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1.
In this study, the impact of mechanical treatments on the physicochemical and emulsifying properties of hen egg yolk and its fractions plasma and granules has been assessed. Yolk, plasma, and granule dispersions at pH 4.0 and 0.75 M NaCl were subjected to rotor-stator and high-pressure pretreatments at different dynamic pressure levels: 30, 100, and 200 bar at 20 degrees C. Physicochemical characteristics (protein solubility, rheological behavior, and micro- and ultra-structures) and emulsifying properties (oil/water 60:40 emulsions: droplet size and flocculation, protein adsorption) of control dispersions and dispersions subjected to mechanical pretreatments (rotor-stator or high pressure) were compared. Homogenization at high pressures (100 and 200 bar) led to a decreased protein solubility and to an increase in apparent viscosity of yolk and plasma dispersions. These pressures certainly disrupted low-density lipoproteins (LDL) particles and generated aggregates of proteins liberated from LDL and livetins in the plasma fraction, and led to a moderated reorganization of the microstructure of granules. Despite the modifications observed in the pretreated plasma and granules dispersions, the oil droplet diameter and the bridging flocculation obtained in emulsions made with these dispersions were similar to that obtained with untreated dispersions. Results concerning interfacial protein adsorption suggested that preformed or natural aggregates at least partially persist at the oil-water interface.  相似文献   

2.
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   

3.
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   

4.
The influence of sucrose on the flocculation stability of hydrocarbon oil-in-water emulsions stabilized by a globular protein was examined using laser diffraction. Salt (150 mM NaCl) and sucrose (0-40 wt %) were added to n-hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin (beta-Lg, pH 7.0) either before or after isothermal heat treatment (30-95 degrees C for 20 min). When salt was added to emulsions before heat treatment, appreciable droplet flocculation was observed below the thermal denaturation temperature of the adsorbed beta-Lg (T(m) approximately 70 degrees C), and more extensive flocculation was observed above T(m). On the other hand, when salt was added to emulsions after heat treatment, appreciable droplet flocculation still occurred below T(m), but little flocculation was observed above T(m). Addition of sucrose to the emulsions increased T(m) and either promoted or suppressed droplet flocculation depending on whether it was added before or after heat treatment. These results are interpreted in terms of the influence of sucrose on protein conformational stability, protein-protein interactions, and the physiochemical properties of aqueous solutions. This study has important implications for the formulation and production of protein stabilized oil-in-water emulsions.  相似文献   

5.
The influence of globular protein denaturation after adsorption to the surface of hydrocarbon droplets on flocculation in oil-in-water emulsions was examined. n-Hexadecane oil-in-water emulsions (pH 7.0) stabilized by beta-lactoglobulin (1-wt % beta-Lg) were prepared by high-pressure valve homogenization. NaCl (0-150 mM) was added to these emulsions immediately after homogenization, and the evolution of the mean particle diameter (d) and particle size distribution (PSD) was measured by laser diffraction during storage at 30 degrees C for 48 h. No change in d or PSD was observed in the absence of added salt, which indicated that these emulsions were stable to flocculation. When 150 mM NaCl was added to emulsions immediately after homogenization, d increased rapidly during the following few hours until it reached a plateau value, while the PSD changed from monomodal to bimodal. Addition of N-ethylmaleimide, a sulfhydryl blocking agent, to the emulsions immediately after homogenization prevented (at 20 mM NaCl) or appreciably retarded (at 150 mM NaCl) droplet flocculation. These data suggests that protein unfolding occurred at the droplet interface, which increased the hydrophobic attraction and disulfide bond formation between droplets. In the absence of added salt, the electrostatic repulsion between droplets was sufficient to prevent flocculation, but in the presence of sufficient salt, the attractive interactions dominated, and flocculation occurred.  相似文献   

6.
Emulsions were made with sunflower protein isolate (SI), helianthinin, and sunflower albumins (SFAs). Emulsion formation and stabilization were studied as a function of pH and ionic strength and after heat treatment of the proteins. The emulsions were characterized with respect to average droplet size, surface excess, and the occurrence of coalescence and/or droplet aggregation. Sunflower proteins were shown to form stable emulsions, with the exception of SFAs at neutral and alkaline pH values. Droplet aggregation occurred in emulsions made with SI, helianthinin, and SFAs. Droplet aggregation and subsequent coalescence of emulsions made with SFAs could be prevented at pH 3. Calcium was found to cause droplet aggregation of emulsions made with helianthinin, at neutral and alkaline pH values. Treatments that increase conformational flexibility of the protein molecule improved the emulsion properties of sunflower proteins.  相似文献   

7.
Protein fractions were isolated from coconut: coconut skim milk protein isolate (CSPI) and coconut skim milk protein concentrate (CSPC). The ability of these proteins to form and stabilize oil-in-water emulsions was compared with that of whey protein isolate (WPI). The solubility of the proteins in CSPI, CSPC, and WPI was determined in aqueous solutions containing 0, 100, and 200 mM NaCl from pH 3 to 8. In the absence of salt, the minimum protein solubility occurred between pH 4 and 5 for CSPI and CSPC and around pH 5 for WPI. In the presence of salt (100 and 200 mM NaCl), all proteins had a higher solubility than in distilled water. Corn oil-in-water emulsions (10 wt %) with relatively small droplet diameters (d32 approximately 0.46, 1.0, and 0.5 mum for CSPI, CSPC, and WPI, respectively) could be produced using 0.2 wt % protein fraction. Emulsions were prepared with different pH values (3-8), salt concentrations (0-500 mM NaCl), and thermal treatments (30-90 degrees C for 30 min), and the mean particle diameter, particle size distribution, zeta-potential, and creaming stability were measured. Considerable droplet flocculation occurred in the emulsions near the isoelectric point of the proteins: CSPI, pH approximately 4.0; CSPC, pH approximately 4.5; WPI, pH approximately 4.8. Emulsions with monomodal particle size distributions, small mean droplet diameters, and good creaming stability could be produced at pH 7 for CSPI and WPI, whereas CSPC produced bimodal distributions. The CSPI and WPI emulsions remained relatively stable to droplet aggregation and creaming at NaCl concentrations of < or =50 and < or =100 mM, respectively. In the absence salt, the CSPI and WPI emulsions were also stable to thermal treatments at < or =80 and < or =90 degrees C for 30 min, respectively. These results suggest that CSPI may be suitable for use as an emulsifier in the food industry.  相似文献   

8.
The ability of alphas1/beta-casein and micellar casein to protect whey proteins from heat-induced aggregation/precipitation reactions and therefore control their functional behavior was examined. Complete suppression (>99%) of heat-induced aggregation of 0.5% (w/w) whey protein isolate (pH 6.0, 85 degrees C, 10 min) was achieved at a ratio of 1:0.1 (w/w) of whey protein isolate (WPI) to alphas1/beta-casein, giving an effective molar ratio of 1:0.15, at 50% whey protein denaturation. However, in the presence of 100 mM NaCl, heating of the WPI/alphas1/beta-casein dispersions to 85 degrees C for 10 min resulted in precipitation between pH 6 and 5.35. WPI heated with micellar casein in simulated milk ultrafiltrate was stable to precipitation at pH>5.4. Protein particle size and turbidity significantly (P相似文献   

9.
The emulsifying ability, heat stability, and coalescence stability of oil-in-water emulsions prepared with whey protein of varied degrees of hydrolysis (DH), and at varied protein contents, was studied. Whey protein hydrolysates (WPH) with a DH of 4% and 10% had poorer emulsifying ability than non-hydrolyzed whey protein concentrate (WPC), but were more heat stable. Increasing DH between 10 and 27% improved emulsifying ability and further improved the heat stability of the emulsion droplets. Increasing DH from 27 to 35% led to a big decrease in both emulsifying ability and heat stability. The quiescent coalescence stability of WPH emulsions was relatively good up to a DH of 27%. Above DH 27% emulsions become highly unstable. It appears that two mechanisms of instability are at work here. At low DH heat-induced denaturation and aggregation occur. In the DH range of 4-20% heat stability increases as protein globular structure is disrupted. At a DH greater than 27% we see a change from a hydrolysis-induced increase in heat-stability to coalescence instability, with a resultant large increase in emulsion breakdown during heating.  相似文献   

10.
The influence of pH and iota-carrageenan concentration on the properties of beta-lactoglobulin (beta-Lg)-stabilized oil-in-water emulsions was investigated by measuring the particle charge, particle size distribution, and creaming stability. Emulsions containing droplets stabilized by beta-Lg were produced by homogenization, and then, iota-carrageenan was added. At pH 3, the droplet charge did not change for iota-carrageenan concentrations 相似文献   

11.
The stability of emulsions prepared with soy protein isolates was investigated as a function of pH in the presence of two negatively charged polysaccharides: high methoxyl pectin (HMP) and soy soluble polysaccharide (SSPS). Both polysaccharides are composed of a backbone which contains galacturonic acid but, when added to soy protein isolate-stabilized emulsions, SSPS showed a different behavior than that of HMP. At neutral pH and above a critical concentration of stabilizer (0.05%), HMP caused flocculation of the emulsion droplets via a depletion mechanism. On the other hand, the emulsions containing a similar amount of SSPS did not show creaming or flocculation. At acidic pH (<4.0) the addition of pectin caused extensive droplet aggregation, while no aggregation was observed with the addition of SSPS. The differences in the stabilization behavior between the two polysaccharides can be attributed to their differences in charge, neutral sugars side chains, and molecular weight.  相似文献   

12.
Functional properties of whey protein concentrates (WPC) are primarily dependent on the degree of denaturation of beta-lactoglobulin (beta-LG), the major globular whey protein. Irreversible modifications in the tertiary structure and association state of beta-LG after heat treatment were studied by partition in aqueous two-phase systems and fluorescence quenching. Partitioning of preheated beta-LG in two-phase systems containing 5% (w/w) poly(ethylene glycol) and 7% (w/w) dextran, between pH 6.0 and7.0, are appropriately related with the intensity of heat treatment. An increase in the partition coefficient of beta-LG was observed with increasing temperature of heat treatment. On the other hand, fluorescence quenching of beta-LG by acrylamide was used to study the conformational flexibility of the protein at pH values between 4. 0 and 9.0. The values of bimolecular quenching rate constant (k(q)) obtained showed that beta-LG appears to be more flexible at high pH values, while at low pH the protein assumes a more compact form. The efficiency of acrylamide quenching on preheated beta-LG was substantially more pronounced than for the untreated protein. This difference can be ascribed to the presence of unfolded monomers and aggregates of denatured molecules formed after heat treatment, whose tryptophanyl residues are more exposed to the solvent. In conclusion, the results suggest that partition studies in aqueous two-phase systems and fluorescence quenching are very useful tools to detect changes in conformation and aggregation of beta-LG induced by heat treatment.  相似文献   

13.
The effect of high-pressure treatment (HPT) on the droplet-size distribution and small-deformation rheology of oil-in-water emulsions containing beta-lactoglobulin and a nonionic surfactant or sodium caseinate has been investigated at neutral pH. Addition of Tween 20 (polyoxyethylenesorbitan monolaurate) to a beta-lactoglobulin-stabilized emulsion results in competitive displacement of the adsorbed globular protein film and, following HPT, the formation of a less flocculated emulsion. The age of the beta-lactoglobulin-stabilized emulsion prior to addition of sodium caseinate influences the competitive adsorption behavior. The strengthening of the beta-lactoglobulin layer with time makes it more resistant to disruption by sodium caseinate. The level of pressure-induced flocculation of beta-lactoglobulin-coated oil droplets depends on the intensity of processing conditions and on the degree of interfacial displacement. In contrast, beta-lactoglobulin added after emulsification appears to show little evidence of competitive adsorption behavior at the caseinate oil-water interface. Changes in the rheological properties of these latter systems following HPT can be attributed to pressure-induced denaturation and gelation of beta-lactoglobulin in the continuous phase of the emulsion.  相似文献   

14.
Changes induced by high pressure (HP) treatment (200-600 MPa) on soybean protein isolates (SPI) at pH 3 (SPI3) and pH 8 (SPI8) were analyzed. Changes in protein solubility, surface hydrophobicity (Ho), and free sulfhydryl content (SH(F)) were determined. Protein aggregation and denaturation and changes in secondary structure were also studied. An increase in protein Ho and aggregation, a reduction of free SH, and a partial unfolding of 7S and 11S fractions were observed in HP-treated SPI8. Changes in secondary structure were also detected, which led to a more disordered structure. HP-treated SPI3 was partially denatured and presented insoluble aggregates. A major molecular unfolding, a decrease of thermal stability, and an increase of protein solubility and Ho were also detected. At 400 and 600 MPa, a decrease of the SH(F) and a total denaturation were observed.  相似文献   

15.
Changes in physicochemical properties of egg yolk were investigated after a treatment with phospholipase A 2 (PLA 2), where phospholipids are converted in lyso-phospholipids. Protein solubility and protein denaturation before and after modification by PLA 2 was monitored as well as the functionality of egg yolk by means of interfacial tension. Enzymatic treatment showed a significant impact on the properties of egg yolk with regard to protein solubility and denaturation behavior. To gain a closer insight, egg yolk was separated in its water-soluble fraction called plasma and the insoluble granules. Both fractions were separately modified by PLA 2. The granule fraction shows a higher protein solubility, and the plasma proteins show very high heat stability after modification by PLA 2. Hypotheses regarding related changes in the low-density lipoprotein (LDL) particles are discussed. Results suggest that significant differences in the functional properties of untreated and PLA 2-modified egg yolk do not primarily result from the existence of lyso-phospholipids but from structural changes in egg yolk granules and LDL particles.  相似文献   

16.
The ability of two protein fractions extracted from cod to form and stabilize oil-in-water emulsions was examined: a high salt extracted fraction (HSE protein) and a pH 3 acid extracted fraction (AE protein). Both fractions consisted of a complex mixture of different proteins, with the predominant one being myosin (200 kDa). The two protein fractions were used to prepare 5 wt % corn oil-in-water emulsions at ambient temperature (pH 3.0, 10 mM citrate-imidazole buffer). Emulsions with relatively small mean droplet diameters (d(3,2) < 1 microm) and good creaming stability (> 9 days) could be produced at protein concentrations > or =0.2 wt % for both fractions. The isoelectric point of droplets stabilized by both protein fractions was pH approximately 5. The emulsions were stable to droplet flocculation and creaming at relatively low pH (< or =4) and NaCl concentrations (< or =150 mM) when stored at room temperature. In the absence of salt, the emulsions were also stable to thermal treatment (30-90 degrees C for 30 min), but in the presence of 100 mM NaCl droplet flocculation and creaming were observed in some of the emulsions, particularly those stabilized by the AE fraction. The results suggest that protein fractions extracted from cod can be used as emulsifiers to form and stabilize food emulsions.  相似文献   

17.
Helianthinin, the main storage protein of sunflowers, has low water solubility and does not form a gel when heated; this behavior is different from other 11S globulins and limits its food applications. To understand this particular behavior, changes on helianthinin association-dissociation state induced by modifications in pH and ionic strength were analyzed. The influence of these different medium conditions on its thermal stability and tendency to form aggregates was also studied. Helianthinin behavior at different pH values and ionic strengths is similar to other 11S globulins except that it remains in a trimeric form at pH 11. Helianthinin thermal stability is higher than other 11S globulins but is lower than oat 11S globulin. Alkaline pH produces a 10 degrees C decrease of its denaturation temperature and also of the cooperativity of denaturation process, but it does not affect the denaturation activation energy. The decrease in thermal stability with the pH increase is also manifested by its tendency to form aggregates by SH/SS interchange reactions. When thermal treatments at alkaline pH are performed, all helianthinin subunits form aggregates, characterized by a higher proportion of beta-polypeptides than alpha-polypeptides, which is an indication that aggregation is accompanied by dissociation. Treatments at 80 degrees C are sufficient to induce aggregation but not to produce denaturation, and in these conditions hexameric forms remain after the treatment.  相似文献   

18.
Interfacial and emulsifying properties of potato protein isolate (PPI) have been studied to evaluate its potential application to stabilize oil/water emulsions at two pH values (2 and 8). The amount, type, and solubility of proteins and the size of aggregates have been determined in aqueous dispersion. Air-water and oil-water interfacial properties (adsorption, spreading, and viscoelastic properties) have been determined as a function of concentration and pH using soluble phases of PPI. The behavior of PPI stabilized oil/water emulsions has been then analyzed by droplet size distribution measurements and interfacial concentration. PPI exhibits low solubility over a wide range of pH values, with the presence of submicrometer aggregates. The pH value exerts a negligible effect on interfacial tension (oil-water) or surface pressure (air-water) but displays very important differences in viscoelastic properties of the interfacial films formed between oil and water. In this sense, pH 8 provides a major elastic response at oil-water interfaces as compared to pH 2. In relation with this result, a much higher ability to produce fine and stable emulsions is noticed at pH 8 as compared to pH 2. Consequently, there is an evident relationship between the rheological properties of the oil-water interfacial films and the macroscopic emulsion behavior.  相似文献   

19.
Proteins isolated from blue-green algae Spirulina platensis strain Pacifica were characterized by visible absorption, differential scanning calorimetry (DSC), viscometry, and dynamic oscillatory rheological measurements. Unique thermal unfolding, denaturation, aggregation, and gelation of the algal protein isolate are presented. DSC analysis showed that thermal transitions occur at about 67 and 109 degrees C at neutral pH. Calcium chloride stabilized the quaternary structure against denaturation and shifted the transitions at higher temperatures. Viscometric studies of Spirulina protein isolate as a function of temperature showed that the onset of the viscosity increase is closely related to the dissociation-denaturation process. Lower viscosities were observed for the protein solutions dissolved at pH 9 due to an increased protein solubility. Solutions of Spirulina protein isolate form elastic gels during heating to 90 degrees C. Subsequent cooling at ambient temperatures caused a further pronounced increase in the elastic moduli and network elasticity. Spirulina protein isolate has good gelling properties with fairly low minimum critical gelling concentrations of about 1.5 and 2.5 wt % in 0.1 M Tris buffer, pH 7, and with 0.02 M CaCl(2) in the same buffer, respectively. It is suggested that mainly the interactions of exposed hydrophobic regions generate the molecular association, initial aggregation, and gelation of the protein isolate during the thermal treatment. Hydrogen bonds reinforce the network rigidity of the protein on cooling and further stabilize the structure of Spirulina protein gels but alone are not sufficient to form a network structure. Intermolecular sulfhydryl and disulfide bonds were found to play a minor role for the network strength of Spirulina protein gels but affect the elasticity of the structures formed. Both time and temperature at isothermal heat-induced gelation within 40-80 degrees C affect substantially the network formation and the development of elastic modulus of Spirulina protein gels. This is also attributed to the strong temperature dependence of hydrophobic interactions. The aggregation, denaturation, and gelation properties of Spirulina algal protein isolate are likely to be controlled from protein-protein complexes rather than individual protein molecules.  相似文献   

20.
The amino acid composition and physicochemical and functional properties of hemp (Cannabis sativa L.) protein isolate (HPI) were evaluated and compared with those of soy protein isolate (SPI). Edestin, a kind of hexameric legumin, was the major protein component. HPI had similar or higher levels of essential amino acids (except lysine), in comparison to those amino acids of SPI. The essential amino acids in HPI (except lysine and sulfur-containing amino acids) are sufficient for the FAO/WHO suggested requirements for 2-5 year old children. The protein solubility (PS) of HPI was lower than that of SPI at pH less than 8.0 but similar at above pH 8.0. HPI contained much higher free sulfhydryl (SH) content than SPI. Differential scanning calorimetry analysis showed that HPI had only one endothermic peak with denaturation temperature (T(d)) of about 95.0 degrees C, attributed to the edestin component. The T(d) of the endotherm was nearly unaffected by 20-40 mM sodium dodecyl sulfate but significantly decreased by 20 mM dithiothreitol (P < 0.05). The emulsifying activity index, emulsion stability index, and water-holding capacity of HPI were much lower than those of SPI, and the fat adsorption capacity was similar. The data suggest that HPI can be used as a valuable source of nutrition for infants and children but has poor functional properties when compared with SPI. The poor functional properties of HPI have been largely attributed to the formation of covalent disulfide bonds between individual proteins and subsequent aggregation at neutral or acidic pH, due to its high free sulfhydryl content from sulfur-containing amino acids.  相似文献   

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