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Comparison of Gum Arabic, Modified Starch, and Whey Protein Isolate as Emulsifiers: Influence of pH, CaCl2 and Temperature

R. CHANAMAI AND D.J. MCCLEMENTS

Food Chemistry and Toxicology

ABSTRACT: The particle size and zeta potential of model beverage emulsions (0.01 wt% soybean oil-in-water emulsions, d 1 mm) stabilized by gum arabic, modified starch, or whey protein isolate (WPI) were studied with varying pH (3 to 9), CaCl2 concentration (0 to 25 mM), and temperature (30 C to 90 C). Temperature, pH, CaCl2 strongly influenced emulsions stabilized by WPI because its stabilizing mechanism was mainly electrostatic repulsion, but not those stabilized by gum arabic or modified starch because their stabilizing modes of action were mainly steric repulsion. This study may have important implications for the application of WPI as an emulsifier in beverage emulsions. Keywords: emulsions, stability, whey protein, gum arabic, modified starch

Introduction

EVERAGE EMULSIONS ARE OIL - IN -WATER EMULSIONS THAT

are normally prepared as a concentrate that is diluted into finished products (Tan 1997, 1998). The oil phase usually consists of vegetable oil, flavor oil, and a weighting agent, while the aqueous phase consists of water, sugar, emulsifier, acids, and preservatives (Tan 1997). This unique class of emulsions must have a high degree of stability in both the concentrated and the diluted form. Beverage emulsions are usually stabilized by amphiphilic polysaccharides, such as gum arabic or hydrophobically modified starch (Ray and others 1995; Trubiano 1995; Kim and others 1996; McNamee and others 1998; Garti 1999). Gum arabic is the most commonly used biopolymer emulsifier in flavor beverage emulsions (Tan 1997, 1998). It is derived from the natural bark exudate of Acacia senegal and consists of at least 3 high-molecular-weight biopolymer fractions. The surface-active fraction is believed to consist of branched arabinogalactan blocks attached to a polypeptide backbone (Anderson and others 1985; Phillips and Williams 1995; Jayme and others 1999). The hydrophobic polypeptide chain is believed to anchor the molecules to the droplet surface, while the hydrophilic arabinogalactan blocks extend into the solution, providing stability against droplet aggregation through steric and electrostatic repulsion (Phillips and Williams 1995; Islam and others 1997; Jayme and others 1999). Gum arabic is an effective emulsifier because of its high water solubility, low solution viscosity, good surface activity, and ability to form a protective film around emulsion droplets (Glicksman 1983). However, the relatively high cost, large quantity required, and problems associated with obtaining a reliable source of consistently high-quality gum arabic have led many food scientists to investigate alternative sources of biopolymer emulsifiers for use in flavor beverages (Kim and others 1996; Tan 1997, 1998; Garti 1999). Hydrophobically modified starches have been identified as one of the most promising replacements for gum arabic (Trubiano 1995). The modified starch used in this study (Purity Gum BE; National Starch, Bridgewater, N.J., U.S.A.) is an octenyl

succinate derivative of waxy maize. It consists primarily of amylopectin that has been chemically modified to contain nonpolar side groups. These side groups anchor the molecule to the droplet surface, while the hydrophilic starch chains protrude into the aqueous phase and protect droplets against aggregation through steric repulsion. Previous studies have indicated that modified starch is mildly anionic in aqueous solutions and has a surface activity that is almost as high as that of gum arabic (Ray and others 1983; Tse 1990). A wide variety of proteins are also used as emulsifiers in foods because they naturally have a high proportion of nonpolar groups and are therefore surface-active (Dickinson 1992; Damodaran 1996). Whey protein is one of the emulsifiers frequently used in foods because of its ability to facilitate the formation and stabilization of oil-in-water emulsions (Phillips and others 1994; Huffman 1996; Dickinson 1997; McClements 1999). The ability of whey protein to form stable emulsions depends on emulsion composition (including pH and mineral content, salt, sugar, surfactant, and polysaccharide contents) and environmental conditions (temperature and pressure) (Dickinson and Stainsby 1982; Kinsella 1984; Kinsella and Phillips 1989; Mangino 1989; Dickinson 1992; Dalgleish 1996; Dematriades and others 1997a, 1997b; Kulmyrzaev and others 2000; Singh and Ye 2000). Whey proteins are therefore suitable for application in food emulsions where the composition and environmental conditions favor a stable product, but not in those products where the conditions promote emulsion instability. Beverage emulsions may have a variety of different compositions and experience a variety of environmental conditions during their storage, transport, and consumption. It is therefore important for manufacturers of these products to understand the influence of these factors on emulsion stability. In this study, we examined the influence of pH, calcium ion concentration, and temperature on the stability of dilute emulsion stabilized with different types of biopolymer emulsifiers: gum arabic, modified starch, and whey protein isolate. Ultimately, we aim to determine whether whey protein can be used as a suitable alternative to polysaccharide-based

Comparison of emulsifier types . . .

Figure 1Droplet size distribution of emulsions measured by light scattering.

Figure 2Mean droplet size (d32) of emulsions stabilized by WPI at different pH and calcium chloride concentration.

emulsifiers in beverage emulsions.

Materials and Methods


Materials
Soybean oil was purchased from a local retailer, and was used without further purification. Modified starch (Purity Gum BE) was obtained from the National Starch and Chemical Co. (Bridgewater, N.J., U.S.A.). Premium spray-dried gum arabic was obtained from Importers Service Corp. ( Jersey City, N.J., U.S.A.). WPI (Alacen 895, protein 93.5%) was obtained from New Zealand Milk Products (Santa Rosa, Calif., U.S.A.). Calcium chloride and sodium azide were purchased from Sigma Chemical Co. (St. Louis, Mo., U.S.A.). Distilled, deionized water was used in the preparation of all solutions.

as the full particle size distribution or as the surface-volume mean radius: r32 = niri3/ niri2, where ni is the number of droplets of radius ri. To prevent multiple scattering effects, the concentrated emulsions were diluted with distilled water prior to analysis so that the droplet concentration was less than about 0.02 wt%. The dilute emulsions were placed directly into the measurement cell of the instrument and stirred slowly during the measurement. Each sample was analyzed 3 times and the data are presented as the average. The initial droplet size distributions of the emulsions stabilized by the 3 types of biopolymer emulsifiers are shown in Figure 1.

-Potential measurements
Oil-in-water emulsions (0.01 wt%) were injected directly into the measurement chamber of a particle electrophoresis instrument capable of measuring the -potential of emulsion droplets (Zetamaster; model ZEM5003; Malvern Instruments, Worcester, U.K.). The -potential measurements are reported as the averages of 3 separate injections, with 3 readings made per injection.

Preparation of emulsions
An aqueous emulsifier solution was prepared by dispersing 20 wt% gum arabic or 14 wt% modified starch or 0.7 wt% WPI with 0.02 wt% sodium azide in distilled water (for antimicrobial agent in this study only, not for food additive) and stirring for at least 6 h to ensure complete dissolution. A 14 wt% soybean oil-in-water emulsion was prepared by weighing 70 g soybean oil and 430 g emulsifier solution into a 1000-cm3 plastic beaker and blending with a high-speed homogenizer for 1 min (Bio Homogenizer; Biospec Products Inc., Bartlesville, Okla., U.S.A.). The size of the emulsion droplets was then reduced further using a high-pressure valve homogenizer (Rannie model 8.30R; Wilmington, Mass., U.S.A.). A series of 0.01 wt% emulsions with different CaCl 2 concentrations was prepared by diluting the concentrated emulsion with distilled water containing different concentrations of calcium chloride. Then the diluted emulsions were adjusted to different pH values by adding a small amount of dilute NaOH or HCl solution.

Results and Discussion


Influence of pH and CaCl2 on droplet aggregation
The pH and CaCl2 concentration dependence of the mean

Particle size determination by light scattering


The particle size distribution of the emulsions was measured using a laser light scattering instrument (Horiba model LA-900; Irvine, Calif., U.S.A.). This instrument measures the angular dependence of the intensity of light scattered from a dilute emulsion. It then finds the particle size distribution that gives the best fit between the experimental measurements and predictions made using light scattering theory. A refractive index ratio of 1.08 was used by the instrument to calculate the particle size distributions. Measurements are either reported

Figure 3Droplet size distribution of emulsions stabilized by whey protein without calcium chloride at selected pH values.

Food Chemistry and Toxicology

Comparison of emulsifier types . . .

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Figure 4 -Potential of emulsion droplets stabilized by gum arabic, modified starch or whey protein in the absence of calcium chloride at different pH.

Figure 5 -Potential of emulsion droplets stabilized by gum arabic at different pH and calcium chloride concentration.

droplet size of emulsions stabilized with gum arabic, modified starch, or whey protein were required. These measurements were carried out 24 h after CaCl2 was added to the emulsions and they had been stored at 30 C. There was no significant difference in mean droplet size of emulsions stabilized with gum arabic or modified starch in pH range from 3 to 9 and CaCl2 concentration 0 to 25 mM (data not shown). Both modified starch and gum arabic have been reported to be mildly anionic in aqueous solutions (Ray and others 1983; Tse 1990; Tan 1997). The carboxyl (-COO) ions are at the periphery of the molecule and are very active in creating an anionic environment (Tan 1997; Thevenet 1988). However, addition of calcium chloride at different pH values did not alter their properties. This finding suggests that these emulsions were predominantly stabilized by steric interactions, as changes in electrostatic interactions did not have a significant impact on droplet aggregation. These results also agree with the -potential of the droplets that will be discussed later. In contrast, the mean droplet sizes of emulsions stabilized by whey protein differed appreciably from that of the initial emulsion, depending on pH and calcium chloride concentration (Figure 2). In the absence of calcium chloride, there was a significant increase in the mean particle size around the isoelectric point (4 pH 6) of the whey proteins, indicating that appreciable droplet aggregation occurred (Figure 3).

The addition of calcium chloride to the emulsions significantly altered the extent of droplet aggregation. When the calcium chloride concentration was increased from 0 to 3 mM, the pH at which the droplets aggregated shifted to a higher value (Figure 2). As the concentration of calcium chloride increased, the range of pH values above the isoelectric point over which the emulsions became unstable grew wider. At high calcium chloride concentration (above 20 mM), the emulsions were unstable to aggregation at all pH values above the isoelectric point, but at pH 3 CaCl 2 did not influence the stability of emulsions stabilized with whey protein. This result indicated the possibility of using whey proteins as emulsifiers for beverage emulsions because these products have a low pH.

Influence of pH and CaCl2 on -potential


The role of electrostatic interactions in stabilizing emulsions was examined by measuring the electrical charge of the droplets. The dependence of droplet -potential on pH and calcium chloride concentration is shown in Figure 4 to 7. In the absence of calcium chloride, the -potential of gum arabic and modified starch remained negative at all pH values (Figure 4), possibly because of the negatively charged (COO) groups on the acidic polysaccharide (Tan 1997; Garti 1999). The modified starch has no cationic groups and there-

Figure 6 -Potential of emulsion droplets stabilized by modified starch at different pH and calcium chloride concentration.

Figure 7 -Potential of emulsion droplets stabilized by WPI at different pH and calcium chloride concentration.

Comparison of emulsifier types . . .

fig A

fig B

Figure 8Mean droplet size of emulsions stabilized by gum arabic, modified starch or WPI with different temperature at pH 3 (a) with 0 mM CaCl2 (b) with 25 mM CaCl2.

fore did not become positively charged at any pH. The gum arabic has some cationic groups in the protein fraction of the molecule and, therefore, would be expected to become positively charged at sufficiently low pH. Nevertheless, the isoelectric point of gum arabic has been reported to be significantly below the pH studied in this work (Jayme and others 1999). Our results also showed that calcium chloride had a small effect on the -potential of emulsions stabilized with gum arabic or modified starch (Figure 5 and 6). In both gum arabic and modified starch at the lowest pH, in the absence of calcium chloride, the droplets had a relatively low negative -potential (Figure 4). An increase in pH in the absence of calcium ions caused an increase in the magnitude of negative charge on the droplets, which was probably due to deprotonation of some of the protonated carboxyl groups (COOH COO + H +) or protonation of some of the amino groups (NH2 + H+ NH3+). When the calcium concentration was increased from 0 to 3 mM, there was a dramatic decrease in the negative value of the -potential on gum arabic-stabilized droplets (Figure 5 and 6), which could have occurred because of 2 different phenomena: electrostatic screening and ion binding (Hunter 1986). At higher CaCl 2 concentration, the zeta potential of the gum arabic-stabilized emulsions became slightly less negative, whereas there was little change in the zeta potential

of the modified starch-stabilized emulsions. This suggests that there may have been some binding of Ca 2+ ions to negative groups on the biopolymer surfaces. The - potential on the emulsion droplets would contribute to electrostatic repulsion, but the magnitude would not be large enough on its own to stabilize emulsions. These results suggest that steric repulsion is a more significant stabilizing force in gum arabic or modified starch-stabilized emulsions than electrostatic repulsion. Calcium chloride concentration and pH significantly influenced the x-potential of droplets stabilized by whey protein (Figure 4 and 7). At the lowest pH, in the absence of calcium chloride, the droplets had a relatively high positive x-potential because the pH was below the isoelectric point of the protein (Figure 4). Under these conditions the amino groups are positively charged (-NH3+), whereas the carboxyl groups are neutral (-COOH). When the pH was increased, the magnitude of the positive charge on the droplets decreased, partly because carboxyl groups became negatively charged (-COO ) and partly because some of the amino groups become neutral (-NH2). Eventually the x-potential of the droplets became zero, which indicates that the number of positively charged groups balanced the number of negatively charged groups. A further increase in pH caused the droplets to gain a net negative charge, which increased as the number of negatively charged groups increased and posi-

fig A

fig B

Figure 9Mean droplet size of emulsions stabilized by gum arabic, modified starch or WPI with different temperature at pH 7 (a) with 0 mM CaCl2 (b) with 25 mM CaCl2.

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Comparison of emulsifier types . . .


tively charged groups decreased. In the absence of CaCl2, the isoelectric point of the emulsions droplets occurred at pH 4.7 (Figure 4), which is close to the mean isoelectric point of whey proteins reported in the literature (Swaisgood 1996). In the presence of CaCl2, the isoelectric point of the emulsions droplets increased to pH 5.5, and was relatively independent of CaCl2 from 3 to 25 mM (Figure 7). This suggested that Ca2+ ions bound to negatively charged groups (-COO ) on the proteins and increased the net positive charge, so that a higher pH had to be reached before the droplet charge was neutralized. An increase in calcium chloride concentration altered the -potential of the whey protein-stabilized droplets (Figure 7). At low pH, calcium chloride caused a decrease in the positive potential on the droplets, whereas at high pH it caused a decrease in the negative potential. These results suggest that at low pH there may have been some binding of Cl ions to the NH3+ groups of the proteins, causing a decrease in positive charge. In contrast, at high pH there may have been some binding of Ca2+ ions to the COO groups of the proteins, causing a decrease in negative charge. Alternatively, the reduction in charge magnitude may be due to electrostatic screening by the ions. acid residues leading to enhanced protein-protein interactions via hydrophobic interactions and thio-disulfide interchanges (Dickinson and Matsamura 1991; McClements and others 1993; Monahan and others 1993, 1996). The addition of 25 mM CaCl 2 had a strong destabilizing influence on the emulsions, and it was strongly temperaturedependent (Figure 9b). Below 70 C, the emulsions were flocculated because of electrostatic screening and charge neutralization by the divalent ions. Above 70 C, there was an additional amount of flocculation because of the increase in surface hydrophobicity of the emulsion droplet associated with protein unfolding. Our results clearly showed that the stability of WPI-stabilized emulsions were much more sensitive to environmental conditions (pH, ionic strength, and thermal history) than gum arabic or modified starch-stabilized emulsions. In order to replace gum arabic or modified starch in beverage emulsions, WPI could only be used when the pH of the system was relatively far from the isoelectric point of the protein, such as < pH 4 or > pH 6 in the absence of minerals. Beverage emulsions fortified with minerals could only be produced using WPI as emulsifier by adjusting the pH to acid conditions to avoid flocculation problems.

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Influence of heating and ionic strength on emulsion stability


Particle size distributions of emulsions at pH 3 and pH 7 containing either 0 or 25 mM CaCl2 were measured after samples had been heated from 30 C to 90 C for 20 min then stored overnight at 30 C (Figure 8 and 9). Particle size distributions of emulsions stabilized with gum arabic or modified starch remained fairly constant over the temperature range, pH values, and CaCl2 concentrations studied. Nevertheless, the change in particle size distribution of the emulsions stabilized with WPI depended on pH, CaCl 2, and temperature. Particle size distributions of the WPI-stabilized emulsions at pH 3 (with 0 mM or 25 mM CaCl2) remained fairly constant over the temperature range studied (Figure 8a and 9a), whereas those at pH 7 WPI showed considerable increase in particle size (Figure 9b). At pH values notably lower than the isoelectric point, the protein molecules had a positive net charge that was sufficient to prevent droplets aggregating through electrostatic repulsive forces (Dematriades and others 1997a, b). At this pH, the counter ions were monovalent Cl ions rather than divalent Ca2+ ions, and therefore electrostatic screening and charge neutralization were less effective than at pH values above the isoelectric point. WPI-stabilized emulsions at pH 3 were therefore stable to heating in the absence or presence of CaCl2. A temperature-dependence was found for the WPI-stabilized emulsions at pH 7. In the absence of CaCl2, the particle size of emulsions changed little between 30 C and 90 C (Figure 9a) except for the emulsion heated to 70 C. A maximum in droplet flocculation has been observed at this temperature in previous studies of the influence of heating on the stability of WPI-stabilized emulsions. The higher degree of flocculation of emulsion droplets above 65 C was most likely caused by heat-induced unfolding of protein molecules adsorbed to the oil-water interface (Hunt and Dalgleish 1995; Dalgleish 1996; Monahan and others 1996). Differential scanning calorimetry has shown that lactoglobulin and -lactalbumin adsorbed to the surface of oil droplets unfolded when the emulsions were heated > 65 C (Dalgleish 1996). When the molecules unfolded, they exposed reactive amino

Conclusions

HIS STUDY SHOWS THAT THERE ARE SIGNIFICANT DIFFERENC-

es in the properties of model beverage emulsions stabilized by gum arabic, modified starch, and WPI. There was no effect of pH, calcium chloride concentration, or temperature on emulsions stabilized by gum arabic or modified starch. In contrast, droplet aggregation of whey protein-stabilized emulsions was strongly dependent on pH, calcium chloride concentration, and temperature. Emulsion droplets stabilized by whey protein were highly unstable to aggregation near the isoelectric point of the proteins because of the relatively low electrostatic repulsion between the droplets. At pH values below the isoelectric point, the emulsion stability was relatively insensitive to calcium chloride concentration, but at the pH values above the isoelectric point, calcium chloride promoted droplet flocculation. Heating emulsions stabilized by whey proteins above 70 C promoted instability to flocculation at pH 7, but it had little effect at pH 3. Our results have important consequences for the application of these emulsifiers in beverage emulsions. To produce an emulsion stabilized by whey protein that is stable to flocculation, it is important to ensure that the pH is sufficiently far from the isoelectric point of the protein and that the calcium concentration is less than that required to promote droplet flocculation. These criteria may be met in many beverage emulsions that have acidic pH.

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Comparison of emulsifier types . . .


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This report is based on work supported by Dairy Management Incorporated and the U.S. Dept. of Agriculture under Hatch Grant 745.

Authors are with the Biopolymers and Colloids Research Laboratory, Dept. of Food Science, Univ. of Mass. Address inquiries to author McClements (Email: mcclements@foodsci.umass.edu).

Food Chemistry and Toxicology

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