An Electronic Imaging System for Determining Droplet Size and Dynamic Breakdown of Protein Stabilized Emulsions

J.L. KLEMASZEWSKI, 2. HAQUE, and J.E. KINSELLA ABSTRACT
A computerized imaging system, consisting of a light microscope and a light sensitive diode array interfaced with a computer, was developed and evaluated for monitoring emulsion droplet size distribution and rate of emulsion droplet coalescence. This system compared favorable with electron microscopic analyses and light scattering studies for determining emulsion droplet size. Oil in water emulsions stabilized with 0.05, 0.1, 0.2, 0.5, and 1.0% /3-lactoglobulin casein or were studied. It was observed that P-lactoglobulin stabilized emul-

sionsformedsmallerdropletsthat coalesced a slowerratethenthose at
stabilized by acid casein. Emulsions stabilized by less than 0.2% protein were extremely unstable.

INTRODUCTION THE INCREASED PRODUCTION of formulated and fabricated foods requires the availability of reliable functional ingredients, and the increased demand for functional ingredients has dramatized a corresponding need for methods to characterize the functional properties of ingredients (Kinsella, 1984). Emulsifying agents are of primary importance in imparting stability to many food systems, such as milk, mayonnaise, salad dressings, whipped toppings, and sauces. Emulsifiers may function by one of several mechanisms; these include lowering the interfacial tension between the phases, surrounding the emulsion droplet with a charged layer and providing a physical barrier to the approach of other droplets (Walstra, 1986). Proteins, which possessan amphiphilic nature by virtue

of their primary structurewith polar and apolardomains,are useful emulsifyingagents.In additionto the electrostatxrepulsion of charged groups, polypeptide loops and trains in an interfacial film provide a barrier to the close approach of oil droplets (Phillips, 1981). The breakdown of emulsions via co-

(Walstra 1965, 1968) and (Pearce and Kinsella, 1978), electrical conductivity measurements (Webb et al, 1970), centrifugation (Sherman, 1971), emulsion capacity tests (Swift et al., 1961), solubility studies (Voutsinas et al., 1983), the Coulter counter (Walstra and Oortwijn, 1969) and electron microscopy (Liboff et al., 1988). However, these methods lack the real time reliability of studying emulsion breakdown with light microscopy (Halling, 1981). Many of these available methods are inadequate for protein stabilized emulsions. For example, the Coulter counter uses salts that can alter the conformation of the interfacial protein and may interfere with the state of dispersion of the emulsion (Tadros and Vincent, 1986). Many researchers now use light scattering methods to study emulsions because of their rapidity and reproducibility (Kinsella, 1984). Studies using light microscopes are limited by the lack of magnification that hinders accurate sizing of the smallest emulsion droplets and is time consuming and tedious. The method reported herein provides further magnification of the microscopic image and permits the sizing of smaller particles using a light sensitive diode array. Because the emulsion is not manipulated, real time studies of emulsion breakdown can be accurately performed. Protein based surface active agents are being increasingly developed for use in food emulsions, and hence rapid and reliable methods are needed to assestheir emulsifying activity (EA) and emulsion stabilizing properties. The present research describes the development of a method for determining EA

and monitoringthe breakdown emulsions of stabilizedby j3lactoglobulinand acid casein.
MATERIALS
Materials

& METHODS

alescence oil droplets,resultingin decreased of surfacearea
and flocculation is retarded by interfacial protein films (Dickinson and Stainsby, 1982). Creaming is slowed by homogenizing the droplets to a small size to minimize the effects of the density differences between the phases (Walstra and Ootwijn, 1975). The wide range of hydrophobic and hydrophilic properties available in different proteins can be exploited in formulated food emulsion systems. Proteins also provide nutritional benefits not available from lipid-based emulsifiers, and they are not subject to the concern and scrutiny provoked by various classes of chemical emulsifiers. The use of proteins as emulsion stabilizers has been the subject of many studies (Halling, 1981). The properties of emulsions stabilized by proteins vary with the equipment used for their preparation (Thorberg and Lundh, 1978). A standard procedure has been improved by interfacing a single piston valve homogenizer with a computer to control energy input (Haque and Kinsella, 1989). Several methods to characterize the stabilizing effects of emulsifiers have been used. These include light scattering
Authors Klemaszewski and Kinsella are with the Inst. of Food Science, Cornell Univ., Ithaca, NY 14853. Author Haque’ press ent address is Dairy Science Dept., Mississippi State Univ., Drawer DD, Mississippi State, MS 39762.

The emulsions in this study were stabilized by either p-lactoglogulin or casein. Pure D-lactoglogulin (A & B from bovine milk, crystallized an lyophilized) ‘ and iGda\ole (crystalline) were both obtaiied from the Simna Chemical Co. (St. Louis. MO\. Casein was nreoared bv the hydrochloric acid precipitation of fresh raw skimmed’ miik (Da<ies, 1936). Emulsions were made with pure peanut oil that did not contain added emulsifiers. The specific gravity of this oil was 0.91. The Staining solution of 0.1% Congo red, a hydrophilic dye, contained 5% gelatin (Bovine skin, type?II) which-was+buffere-d;o pH 7.0 with 0.05M imidazole buffer. The staining solution was maintained as a liquid by keeping the solution at 90°C. The gelatin was obtained from Sigma Chemical Co., and pure Congo red was obtained from Electron Microsconv Science (Fort Washington. PAL All other chemicals used were reagent grade and distilled deionized water was Used throughout this study. The imaging system consistedof a light sensitive diode array mounted atop the right eyepiece of an American Optical AO-150 light microscope. The light microscope was equipped with a 15X eyepiece for examining fine emulsions and a 10X eyepiece for examining coarse emulsions. The diode array is composed of a series of 32768 pixels, 3.56 per horizontal line and 128 per vertical line. The diode array was interfaced to a Turbo-XT computer via an input/output board. The computer was used to set the threshold light level for the diodes, set the exposure time for the pixels and was used to gather the image data from the diode array. The computer set the exposure time foi the pixels such that 25 to 30% of the pixels were transmitting 5 volts to the computer. The exposure time was changed as needed by the com.< _ I

440-JOURNAL

OF FOOD SCIENCE-Volume

54, No. 2, 1989

The lower refractive index of the oil. The computer converted these data to an image on the screen. 2 N (1) the average droplet diameter. from the homogenizer. The microspheres were obtained from the Epics division of Coulter Corp.0% (w/w).1. compared to water. 2. The use of Congo red accentuated the contrast. i. 0.2% casein obtained using a computerized diode array imaging system to magnify light microscope image (2940 x).1 mL) of the emulsion were removed at hourly intervals and mixed in a testube with 0. The homogenizing system was kept at a constant 25°C using a circulating water bath. (Hialeah. Coalescencewas observed by a decreasein the emulsion surface area and an increase in the average size of the droplets with time. 0. was made LID in 50 mM imidazole’ pH 7. The emulsion was transferred to a beaker and slowly stirred to prevent creaming. The method of Walstra (1968) uses the &s obtained from light scattering data in equation (3). The d.2 mL of the staining solution at 90°C. 0. Calculations. (3) is in units of meter2 per Volume 54. A series of 8-lactoglogulin or acid casein solutions. Emulsions samples for the electron microscope were prepared in the same manner as for the imaging system. corresponding to an energy input of 640 X 10” J. This image was printed out for manual analyses. Emulsions were then viewed using the imaging system. The image onthe screen was a magnification of the emulsion as seen by an experimenter through the eyepiece (Fig. and emulsion surface area were determined by the spectroturbidimetric method of Walstra (1968) using a Gary 219 dual beam spectrophotometer with automatic base-line correction to scan the samples from 350 to 870 mm. 1). The magnification of the diode array and the light microscope was approximately 5500 fold with an approximate resolution of 0. Surface area of the emulsion was also determined from the turbidity at 550 nm using the equations of Pearce and Kinsella (1978). The stained emulsion was immediately placed on a microscope slide and spread thinly to obtain a uniform layer of emulsion. Area = 4s The surface area obtained from Eq. aliquots (0. The calibration was confirmed using latex microspheres of a known diameter. the emulsion. By measuring the diameter of all the droplets on an image.2.05. Emulsion samples for the light scattering studies were prepared in the same manner as for the imaging system.01 The emulsions were made by initially to dispersing 12 g of protein solution and 8 g of oil with a Janke-Kunkel TP 18-10 turbo blender for 5 set prior to passage through the valve homogenizer. 1957). casein stabilized emulsions were viewed using scanning electron microscopy @EM). Data from the diode array consisted of binary data reflecting the threshold light levels on each of the pixels. provided the minimum contrast required for droplets to be distinguished.5. (2). The average droplet size was determined using equation (l).05M imidazole-HCl to give an absorbance between 0.04~. 6. and the image was printed out for measurement of the droplet diameters. where 6 is the volume fraction of oil. This method involves gathering light scattering data over a range of wavelengths and fitting the absorbance obtained to equations for ideal theoretical turbidometric data for best fit lines as described by Walstra (1965). 2. Sample preparation for light scattering studies. For these studies. No. nt is the number of droplets of size i microns and N is the total number of droplets measured. To check the accuracy of the imaging system.1~ divisions. The average droplet size of the emulsions were determined from the histograms prepared from the data obtained using the imaging system. described by Walstra (1965) as the average volume to surface ratio. as described by Haque and Kinsella (1989).rne3. of the emulsion. The d.Methods Emulsion preparation. have been applied to the study of emulsions (Walstra. was immediately diluted from 50 to 5000 fold in a 0. a histogram of the droplet size distribution for each view of an emulsion was prepared.1% SDS solution buffered to pH 7. changesin droplet size with time. over 100 droplets were measured for each sample. where d.. 0.0 by 0. = of an oil (light) in water (dark) fig. d x3 = X i3 ni X i2 ni l l puter. Surface area of emulsions were calculated by three different methods. based on the Mie theory (Van De Hulst.18~ when the 15X eyepiece was used. To monitor stability.e. was determined from the histograms obtained by the imaging system using Eq. The methodology for sample preparation for SEM has been decribed by Liboff et al. FL). is d. In order to make the experiment statistically valid.0 S. 0. The cuvettes used for this study allowed a small acceptance angle of light to be passed through the sample. The imaging system was calibrated using an American Optical stage micrometer marked in 0.7.75 and 1.2 and 0. Sample preparation for electron microscopy. A cover slip was placed on the slide and the stained emulsion sample was then cooled on ice to solidify the warm gelatin and prevent further coalescence of the emulsion. of the emulsion was also determined using the light scattering method of Walstra (1965). 1989-JOURNAL OF FOOD SCIENCE-441 . 1-A typical micrograph emulsion stabilized by 0. Emulsions were obtained by passing the protein solution and oil mixture through a valve homogenizer for 180 strokes. Light scattering methods. 1965) and Pearce and Kinsella (1978). The temperature of the emulsion was held constant at 25°C. (1988). The d.

4 6. where r is droplet radius. Since the droplet size distribution of this emulsion should be normal (Walstra. The total volume and total surface area of all the droplets observed was determined using Eq.5 a. Volume = I: F Surface Area = I: 47rr2 (5) (6) 1. 2)..6~ to 7.Op. The droplet size distribution of the sample taken after 2 hr is skewed to the right slightly more than the 6 hr sample.2% acid casein stabilized emulsion (Fig. Data were gathered for similar emulsions stabilized with specified concentrations of &lactoglobulin and acid casein as emulsifying agents.3 4.5 7. skewness indicates that some droplets were smaller than the resolving power of the imaging system.2% P-lactoglobulin (Fig. The histograms revealed that the droplet size distributions were normally distributed with one mode (Fig. This type of distribution is usual for a simple emulsion system (Walstra. 1968).05% P-lactoglobulin. 40 a 30 f E 20 10 Fig.6 2. 1). The surface area as calculated using Eq.0 7.6~ for an 442-JOURNAL emulsion stabilized by 0.Og of oil.5 Dilution Factor = Volume “Og Oil Result of Eq.0 6.2% casein after 0 hr.5% P-lactoglobulin stabilized emulsions 2 and 6 hr after the emulsion was prepared. By measuring the diameter of the droplets on an image printout. The change in emulsion stability with time was observed as the tendency for the droplet size distribution to increase with time.4 2.DETM.8 4. 1989 . gram of emulsion. 1s the volume b fraction of oil.4 DmplU 5. light scattering OF FOOD SCIENCE-Volume 54. The droplet sizes observed ranged from 0. (4) is also known as the emulsifying activity (EA) for proteins. distribution in after 0 hr.3 3. (5) and (6). as shown by electron microscopy (Fig. and the droplet size distribution of emulsions were studied by electron microscopic. .5 (haicmns) 7.41~. as compared to 1. (5) This dilution factor gave the factor with which the result of equation (6) was multiplied to calculate the surface area of l. The “dilution factor” was determined using EQ.2% plactoglobulin 0. 8. as these were the units used for comparing the emulsifying activity (EA) of proteins.5 10. The method of Pearce and Kinsella (1978) gives the surface area of the emulsion in units of meter* per gram of rotein directly from Eq.2~ for an 0. which are the combined histograms obtained for 0.7 3. 2-Scanning electron microscope view of emu(sion stabilized by 0. an emulsion stabilized by 1% P-lactoglobulin to dropfor lets larger than 40 p. 2. The smallest droplets observed using the imaging system have diameters around 0. Fig.36~. These two emulsions had comparable average diameters of approximately 5~. are shown as printouts of what was observed through the light microscope (Fig. 0 1. These emulsions. J-Histograms of emulsion droplet size emulsions stabilized by (a) 0.4 4. in emulsions stabilized by dilute. (b) RESULTS THE EMULSIONS studied in these experiments were composed of a heterogenous population of dispersed spherical oil droplets. 4. (7). as observed using the imaging system.4 sii 6. DROPLET SIZE DYNAMIC BREAKDOWN OF EMULSIONS. 3).6 Dmplu Si (Micmns) (1988) (2704 x). . C is the protein concentration of the solution used to make the emulsion and 1 is the pathlength of the cuvette. 3a) to the range of 1. as shown by comparing the range of droplet sizes of 1.2 2.3% casein obtained using the methods of Liboff et al. 0. where A is the absorbance at 550 nm. Emulsions stabilized by P-lactoglobulin were less heterogeneous than those stabilized by acid casein.4~ for the sample at 6 hr.4 3. as shown in Fig. No. 3b). The surface area of an emulsion can also be calculated from the histogram obtained from the imaging system data. Values of surface area obtained were all converted to meters2 per gram of protein. (4). 1968).9 5. a histogram of droplet size distribution for each emulsion was prepared. The distribution mode for the sample taken at 2 hr was l.4~ to 10.5 9.

A-A method of Pearce and Kinsella (1978).5% plactoglobulin of coalescence.2%. Comparison with light scattering method. for light scattering data (Fig. 6). 3 8 z d 6. 5-Effect of protein concentration and method of determination on d. The imaging system was also used to study the breakdown of these emulsions. At protein concentrations less than 0..8 1. At protein concentrations greater than 0.4 0. 0.6 0.4 0.3% of either protein. A-A casein stabilized emulsion. M-H method of Walstra (1965). determined by light scattering (Walstra.8 1.0 - 0. it appeared that the light scattering method was appropriate for emulsions with average droplet diameters less than 7.2 0.0 0. observed using imaging system.1~ for data obtained from the imaging system. The 4% of an emulsion stabilized with 0..0 1.2% protein or greater (Fig.0 4. 5)..3 0. for emulsion droplets stabilized by greater than 0. 5).0 1. of the emulsions was very comparable for emulsions stabilized by 0.. Since the method of Walstra (1965) calculates surface area directly from d.96.. It has been reported that the light scattering method used is not accurate in studying coarse emulsions (Walstra. The a.0 Protein Concentration(96) 0.The results obtained from light scattering for finer emulsions were much more variable than the data obtained from the imaging system.2 0.4 0.0j T Pmein CImcentration(96) Fig. This agreement was offset by the high variation of the light scattering method.. The results of these experiments showed that the light scattering method of Walstra (1965) again showed greater disparity compared to the imaging system when studying coarse emulsions (Fig.2%.2 Protein Concentration(%) Fig. Pearce and Kinsella (1978) and the imaging system. methods and the imaging system. this method indicated a finer emulsion than was actually present.1% casein was determined to be 25. 1989-JOURNAL OF FOOD SCIENCE-443 .2 3. (3).4 2. was compared with the 4. of emulsions (as defined by Eq.0~~.91.L. it is expected that the same limitations apply to surface area calculations. monitored using the method of Walstra (1965). as the standard error of the d. (a) casein (b) plactoglobulin. (2).8 1. U-Q plactoglobulin stabilized emulsion.5l.7 2. 1968). monitored using the method of Walstra (1965).6 1.1 2.. 1968).0 1. whereas it was less than 0. No.5 ‘ Fig. but this light scattering method gave a d. u plactoglobulin stabilized emulsion. of the same emulsions obtained using the imaging system. Surface area determined using a--o imaging system.2 8.. of 4. as determined by these two methods did not differ by more than 0. 6-Relationship between methods for determination of surface area for emulsions stabilized by different concentrations of proteins. using Eq. 2. 5).8 3. The d.0 0. 4-Histograms of emulsion droplet emulsions stabilized by 0. observed using imaging system. when protein concentrations were reduced to less than 0. The correlation between the imaging system and the light scattering method was quite high.800 0. A-A casein stabilized emulsion. size distribution in after 2 hr and 6 hr 0.2%.2 0.6 0.according to the imaging system.4 1.0 2. the imaging system compared favorably with the results obtained using the method of Walstra (1965).6 0. From the data gathered in these experiments. was greater than OSp. The results derived from the light scattering method of Pearce and Kinsella (1978) were comparable to the results obtained with the imaging system at protein concentraVolume 54.. The surface area of the emulsions was determined using the methods of Walstra (1965). However.8t~.~ for smaller droplets (Fig. The average emulsion droplet volume to surface diameter (&). this light scattering method gave lower values for the &.

at 640 x lo6 J-m-’ of energy input.03t.2 1.0 0.2% protein were initially unstable. 8a). 2. B-lactoglobulin formed emulsions with smaller emulsion droplets than acid casein.9111. Halling.for 1. 1981).0 0.4 0.0% P-lactoglobulin was 1.39p. At lower protein concentrations. The method of Pearce and Kinsella (1978) had a higher variability than the imaging system. The average droplet size did not differ much between emulsions stabilized by 0.0% protein for the proteins studied.0 0. but the variability was similar to that of the Walstra (1965) method.3111 after 5 hr of storage at 25°C.0% plactoglobulin.5% protein and then decreased. this was not the case for surface area per unit protein at different protein concentrations (Fig.0% acid casein stabilized emulsions. 1982). the protein at the interface may not com-pletely unfold. Initial emulsion characteristics.0% P-lactoglobulin and O. The method of Pearce and Kinsella (1978) is simple and is useful for estimating surface area of emulsions with mean droplet sizes in the range of 2t.8 Protein Concentration (46) 1. 1984). 8-Effect of emulsion breakdown time on (a) average droplet diameter and (b) emulsion surface area for emulsions stabilized by U-U 0. At protein concentrations greater than 0. Emulsions stabilized by less than 0. . . Data gathered using the imaging system showed that the average droplet size of emulsions increased and the interfacial surface area decreased with time (Fig. 1989 sequent interactions are also critically important (Graham and Phillips 1979.to 15p. Kinsella. but emulsions stabilized with plactoglobulin did not compare as favorably (Fig. as compared to 1.5% casein.2%.91b to 2.5% and 1.~. 7-Effect of protein concentration on (A) average droplet diameter and (B)‘ emulsion surface area for emulsions stabilized by M Plactoglobulin and A-A casein.8 Protein Concentration (%) 1. 7a).1.2 0 2 4 6 Breakdown Tie (bows) a 10 b 0.0% acid casein. 7b).0% p-lactoglobulin increased from 1. in the same time period (Fig.6 0. surface area. Emulsion stability.0% acid casein increased from 1./ hr for 1. 6b). No. A-A 1. The average droplet size of the emulsions stabilized by 1. The effects of protein concentration on unit surface area of emulsion were similar.r. the EA initially increased to a maximum at 0. As protein concentration increased. 8). W--W 0. The average droplet diameter of an emulsion stabilized by 1.14+. The ability of a protein to adsorb at interfaces influences its ability to form emulsions (Dickinson and Stainsby. tions less than 0.5% plactoglobulin. The slopes of the bestfit lines for the breakdown of these two emulsions were 0. with average droplet sizes much greater than 5t. This effect may be caused by protein forming a thicker film at the interface without an increase in surface area directly proportional to the amount of available protein.2%. a 0. with surface area increasing with increased protein concentration. 1979. Fig.2 0 2 8 4 6 Breakdown Tie (hours) 10 Fig.DETM.4 0. However. decreased with increasing protein concentration (Fig.2 1. it was observed that acid casein stabilized emulsions had a faster breakdown rate than did p- . 6a). The average droplet size of emulsions stabilized by S-lactoglobulin and acid casein. The average droplet diameter of an emulsion stabilized by 1.2%. DROPLET SIZE DYNAMIC BREAKDOWN OF EMULSIONS. The data obtained from the imaging system and those by the method of Pearce and Kinsella (1978) were comparable at all the casein concentrations studied (Fig. B-Lactoglobulin may form finer emulsions than acid casein because it may adsorb at the interface more rapidly than acid casein and perform extensive molecular interactions.0 0.6 0. The effects of increasing protein concentration on droplet size were small at protein concentrations greater than 0. the protein may unfold more extensively because it is thermodynamically favorable to coat as much interfacial area as possible by unfolding (Graham and Phillips.2% and greater than 0. At higher concentrations. By comparing these slopes. A-A 1. but sub444-JOURNAL OF FOOD SCIENCE-Volume 54.0% casein.14~ to 1.O9p&r for 1.

Emulsion Stability. 1988. Agric.5% protein (Fig. the imaging system could be used to study a wide range of fine and coarseemulsions (Klemaszewski and Kinsella.. NY. 1983. MS received 2/19/88. Walstraj P. 21(3): 197. Coil.K. Emulsifying properties of proteins: evaluation of a turbidimetric technique.L. F. and Oortwign. and Fryar.ior to emulsification. %. 1965. 15: 468. (Ed. Tornberg. 1986. Volume 54. andNakai. We. M. a greaternumber of observations must be taken as compared to the average diameter. Publishers. Large droplets provide a greater driving force for the creaming of the emulsion and possibly resulting in higher rate of droplet collisions. C.E.J.5% acid casein was O. N. Crai H. larger surface area. Klemarzewski. In “En clopedia of Emulsion Technology. in part. 2. Suuuortfrom the National Dairy Research Board is aclmowledaed. 26: 716. 43: 1653.5% protein would be greater than the EA of an emulsion with 1. 1987. C. Food Sci. The measurement of emulsion capacity 6 y electrical resistance. Van De Hulst. In “The Chemistry of Milk.J. the larger droplets of the emulsion initially. even though both were calculated from the same data obtained from the imaging system. 1984.O9tL/hrfor 1. H. P. Tadros.A. Unpublished data. an B Stamsby. Lockett.. Essex. Food Technol. P::X.~~eina Develo ‘ mint of a stand&&d method J 00” Kinse la. Liboff. J. W. New York. 1979. N..” P.B. 2 and Kinsella J E 1969 Emulsip ~~m&. To obtain the same degreeof precision for surfaceareacalculations. and Jones. This effect was observed at both protein concentrations studied. This was-done p.F.E. 1975. __“. The surface area per gram of emulsion decreased with increasing breakdown time (Fig. The slope of curve of coalescenceof an emulsion stabilized by 0. Cornell University.llpJhr. Interface Sc-i 97. in part. P.. REFERENCES Davies.).lactoglobulin stabilized emulsions. Stability associatedwith concentrationmay also reflect a thicker interfacial protein layer providing a stronger barrier to the approach of other emulsion droplets and minimizing coalescence (Dickinson and Stainsby. 1957. Inc. Relationships of hydrophobiit2v6 to emulslfylng properties of heat denatured protems. New York. 1975). MC. J. This indicated that the imaging system could be used for the study of emulsions where the oil phase was continuous. J. 1978. D.. The imaging system can also be used on systems other than oil in water emulsions.” Applied Science .. Haque. !. Effect of globule size and concentration on creaming in pasteurized milk. Estimating globule-size distribution . Institute of Food Science. “Colloids in Foods. Increasing the protein concentration resulted in a retardation of the rate of coalescence. Food Sa. Walstra. Light scattering by milk fat globules.2%. J. SUMMARY USING THE DIODE assistedimaging system described in this paper. Proteins at li uid interfaces.E. D. England.. Z. Nutr. 1968. The faster breakdown rate of the acid casein stabilized emulsions may reflect. Z”“. B. The effects of protein concentration on emulsion stability may also reflect. Neth. Formation of emulsions. New York.. “. Halling.2%. AOR Walstra! P. Haqu. New York. Sherman. and Phillips. 1986. -. The data gathered compared favorably with light scattering studies and electron microscopy.. Marcel Dekker. Walstra. Accelerated tests of emulsion stability. 1969. Neth.” P.J.Interface Ser. J. Appl. 1981. r nc. Ivey. ..E. J.. 1981. Food Technol. Soap Perfumery Cosmetics 44: 693. it was possible to study the droplet sizes and breakdown of emulsions stabilized by acid casein and p-lactoglobulin. -__. 29: 263. J. Tri (Ed.0% protein if the emulsions were identical in droplet size distribution. 2 011.&. P. In press. Food Sci.B. and Kinsella. A. J.J... . Food Sci.. Phys. H. Data for the average diameter of emulsions was more precise than the surface area data obtained.. E. E. The proteins of milk: Casein.L. 1975). 1970.C. 8b). the emulsions were extremely unstable. caseins may form weaker films around the fat globules which are desorbed or ruptured upon contact of the droplets. The imaging system gave similar data when either Sudanblack or congo red was used to increase contrast. and a slower rate of breakdown at protein concentrations greater than 0. Barking. W. J. “Light Scattering by Small Particles. 1978. H.0% acid casein. With the use of high and low magnification eyepieces.” John Wiley and Sons.&&-m-water emulsions by Coulter Counter. 1936. J. Surface area was calculated in meter* per gram of emulsion to avoid confusion when comparing the coalescence rates of emulsions stabilized by differing levels of protein concentration. Comminuted meat emulsions: The capacity of meats for emulsifying fat.” E. Becher (Ed.J. Rev. T. In “Encyclopedia of Emulsion Technology. In addition. 35: 601. Jordan. Food Sci. and Vincent. Food Chem. 1961. Dickinson. as compared to O. This could result in an increase in the rate of coalescence (Walstra and Oortwign.&& P. Functional characterization of protein stabilized emulsions: standardized emulsifying procedure. Protein stabilized foams and emulsions.H. Estimating globule-size distribution of oil-in-water emulsions by spectroturbidimetry. E. Phillips. The P-lactoglobulin gave emulsionsthat had a smaller averagedroplet size. Changes in the ultrastructure of emulsions as a result of electron mipreparation procedures. MC. Mdk Dany J. Food Microstructure.). Becher.i. J.). The EA of an emulsion stabilized by 0. Graham. 8a). H. J. and Kinsella. CRC Crit. 6: 1187. Emulsions stabilized by 1. S. Webb.-so the lipid phase gave greater contrast. 3550.E. and Lundh. and Oort\?ngn. CRC Critical Rev. Protein conformation at liquid interfaces and its role in stabilizing emulsions.J. G. Swift. Br.J. 13: 166. 1987). 29: I-_. P. Milk Dairy J. Inc. revised 7/11/88. 1971.E. Van Nostrand Co. Goff. At protein concentrations less than 0. The imaging system was used to study emulsions that had the oil phase dyed with Sudan black. V. L. G. Marcel Dekker. 1989-JOURNAL OF FOOD SCIENCE-445 .0% protein had a slower rate of droplet size increase than those stabilized by 0. r?utr. 1982). a hydrophobic dye. Ithaca. Other applications. Voutsinas. Cheung. accepted g/30/88. the slightly larger droplet size present at lower stabilizing protein concentrations(Walstra and Oortwign.. J.D. Milk proteins: Ph sicochemical and unctional properties. 1982. No.s of adsorptron and surface denaturatron. and Kinsella. This resulted from the inordinate contributions of small droplets to surface area as opposed to volume in equations (5) and (6).

Sign up to vote on this title
UsefulNot useful