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1.
Foam properties of a sunflower isolate (SI), as well as those of helianthinin and sunflower albumins (SFAs), were studied at various pH values and ionic strengths and after heat treatment. Less foam could be formed from helianthinin than from SFAs, but foam prepared with helianthinin was more stable against Ostwald ripening and drainage than foam prepared with SFAs. Foams made with SFAs suffered from extensive coalescence. The formation and stability of foams made from reconstituted mixtures of both proteins and from SI showed the deteriorating effect of SFAs on foam stability. Foam stability against Ostwald ripening increased after acid and heat treatment of helianthinin. Partial unfolding of sunflower proteins, resulting in increased structural flexibility, improved protein performance at the air/water interface. Furthermore, it was observed that the protein available is used inefficiently and that typically only approximately 20% of the protein present is incorporated in the foam.  相似文献   

2.
In the present study emulsions were made with various potato protein preparations, which varied in protease inhibitor and patatin content. These emulsions were characterized with respect to average droplet size, plateau surface excess, and the occurrence of droplet aggregation. Droplet aggregation occurred only with potato protein preparations that contained a substantial amount of protease inhibitors and could be prevented only at pH 3. The average droplet size of the emulsions made with potato proteins appeared to be related to the patatin content of the preparation used. Average droplet size was found to be dominated by the patatin-catalyzed lipolytic release of surface active fatty acids and monoglycerides from the tricaprylin oil phase during the emulsification process. Addition of monoglycerides and especially fatty acids, at concentrations representative of those during emulsification, was shown to cause a stronger and much faster decrease of the interfacial tension than that with protein alone and to result in a drastic decrease in droplet size. The patatin used was shown to have a lipolytic activity of 820 units/g with emulsified tricaprylin as the substrate. Because of the droplet aggregating properties of the protease inhibitors, the patatin-rich potato preparations seem to be the most promising for food emulsion applications over a broad pH range, provided the lipolytic activity can be diminished or circumvented.  相似文献   

3.
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   

4.
Whey protein isolate was modified by ethylene diamine in order to shift its isoelectric point to an alkaline pH. The extent of the modification was studied using SDS-PAGE and MALDI-TOF mass spectrometry. The modified whey proteins were used as an emulsifier to stabilize oil-in-water emulsions at acidic and neutral pH ranges, and their emulsifying properties were compared with that of the unmodified whey proteins and with the previously studied ethylene diamine modified sodium caseinate. The emulsifying activity of the modified whey proteins was similar to that of the unmodified ones, but the stability of an emulsion at pH 5 was significantly improved after the modification. Charge and coverage of droplet surface and the displacement of the interfacial proteins by surfactant Tween 20 were further studied as a function of pH. As compared with the unmodified whey proteins, the modified ones were proven to cover the interface more efficiently with extensive surface charge at pH 5, although the interfacial layer was less resistant to the surfactant displacement.  相似文献   

5.
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   

6.
High-pressure treatment represents a potential method to stabilize microbiologically agricultural raw materials that are sensitive to heat treatments. Low-density lipoproteins (LDL), the main contributors to the exceptional emulsifying properties of yolk, are particularly sensitive to heat treatment. In this study, high-pressure treatments have been performed on LDL, and their impact on LDL physicochemical and emulsifying properties has been assessed. LDL dispersions at two pH levels (pH 3 and 8) were treated at different pressure levels: 200, 400, and 600 MPa at 20 degrees C. LDL dispersion characteristics (solubility, aggregation, and protein denaturation) and LDL emulsifying properties (o/w 30:70 emulsions: droplet size, flocculation, and protein adsorption) of nontreated and high-pressure treated dispersions were compared. Solubility is not altered by high-pressure treatment whatever the pH, whereas aggregation and protein denaturation are drastically enhanced, in particular at pH 8. The effects of these modifications on LDL emulsifying properties are mainly a diminution of the flocculation (depletion and bridging) at this same pH. Finally, it seems that high-pressure treatment combined with an alkaline pH decreases droplet flocculation of LDL dispersions.  相似文献   

7.
The disulfide bonds of beta-lactoglobulin (beta-lg) were modified by oxidative sulfitolysis to generate beta-lgSO(3). The native protein (beta-lg) and the modified protein (beta-lgSO(3)) were conjugated to activated polyethylene glycol (PEG) to generate beta-lgPEG and beta-lgSO(3)PEG, respectively. Oil-in-water (o/w) emulsions containing 1% beta-lg or beta-lg conjugates were prepared at pH 2.8, 5.0, and 7.0. Emulsion droplet diameters and zeta potentials were measured. For the same emulsifier, emulsion droplet diameters decreased when emulsion pH increased. Zeta potentials of emulsion droplets increased with pH for beta-lg and beta-lgSO(3). Zeta potentials of beta-lgPEG and beta-lgSO(3)PEG approached zero, suggesting that the protein molecule was covered by PEG chains. Accelerated and 7-day storage stabilities at 21 degrees C of the emulsions were monitored. The emulsifying activity index (EAI) of beta-lgPEG was not significantly different from the EAI of beta-lg. The EAI of beta-lg was enhanced following sulfitolysis of beta-lactoglobulin. The emulsifying activity increased more when the oxidatively modified protein was conjugated to polyethylene glycol. Emulsions made with beta-lgSO(3)PEG were more stable than emulsions made with beta-lg, beta-lgPEG, or beta-lgSO(3) under accelerated stability study and for 7 days at 21 degrees C. The stability of o/w emulsions stabilized with beta-lgSO(3)PEG increased because individual droplets were better protected, against protein bridging or coalescence, by the thick adsorbed protein-PEG layer.  相似文献   

8.
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was investigated as a function of pH and temperature. Dissociation of the 11S form (hexamer) into the 7S form (trimer) gradually increased with increasing pH from 5.8 to 9.0. High ionic strength (I = 250 mM) stabilizes the 11S form at pH > 7.0. Heating and low pH resulted in dissociation into the monomeric constituents (2-3S). Next, the 7S and 11S forms of helianthinin were isolated and shown to differ in their secondary and tertiary structure, and to have denaturation temperatures (T(d)) of 65 and 90 degrees C, respectively. Furthermore, the existence of two populations of the monomeric form of helianthinin with denaturation temperatures of 65 and 90 degrees C was described. This leads to the hypothesis that helianthinin can adopt two different conformational states: one with T(d) = 65 degrees C and a second with T(d) = 90 degrees C.  相似文献   

9.
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   

10.
Proteins often stabilize food emulsions and are also able to promote or delay lipid oxidation in complex systems. The purpose of this work was to investigate the relationship between metal ion availability and oxidative stability of oil-in-water emulsions stabilized by bovine serum albumin (BSA) or sodium caseinate (NaCas). Emulsions with similar and stable droplet size distributions were prepared with stripped sunflower oil (30 vol %) and protein solutions (20 g L(-)(1); pH = 6.5). In the absence of the water-soluble metal chelator EDTA, oxygen uptake, conjugated dienes, and volatile compounds developed faster in NaCas-stabilized emulsions than in those prepared with BSA. This effect is attributed to the chelating properties of NaCas and to electrostatic interactions that attract some metal ions at the interface where they could initiate lipid oxidation. When EDTA (100 muM) was present, oxidation was delayed to a greater extent in emulsions made with NaCas than in BSA stabilized emulsions. These conditions probably enabled NaCas to exert free-radical-scavenging activity.  相似文献   

11.
The objective of this study was to examine the effects of added xanthan gum, guar gum, or kappa-carrageenan on the formation and properties of emulsions (4 wt % corn oil) formed with an extensively hydrolyzed commercial whey protein (WPH) product under a range of conditions. The rate of coalescence was calculated on the basis of the changes in the droplet size of emulsions during storage of the emulsions at 20 degrees C. Compared with the emulsion made without the addition of polysaccharides, the rate of creaming and coalescence in emulsions containing xanthan gum, guar gum, or kappa-carrageenan was markedly enhanced with increasing concentration of polysaccharides during storage for up to 7 days. At a given concentration, the rate of coalescence was highest in the emulsions containing guar gum, whereas it was lowest in the emulsions containing kappa-carrageenan. All emulsions containing xanthan gum, guar gum, or kappa-carrageenan showed flocculation of oil droplets by a depletion mechanism. This flocculation was considered to enhance the coalescence of oil droplets. The different rates of coalescence could be explained on the basis of the strength of the depletion potential, which was dependent on the molecular weight and the radius of gyration of the polysaccharides.  相似文献   

12.
Sunflower protein isolates and the proteases pepsin and pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Hydrolysates obtained after 3 h of incubation with pepsin and 3 h with pancreatin were studied. An ACE inhibitory peptide with the sequence Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser was obtained by G-50 gel filtration chromatography and high-performance liquid chromatography C18 reverse phase chromatography. This peptide corresponds to a fragment of helianthinin, the 11S globulin from sunflower seeds, which is the main storage protein in sunflower. These results show that sunflower seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with pepsin and pancreatin.  相似文献   

13.
The purpose of this research was to better understand the mechanisms by which proteins affect the rates of lipid oxidation in order to develop protein-stabilized emulsion delivery systems with maximal oxidative stability. This study evaluated the affect of pH and emulsifier concentration on the stability of cumene hydroperoxide in hexadecane-in-water emulsions stabilized by beta-lactoglobulin (beta-Lg). Emulsions prepared with 0.2 wt % beta-Lg (at pH 7.0) showed a 26.9% decrease in hydroperoxide concentrations 5 min after 0.25 mM ferrous ion was added to the emulsion. EDTA, but not continuous phase beta-Lg, could inhibit iron-promoted lipid hydroperoxide decomposition. Lipid hydroperoxides were more stable to iron-promoted degradation at pH values below the pI of beta-Lg, where the emulsion droplet would be cationic and thus able to repel iron away from the lipid hydroperoxides. Heating the beta-Lg-stabilized emulsions to produce a cohesive protein layer on the emulsion droplet surface did not alter the ability of iron to decompose lipid hydroperoxides. These results suggest that proteins at the interface of emulsion droplets primarily stabilize lipid hydroperoxides by electrostatically inhibiting iron-hydroperoxide interactions.  相似文献   

14.
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   

15.
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   

16.
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   

17.
Measurement of the intensity (I(MAX)) and/or wavelength (lambda(MAX)) of the maximum in the tryptophan (TRP) emission spectrum using front-face fluorescence spectroscopy (FFFS) can be used to provide information about the molecular environment of proteins in nondiluted emulsions. Many protein-stabilized emulsions in the food industry are flocculated, and therefore, we examined the influence of droplet flocculation on FFFS. Stock oil-in-water emulsions stabilized by bovine serum albumin were prepared by high-pressure valve homogenization (30 wt % n-hexadecane, 0.35 wt % BSA, pH 7). These emulsions were used to create model systems with different degrees of droplet flocculation, either by changing the pH, adding surfactant, or adding xanthan. Emulsions (21 wt % n-hexadecane, 0.22 wt % BSA) with different pH (5 and 7) and molar ratios of Tween 20 to BSA (R = 0-131) were prepared by dilution of the stock emulsion. As the surfactant concentration was increased, the protein was displaced from the droplet surfaces, which caused an increase in both I(MAX) and lambda(MAX), because of the change in TRP environment. The dependence of I(MAX) and lambda(MAX) on surfactant concentration followed a similar pattern in emulsions that were initially flocculated (pH 5) and nonflocculated (pH 7). Relatively small changes in FFFS emission spectra were observed in emulsions (21 wt % n-hexadecane, 0.22 wt % BSA, pH 7) with different levels of depletion flocculation induced by adding xanthan. These results suggested that droplet flocculation did not have a major impact on FFFS. This study shows that FFFS is a powerful technique for nondestructively providing information about the molecular environment of proteins in concentrated and flocculated protein-stabilized emulsions. Nevertheless, in general the suitability of the technique may also depend on protein type and the nature of the physicochemical matrix surrounding the proteins.  相似文献   

18.
Water soluble plasma proteins were fractionated from hen's egg yolk, and the molecular weight and pI of the most abundant protein species were characterized with gel electrophoresis. The proteins were identified by mass spectrometry. The protein fraction was used to produce oil-in-water emulsions, both at various protein concentrations and at various pH values, and the surface load was determined through serum depletion. The competitive adsorption was studied through the determination of nonadsorbing species with gel electrophoresis. The results show that it was possible to form an oil-in-water emulsion for which droplet size and maximum surface load depended on the protein concentration and pH. Serum albumin and YGP40 adsorbed selectively at the oil/water interface throughout the pH range investigated, and for albumin the selectivity increased close to its pI. It is suggested that this selective adsorption is due to long hydrophobic stretches in the polypeptide chain, which are present in the selectively adsorbing species but absent in less adsorbing species.  相似文献   

19.
Transglutaminase-catalyzed cross-linking of interfacial proteins in oil-in-water has been shown to influence physical stability, but little is known about how this reaction impacts lipid oxidation. Therefore, this study evaluated the influence of transglutaminase-induced interfacial protein cross-linking on the oxidative stability of casein-stabilized menhaden oil-in-water emulsions. Interfacial casein in menhaden oil-in-water emulsions cross-linked by transglutaminase (pH 7.0) produced a cohesive interfacial protein layer that could not be removed from the emulsion droplet by Tween 20. Although transglutaminase cross-linked the interfacial casein, these emulsions did not show increased oxidative stability when compared to untreated emulsions as determined by measurement of lipid hydroperoxides and thiobarbituric acid reactive substances. These results indicate that increasing the cohesiveness of proteins at the interface of oil-in-water emulsions does not inhibit lipid oxidation. This could be due to the ability of prooxidative species such as iron to diffuse through the cross-linked protein layer where it could promote the decomposition of lipid hydroperoxides into free radicals that could oxidize unsaturated fatty acids in the emulsion droplet core.  相似文献   

20.
Casein and whey protein were hydrolyzed using 11 different commercially available enzyme preparations. Emulsion-forming ability and emulsion stability of the digests were measured as well as biochemical properties with the objective to study the relations between hydrolysate characteristics and emulsion properties. All whey protein hydrolysates formed emulsions with bimodal droplet size distributions, signifying poor emulsion-forming ability. Emulsion-forming ability of some casein hydrolysates was comparable to that of intact casein. Emulsion instability was caused by creaming and coalescence. Creaming occurred mainly in whey hydrolysate emulsions and in casein hydrolysate emulsions containing large emulsion droplets. Coalescence was dominant in casein emulsions with a broad particle size distribution. Emulsion instability due to coalescence was related to apparent molecular weight distribution of hydrolysates; a relative high amount of peptides larger than 2 kDa positively influences emulsion stability.  相似文献   

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