased to 6.0. The HDLG gel microstructure was composed of strands and clumps of small globular aggregates in contrast to beta-LG gels, which contained a particulate network of compacted globules. The HDLG formed a gel at a lower concentration and lower temperature than beta-LG in the high-salt buffer, suggesting an application in meat systems or other food products prepared with salt and processed at temperatures of < or =71 degrees C.  相似文献   

7.
The effects of several conditions on the amounts and compositions of aggregates formed in mixtures of whey protein hydrolysate, made with Bacillus licheniformis protease, and whey protein isolate were investigated using response surface methodology. Next, the peptides present in the aggregates were separated from the intact protein and identified with liquid chromatography-mass spectrometry. Increasing both temperature and ionic strength increased the amounts of both intact protein and peptides in the aggregates. There was an optimal amount of added intact WPI that could aggregate with peptides, yielding a maximal amount of aggregated material in which the peptide/protein molar ratio was around 6. Under all conditions applied, the same peptides were observed in the protein-peptide aggregates formed. The dominant peptides were beta-lg AB [f1-45], beta-lg AB [f90-108], and alpha-la [f50-113]. It was hypothesized that peptides could form a kind of glue network that can include beta-lactoglobulin via hydrophobic interactions at the hydrophobic binding sites at the surface of the protein.  相似文献   

8.
The properties of whey protein isolate (WPI) stabilized oil-in-water (O/W) nanoemulsions (d(43) ≈ 66 nm; 0.5% oil, 0.9% WPI) and emulsions (d(43) ≈ 325 nm; 0.5% oil, 0.045% WPI) were compared. Emulsions were prepared by high-pressure homogenization, while nanoemulsions were prepared by high-pressure homogenization and solvent (ethyl acetate) evaporation. The effects of pH, ionic strength (0-500 mM NaCl), thermal treatment (30-90 °C), and freezing/thawing on the stability and properties of the nanoemulsions and emulsions were compared. In general, nanoemulsions had better stability to droplet aggregation and creaming than emulsions. The nanoemulsions were unstable to droplet flocculation near the isoelectric point of WPI but remained stable at higher or lower pH values. In addition, the nanoemulsions were stable to salt addition, thermal treatment, and freezing/thawing (pH 7). Lipid oxidation was faster in nanoemulsions than emulsions, which was attributed to the increased surface area. Lipase digestibility of lipids was slower in nanoemulsions than emulsions, which was attributed to changes in interfacial structure and protein content. These results have important consequences for the design and utilization of food-grade nanoemulsions.  相似文献   

9.
Oil-in-water emulsions containing droplets stabilized by beta-lactoglobulin (beta-Lg)-pectin membranes were produced using a two-stage process. A primary emulsion containing small droplets (d(32) approximately 0.3 microm) was prepared by homogenizing 10 wt % corn oil with 90 wt % aqueous solution (1 wt % beta-Lg, 5 mM imidazole/acetate buffer, pH 3.0) using a high-pressure valve homogenizer. The primary emulsion was then diluted with pectin solutions to produce secondary emulsions with a range of pectin concentrations (5 wt % corn oil, 0.45 wt % beta-Lg, 5 mM imidazole/acetate buffer, 0-0.22 wt % pectin, pH 3.0). The electrical charge on the droplets in the secondary emulsions decreased from +33 +/- 3 to -19 +/- 1 mV as the pectin concentration was increased from 0 to 0.22 wt %, which indicated that pectin adsorbed to the droplet surfaces. The mean particle diameter of the secondary emulsions was small (d(32) < 1 microm) at relatively low pectin concentrations (<0.04 wt %), but increased dramatically at higher pectin concentrations (e.g., d(32) approximately 13 microm at 0.1 wt % pectin), which was attributed to charge neutralization and bridging flocculation effects. Emulsions with relatively small mean particle diameters (d(32) approximately 1.2 microm at 0.1 wt % pectin) could be produced by disrupting flocs formed in secondary emulsions containing highly negatively charged droplets, for example, by sonication, blending, or homogenization. The particles in these emulsions probably consisted of small flocs containing a number of protein-coated droplets bound together by pectin molecules. These emulsions had good stability to further particle aggregation up to relatively high ionic strengths (< or =500 mM NaCl) and low pH (pH 3). The interfacial engineering technology used in this study could lead to the creation of food emulsions with improved physicochemical properties or stability.  相似文献   

10.
The influence of gamma-irradiation (32 kGy) followed by the addition of polysaccharides (potato starch, soluble potato starch, and sodium alginate) and heating on the properties of the films based on calcium caseinate (CC)-whey proteins isolate (WPI) and the gels formed with CaCl(2) was evaluated. Radiation induced an improvement of the mechanical and barrier properties of all films. The polysaccharides' effect on the irradiated and non-irradiated CC-WPI gels could be predicted as the sum of their separate effects on CC and on WPI, apart from the alginate interaction with the irradiated CC-WPI. The better properties of the films achieved after admixing polysaccharides to the formerly irradiated protein solution correspond to the smaller strength of gels. Properties of the films and gels prepared using the irradiated proteins and alginate differed depending on whether alginate was admixed before or after irradiation. Results were related to the protein structure, interaction with polysaccharides, and the film's microstructure.  相似文献   

11.
The effect of heat-denatured whey protein isolate (dWPI)/whey protein isolate (WPI) ratio (0-0.6), microfluidization pressure (0-1000 bar), and number of passes (1-10) on the uniaxial shear stress at 10% (sigma(10)) and 80% (sigma(80)) relative deformation of dWPI/WPI heat-induced gels (14% total protein, w/w) was studied. No correlation between the average diameter of aggregates and the dWPI/WPI ratio, microfluidization pressure, or number of passes was found. However, increasing the microfluidization pressure or the number of passes resulted in a narrower size distribution of aggregates. Increasing the dWPI/WPI ratio and the number of passes resulted in a decrease and an increase of gel hardness, respectively. The results were interpreted in terms of more random aggregation/gelation of proteins in the presence of aggregates that could result in localized heterogeneities into gels and more dissipation of the deformation energy during compression. The positive effect of the number of passes on the gel hardness was also considered to be due to a more homogeneous aggregation/gelation of proteins in the presence of smaller aggregates.  相似文献   

12.
The mechanical properties, moisture contents (MC), and glass transition temperature (T(g)) of whey protein isolate (WPI) films were studied at various pH values using sorbitol (S) as a plasticizer. The films were cast from heated aqueous solutions and dried in a climate chamber at 23 degrees C and 50% relative humidity (RH) for 16 h. The critical gel concentrations (c(g)) for the cooled aqueous solutions were found to be 11.7, 12.1, and 11.3% (w/w) WPI for pH 7, 8, and 9, respectively. The cooling rate influenced the c(g), in that a lower amount of WPI was needed for gelation when a slower cooling rate was applied. Both cooling rates used in this study showed a maximum in the c(g) at pH 8. The influence of the polymer network on the film properties was elucidated by varying the concentration of WPI over and under the c(g). Strain at break (epsilon(b)) showed a maximum at the c(g) for all pH values, thus implying that the most favorable structure regarding the ability of the films to stretch is formed at this concentration. Young's modulus (E) and stress at break (sigma(b)) showed a maximum at c(g) for pH 7 and 8. The MC and epsilon(b) increased when pH increased from 7 to 9, whereas T(g) decreased. Hence, T(g) values were -17, -18, and -21 degrees C for pH 7, 8, and 9, respectively. E and sigma(b) decreased and epsilon(b) and thickness increased when the surrounding RH increased. The thickness of the WPI films also increased with the concentration of WPI.  相似文献   

13.
Cold gelation of whey proteins is a two-step process. First, protein aggregates are prepared by a heat treatment of a solution of native proteins in the absence of salt. Second, after cooling of the solution, gelation is induced by lowering the pH at ambient temperature. To demonstrate the additional formation of disulfide bonds during this second step, gelation of whey protein aggregates with and without a thiol-blocking treatment was studied. Modification of reactive thiols on the surface of the aggregates was carried out after the heat-treatment step. To exclude specific effects of the agent itself, different thiol-blocking agents were used. Dynamic light scattering and SDS-agarose gel electrophoresis were used to show that the size of the aggregates was not changed by this modification. The kinetics of gelation as determined by the development of pH and turbidity within the first 8 h of acidification were not affected by blocking thiol groups. During gelation, formation of large, covalently linked, aggregates occurred only in the case of unblocked WPI aggregates, which demonstrates that additional disulfide bonds were formed. Results of permeability and confocal scanning laser microscope measurements did not reveal any differences in the microstructure of networks prepared from treated or untreated whey protein aggregates. However, gel hardness was decreased 10-fold in gels prepared from blocked aggregates. Mixing different amounts of blocked and unblocked aggregates allowed gel hardness to be controlled. It is proposed that the initial microstructure of the gels is primarily determined by the acid-induced noncovalent interactions. The additional covalent disulfide bonds formed during gelation are involved in stabilizing the network and increase gel strength.  相似文献   

14.
It was previously reported that water-soluble fish meat can be prepared by the Maillard reaction with reducing monosaccharides. To clarify the molecular mechanism of the solubility improvement caused by the glycosylation, carp myosin and myosin rod region were reacted with glucose and ribose, and their solubilities and filament-forming abilities at low ionic strength were investigated. The solubility of myosin in 0.1 M NaCl increased with the glycosylation and reached the same level as in 0.5 M NaCl. Although the same solubility improvement was observed in glycosylated myosin rod and the alpha-helix content remained unchanged, the filament-forming ability was completely lost by the glycosylation. These results suggest that the solubility improvement of fish meat at low ionic strength is caused by the solubilization of myosin and the dissociation of myosin filaments.  相似文献   

15.
The objective of the present work was to investigate the physicochemical conditions that trigger the self-assembly of peptide β-lg f1-8 and therefore lead to nanofibers and hydrogel formation. Nanostructures formed by self-assembly of peptide β-lg f1-8 in the pH range of 2.0-11.0 were studied by transmission electron microscopy (TEM). Hydrogel formation was studied as a function of pH and resulted in evidence of a link between hydrogel formation and the charge distribution carried by the peptide structure. Finally, circular dichroism (CD) spectroscopy was used to characterize the effects of peptide concentration (0.4-2.0 mg/mL), ionic strength (0-1 M NaCl), and temperature (20-80 °C) on the secondary structure of peptide β-lg f1-8. Hydrogels were obtained at peptide concentrations above 2.5 mg/mL. Peptide concentration and pH adjustment were shown to trigger self-assembly of β-lg f1-8, but increasing ionic strength had no effect. Heating to 80 °C induced a stronger CD signal intensity due to an increase in solubility of the peptide, whereas only slight changes in CD pattern were found upon cooling to 20 °C. Overall, results emphasize the role of particular molecular interactions in β-sheet self-assembly of peptide β-lg f1-8 and pH-dependent electrostatic interactions occurring between β-lg f1-8 units, which can explain its propensity to self-assembly.  相似文献   

16.
Brookfield viscosimetry, Fourier transform infrared spectroscopy, transmission electron microscopy (TEM), and measurements of the texture strength of gels formed with CaCl2 and the mechanical and barrier properties of the film were applied in studies of gel formation and structural and mechanical properties of gels and films prepared using calcium caseinate (CC)-whey protein isolate (WPI)-glycerol (1:1:1), control, and irradiated with 60Co gamma rays using a 32 kGy dose. The irradiated gels have appeared to be more "fine-stranded" as compared to the more "particulate" control gels and lead to the formation of more rigid films with improved mechanical strength and barrier properties. This results from cross-linking and the modification of protein conformations were induced by irradiation, in particular the increase in the beta-sheet and beta-strand contents. Structural modifications taking place in CC-WPI composition are related to modifications taking place separately in CC and WPI. Improvement of the properties of the films after irradiation corresponds to the increased density of the cross-linked material because no change in the porosity of the films was observed by TEM.  相似文献   

17.
高场强超声-加热联用增强大豆分离蛋白冷凝胶凝胶特性   总被引：1，自引：1，他引：0  
为探究高场强超声技术对大豆分离蛋白葡萄糖酸内酯冷凝胶性的影响,该研究将高场强超声技术与加热处理联用,对大豆蛋白进行预处理后形成冷凝胶。采用质构仪、圆二色谱、荧光色谱、扫描电镜、电泳、粒度仪等多种表征手段,比较了2种高场强超声-加热联用工艺对大豆分离蛋白冷凝胶凝胶性的影响,并推测其作用机理。研究发现:与传统加热预处理相比,2种高场强超声-加热联用预处理都能够显著(P0.05)增强大豆分离蛋白冷凝胶的持水性和凝胶强度。工艺一(20 k Hz,400 W下先超声0、2、4、10 min后加热20 min)制备的冷凝胶的凝胶强度与持水性随超声时间的增加逐步增加(凝胶强度由(5.83±0.31)g增加到(46.37±1.15)g;持水性由42.04%±1.59%增加到81.74%±6.22%),而工艺二(先加热20 min后超声0、2、4、10 min)制备的冷凝胶的凝胶强度与持水性在较短超声时间内(4 min内)迅速增加(凝胶强度由(5.83±0.31)g增加到(37.57±2.57)g;持水性由42.03%±1.85%增加到79.31%±3.00%)。与工艺一相比,工艺二能够在较短超声时间内增强大豆分离蛋白冷凝胶性的机理可能在于:工艺二的处理方式,大豆蛋白经过热处理后充分展开、变性,使超声作用能在较短的时间内对大豆分离蛋白的二级结构和三级结构明显改变,暴露更多疏水基团,增加疏水环境和表面疏水性,增强蛋白在溶液中的溶解性,并增强大豆蛋白分子间的静电相互作用,从而形成致密、均一的微观凝胶结构,增加凝胶的持水性和凝胶强度。研究结果可为高场强超声-加热联用技术在大豆加工领域中的应用提供参考。  相似文献   

18.
The influence of sucrose (0-40 wt %) on the thermal denaturation and functionality of whey protein isolate (WPI) solutions has been studied. The effect of sucrose on the heat denaturation of 0.2 wt % WPI solutions (pH 7.0) was measured using differential scanning calorimetry. Sucrose increased the temperature at which protein denaturation occurred, for example, by 6-8 degrees C for 40 wt % sucrose. The dynamic shear rheology of 10 wt % WPI solutions (pH 7.0, 100 mM NaCl) was monitored as they were heated from 30 to 90 degrees C and then cooled to 30 degrees C. Sucrose increased the gelation temperature and the final rigidity of the cooled gels. The degree of flocculation in 10 wt % oil-in-water emulsions stabilized by 1 wt % WPI (pH 7.0, 100 mM NaCl) was measured using a light scattering technique after they were heated at fixed temperatures from 30 to 90 degrees C for 15 min and then cooled to 30 degrees C. Sucrose increased the temperature at which maximum flocculation was observed and increased the extent of droplet flocculation. These results are interpreted in terms of the influence of sucrose on the thermal unfolding and aggregation of protein molecules.  相似文献   

19.
In this paper we present surface dynamic properties (interfacial tension and surface dilational properties) of a whey protein isolate with a high content of beta-lactoglobulin (WPI) adsorbed on the oil-water interface as a function of adsorption time. The experiments were performed at constant temperature (20 degrees C), pH (5), and ionic strength (0.05 M). The surface rheological parameters and the interfacial tension were measured as a function of WPI concentration (ranging from 1 x 10(-)(1) to 1 x 10(-)(5)% w/w) and different processing factors (effect of convection and heat treatment). We found that the interfacial pressure, pi, and surface dilational modulus, E, increase and the phase angle, phi, decreases with time, theta, which should be associated with WPI adsorption. These phenomena have been related to diffusion of the protein toward the interface (at short adsorption time) and to the protein unfolding and/or protein-protein interactions (at long-term adsorption) as a function of protein concentration in solution and processing conditions.  相似文献   

20.
利用电子万能材料试验机对荞麦、玉米、马铃薯淀粉的力学特性进行了研究。结果表明：在一定范围内，随着淀粉乳浓度的增加，荞麦、玉米、马铃薯的凝胶强度、弹性模量和凝胶弹性呈线性增加，但凝胶弹性变化较小；同一淀粉乳浓度下凝胶强度由高到低顺序为马铃薯淀粉＞玉米淀粉＞荞麦淀粉，弹性模量为马铃薯淀粉＞玉米淀粉＞荞麦淀粉，凝胶弹性为荞麦淀粉＞玉米淀粉＞马铃薯淀粉。在淀粉乳浓度为20％时，随着NaCl浓度增加，3种淀粉的凝胶强度均有一定程度增强。在同一NaCl浓度下，其凝胶强度为马铃薯淀粉＞玉米淀粉＞荞麦淀粉，弹性模量为马铃薯淀粉＞玉米淀粉＞荞麦淀粉，对凝胶弹性的影响不大。  相似文献   

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