PL160671B1 - Protective agent for corrosion prevention and consolidation of corrosion products - Google Patents

Abstract

1. A method of producing a cream substitute, consisting essentially of non-aggregated, spheroidal, macrocolloid protein particles containing a core which is the casein micelles and an outer coating of denatured egg white, characterized in that it is heated egg white protein and source of substantially non-aggregated casein micelles, with a pH in the range between about 6.0 and about 7.0 under sufficient shear conditions to form particles macrocolloid caseins surrounded by denatured egg white protein, possibly in the presence of a polyhydric compound and an aggregation inhibiting agent.

Description

Przedmrntem invented is SPOS <5b wytwarzama nammstkł ^COG city tank Śmtetan ^ ^that is used to produce food products of non-fat and reduced fat that have the organoleptic properties of products such as high-fat, in particular frozen desserts such as ice cream and related frozen dairy desserts, mousses , cupcake fillers and icings.

The term "ice cream desserts" refers to a wide variety of products including ice cream, frozen creams, dairy ice cream, sorbet, corbet, frozen sweet dairy, frozen confectionery, frozen dietary desserts, Mellorine and non-dairy desserts, all of which are specified in US Government standards. Federal Standards. Frozen desserts not regulated by federal standards include frozen puddings, mousses, and spiced milk mixed with egg. For frozen dairy desserts, the standards specify a lower limit for milk fat and / or milk solids. For example, ice cream must contain not less than 10% milk fat and 20% total milk solids (including total milk fat and non-fat milk solids, "MSNF"); Milk ice cream must contain 2 to 7% milk fat and not less than 11% total milk solids; the sorbet must contain 1 to 2% milk fat and 2 to 5% total milk solids, see R. S. Redfern and W. S. Arbuckle, "Ice Cream Technology Manual 4th ed. 1985, Redfern and Assoc. Ltd., Raleigh, N. Carolina 27622.

Known ice cream and other frozen whipped milk desserts are complex foams consisting of air bubbles surrounded by a partially frozen emulsion in which ice crystals and solidified fat globules are embedded in the non-frozen aqueous phase. The approximate values of the coarsely dispersed structural components of ice cream vary. Ice crystals range in diameter between 20 to 60μτα and are spaced 7 μτη apart, air bubbles range between 10 to 175μιη and are in

At intervals of about 125 µm, solidified fat globules vary in size from 0.2 to 2.0 µτη and form clusters, thus giving a "skin around trapped air cells, see. . Fundamerta's of Dairy Chemistry, 2nd Ed., 1983, B. H. Webb et al., Avi Publishing Company, Inc., Westport, Connecticut, pp. 896-913.

It is well known that the fat content of frozen milk desserts is essential not only for the texture and consistency of the product, but also for its flavor characteristics. The smoothness of cream ice cream is generally inversely related to the average size of the ice crystals. Increase in milk fat content for a given iced dessert, both smaller size of ice crystals and smaller distance between the crystals. Despite the high price and high caloric value associated with milk fat, as well as its susceptibility to oxidation, which causes an unpleasant smell and a tendency to give the effect of a whipped solder, buttery consistency, usually products such as full-fat cream ice cream are preferable to milk ice cream, sorbets, etc. , the so-called Premium grade cream ice cream generally has a higher milkfat content than the standard 15 to 18% and is generally considered to be tastier and correspondingly smoother and better in texture compared to standard grade cream ice cream and lower dairy dessert products. fat content.

In attempts to develop recipes for frozen dessert type products in which some or all of the fat content has been replaced with a non-fat substance, none of the products produced has been substantially successful as a replacement product for full-fat cream or dairy ice cream. See, e.g., U.S. Patent 4,510,166, relating to ice cream recipes that use starch gels as fat replacer, and U.S. Pat. 4,421,778 and 4,552,773 for whipped food products containing beta-phase crystalline fats, and British Patent No. 915,389 and US Pat. No. 3,510,516, No. 3,556,813, No. 4,400,405 and No. 4,631,196.

Thus, there is an ongoing need for low-fat and reduced-fat frozen dessert products that have organoleptic and physical characteristics such as full fat frozen dairy desserts. Ideally, such products should have the same or higher nutritional value as standard whipped dessert products but have a reduced caloric value. In addition, there is a need for fat substitutes or creamers that can be made, stored and used in the preparation of a variety of low-fat and non-fat food products, including frozen whipped desserts.

The method of the present invention produces a creamer substitute consisting of substantially non-aggregated spheroidal macrocolloidal protein particles comprising a casein micellar core and an outer shell of denatured egg white protein. The method consists in heating the egg white protein and the source of substantially non-aggregated casein micelles, at a pH in the range between about 6.0 and about 7.0, under sufficient shear conditions to form macrocolloidal casein particles surrounded by denatured protein. from egg whites, optionally in the presence of a polyhydric compound and an aggregation inhibiting agent.

Preferably, ultrafiltered egg white is used as egg white, and condensed skim milk or ultra-filtered skim milk is used as the source of casein micelles.

Preferably, sugar, corn sugar, lactose or a mixture thereof is used as the polyhydric compound, and pectin, lecithin, xanthan gum, guar gum, date esters, carrageenan, alginate, maltodextrin, calcium steroyl lactate or mixtures thereof are used as the aggregation inhibiting agent, and especially a sugar, lactose or a mixture thereof is used as the polyhydric compound, and a mixture of pectin and lecithin is used as the aggregation inhibiting agent.

Preferably, the heat treatment is at a temperature of from about 80 ° C to about 125 ° C, using a shear rate of from about 5,000 to 7,500 sec- ¹ .

In addition, it is preferred to heat the egg white protein and the source of non-aggregated casein micelles with a protein: casein micelles weight ratio of 1.5-99 such that in the finished product the egg white provides from about 60 to about 99% of the total amount of protein.

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The above-described process of the invention produces a creamer substitute from a coagulating protein such as egg white and a nucleus such as casein micelles to produce substantially non-aggregated denatured protein macrocolloid complex particles which are substantially spheroidal and have a size distribution that gives an organoleptic effect. emulsion characteristic, as evidenced by taste, that is, have diameters ranging from about 0.1 µπι to about 3.0 µm, and less than about 2% of the total number of particles have a diameter greater than 3.0 µπι. These protein particles when hydrated form a macrocolloid which is substantially smooth and emulsion-like organoleptic in nature, ie with a fat or cream flavor in the mouth. In cross-section, it can be seen that the particles consist of a "core, a nucleus and a" shell of coagulating protein. " Such a food ingredient, coagulating protein (nucleating agent, used as a fat substitute) cream for making low-fat or non-fat whipped frozen desserts, and it can be used as a substitute for cream in the preparation of other low-fat or non-fat food products such as sauces, fillings for cream cupcakes, pastes, mousses and icings.

Thus, a fat-free and reduced-fat whipped frozen dessert can be prepared in which some or preferably all of the fat, vegetable fat or oil normally incorporated therein is replaced with a protein macrocolloid comprising denatured protein particles. These products have physical and organoleptic properties such as full fat products despite the absence of fat or a substantially reduced content of fat / oil droplets or globules which are known to play an important role in air cell formation and the formation and maintenance of small size ice crystals in frozen whipped desserts . Partial or complete replacement of fats or oils with proteinaceous macrocolloid substances leads to highly desirable products with reduced caloric value but high nutritional value due to the presence of additional protein. The method of producing these frozen dessert products requires no equipment other than that normally used to prepare frozen dairy desserts and in all cases the protein macroloids can be incorporated into the dessert recipe as a substitute for milk fat, or vegetable fats or oils.

Preferably, the creamer substitute prepared according to vanalaz is used to prepare frozen whipped desserts of the type that would normally contain fat and in which the protein macrocolloids completely replace the fat normally present, and are e.g. products that are the same as ice cream, which have physical and organoleptic characteristics. as premium grade ice cream, but with less than 1% fat.

A brief description of the attached drawing figures and a detailed description of the method of implementation are given below.

Figures 1 and 1a of the drawing show a flow chart of a method for producing a cream substitute from egg white and casein micelles according to the invention.

Figure 2 is an electron micrograph which shows macrocolloid particles of the egg white protein / casein micelle system, the majority of which have a casein micelle core and an outer shell of denatured egg white protein.

Figure 3 shows an electron micrograph of macrocolloid particles of egg white protein / casein micelles generated in situ in the preparation of frozen whipped desserts as further described.

Figure 4 shows an electron micrograph of an ice cream analogue product that contains the macrocolloid egg white protein / casein micelles as a cream substitute and Figure 5 shows an electron micrograph of super premium grade ice cream.

All micrographs are made at a magnification of 32,500 and contain a 1μπι reference standard.

Particularly desirable organoleptic properties of the macrocolloidal substances used in the process according to the invention depend on the size and shape of the macrocolloid particles.

Dispersions of larger denatured protein coagulates (ie, diameters greater than 3μπι when dry) have been found to produce an undesirable chalky mouthfeel. The chalky one

The aftertaste can be equated with a milder variant of the gritty mouthfeel produced by the known heat-denatured proteins (about 15-175 µm). The sharply defined threshold of perception appears to be exceeded when the number of protein coagulum particles with diameters greater than about 2 to 5μιη in their largest dimension increases.

The shapes of the particles are also important. Fibrous particles greater than about 5 µιη in length and typically less than about 1 µιη in diameter produce pastes that are smooth but with increased volume; as more force is applied between the tongue and palate, an increasing solid sensation is perceived. The impression obtained does not resemble cream. As the fibers are shorter and come closer to a spherical shape, this sensation diminishes.

Further, the particles, which are usually spheroidal, tend to produce a smoother, more emulsion-like organoleptic feeling. When the proportion of macrocolloid spheroidal particles is increased or the macrocolloid particles are more accurately spheroidal, there may be occasions where a slightly larger proportion of the particles may be greater than about 2μπι in diameter, without prejudice to the organoleptic characteristics of the macrocolloid mixture. As mentioned above, however, rod-shaped particles greater than about 1 μιη in diameter tend to give a chalky or powdery impression in the mouth.

When the proportion of macrocolloid spheroidal particles is increased, or where the macrocolloid particles are more finely spheroidal, it may happen that a slightly larger proportion of particles may be greater than about 2 μιη in diameter, without prejudice to the organoleptic characteristics of the macrocolloid mixture. As mentioned above, however, rod-shaped particles greater than about 1 μιη in diameter tend to give a chalky or powdery impression in the mouth.

Particles about 0.1 μιη give a sticky feeling in the mouth that can be unpleasant if perceived as the primary tactile quality. Since the perceived transition from the emulsion mouthfeel to the greasy feel appears to be more gradual than the shift from emulsion to chalky feel, it is assumed that the macrocolloids used in the process of the invention have a larger proportion of particles with a diameter in the order of 0.1 μηι. Thus, the emulsion-like character prevails as long as the mean particle size is not less than 0.1 µιη, however, the size distribution may include the actual fraction of individual particles less than 0.1 µιη in diameter.

The particle size test gives a measure of the organoleptic properties of the products produced according to the invention.

One of the simplest and fastest techniques available to a person skilled in the art is to prepare the formulation in a manner analogous to that for preparing clinical blood smears. According to this method, first a suitable dilution of the dispersed macrocolloid is made and the pH is adjusted to a value preferably in the range 6.5 to 7. Then high velocity magnetic stirring, sonication or homogenization is applied> to completely dissipate any weak bonds that might be present. between individual macrocolloid particles. Then a small amount (eg 8 µΐ) of the diluted, neutralized dispersion is applied to the microscope slide and allowed to dry. The sample is viewed under a known magnification using an "alignment eyepiece". The dispersed macrocolloid particles of the sample are visually compared to the mesh on the eyepiece to give a good estimate of the statistical size of oversized or aggregated particles within the population as a whole.

An alternative method of analyzing the particle size distributions is to use a computer adapted to image analysis, e.g., QUANTIMET ™ 720, from the Cambridge Institute, US. Kingdom.

The known method is based on the use of a MICROTRAC ™ particle size analyzer. General aspects of such a technique are described in the article by J. W. Stitley et al. Fri Particie Size Analysis and Characterization Using Laser Light Scattering Applications in Food Product Development, December, 1976.

In view of the present disclosures, it is obvious to those skilled in the art that sedimentation techniques may also be used to determine particle size. It is understood, however, that gravimetric techniques should take into account the protective effect of the colloid, e.g., whatever treatment agents might be used during the heat denaturation described above.

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One example of a gravimetric method for determining the percentage of "oversized" protein aggregates is provided below.

1. Prepare a 5 wt.% Dispersion of the macrocolloid according to the invention and neutralize it to a pH ranging between 6.5 and 7;

2. To the neutralized 5% macrocolloid dispersion is added high fructose corn syrup having a specific gravity of 1.351, pH 3.3, total nitrogen 0.006% and a solids concentration of about 71%, in a weight ratio of 1: 4;

3. The mixture is then homogenized to disperse loose bonds between the macrocolloid particles;

4. The mixture is then centrifuged under gravity 478 for 20 minutes at 15 ° C. The fraction of oversized protein aggregates, i.e. particles substantially greater than 2 µm in diameter, can be expressed as the percentage of the weight of protein contained in the centrifuged pellet divided by the weight of protein contained in the macrocolloid dispersion prior to centrifugation.

These studies are applicable both to macrocolloid dispersion and to protein substances useful as a raw material for the preparation of these macrocolloids. It is understood by those skilled in the art that capacity-based particle size analysis devices, such as the well-known "Coulter Counter ™" analyzer, are not suitable for this application due to the charge of macrocolloid particles at certain pH values, unless the macrocolloid is diluted with saline. (NaCl) with a concentration sufficient for the salt ions to exceed the natural charge on the macrocolloid particles.

The preferred conditions for the preparation of the macroloid, however, are that the aqueous protein solution is subjected to high temperature in a very short time at a speed of 5000 to 10,000 sec -1 or more. In the case of a drive for a 3.81 type Maring dry blender equipped with a miniature (e.g. 1 liter) "Henschel" mixer, for example, a speed of 5000 rpm has been found to provide sufficient shear force.

A preferred processing temperature range is from about 80 ° C to about 125 ° C for about 3 seconds to about 15 minutes or more, preferably from about 10 seconds to about 2 minutes. A longer treatment time at lower temperatures is used, with treatment at 80 ° C requiring 15 minutes, while treatment time at temperatures between 90 ° C and 95 ° C is approximately 5 minutes. At 120 ° C, the treatment time can only be about 3 seconds. The high processing temperatures are complemented by the increased heat transfer rates. When the nature of the apparatus allows it, it is therefore advantageous to carry out treatment at high heat transfer rates and high denaturation temperatures in a very short time. It should be noted, however, that at temperatures above 120 ° C and with correspondingly reduced product residence times, a "thinner macrocolloid" which may be less desirable is produced.

The method of producing macrocolloids uses an aqueous protein solution with a protein concentration between about 10% and 20% by weight, preferably between about 15% and 18% by weight. At protein concentrations below about 10% by weight, there is a tendency to form pulp. The fibrous masses are in the form of a stable dispersion and have undesirable organoleptic properties. Solutions with a protein concentration much greater than about 20% by weight have extremely high viscosities and thus prevent the application of the required shear rate on the protein solution.

The aqueous protein solutions may still contain up to 100 parts by weight (protein) or more of a polyhydric compound, preferably a mono- or disaccharide. These compounds can be present as natural components of protein raw materials (e.g. lactose in sweet milk whey protein concentrates) or they can be added to the solution prior to the denaturation process. Preferred polyhydric compounds include reducing sugars such as lactose, fructose and maltor, preferably lactose. Suitable non-reducing sugars include sucrose and lactitol.

The high shear forces applied during processing are believed to prevent the production of large aggregates of denatured protein during denaturation. Optionally, aggregation inhibitors can be added to the aqueous solutions to facilitate formation of the desired product. Such an aggregation inhibiting agent is selected or its concentration adjusted so as not to alter the pH of the mixture in turn beyond the optimal range for the treatment. Suitable aggregation inhibiting agents include hydrated anionic agents such as xanth gum (usually 0.1% to 1.0%

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By weight and protein concentrate), "datem esters" (0.5% to 2.0% by weight of the protein concentrate, although these esters contribute to the tastelessness and odor of the final product) and lecithin (1% to 10%). % by weight of protein concentrate). Other suitable aggregation inhibiting agents include carrageenan, alginate, and calcium steroisolactate.

Maltodextrins, produced by enzymatic or acid hydrolysis of starch, are another chemical aggregation inhibiting agent useful in the method of vanazine. The preferred concentration ranges from 10 to 50% by weight of the protein concentration. These substances are believed to result in a saving of protein like high fructose syrups, although syrups are not as effective in this application. These inhibitory agents are hydrocarbons and thus are a source of calories, a factor that may prevent them from being selected for use in the manufacture of reduced calorie food products.

Another suitable aggregation inhibiting agent is pectins from plant resins. Lemon pectin is preferred for a fruit flavored product, while "pure tasting products, such as the cream, vanilla ice cream type, preferably should contain pectin derived from sources other than lemon, e.g. apple pectin. Also, if the final product or cream substitutes contain calcium (dairy products), the pectin used as an aggregation inhibitor should not gel in the presence of calcium.

Hydrated lecithin and hydrated xanthan gum are examples of the different activities of the inhibitory agents. Both give the final product a mouth-feel. Lecithin, however, being somewhat more effective as an inhibitory agent, gives slightly larger mean dimensions of the colloidal particles. In contrast, the particles produced with the xanthan agent are smaller and smoother. Both have a whitening effect on the final product resulting from the fact that they assist in the formation of a homogeneously dispersed system, thereby increasing the light scattering effect which is perceived as white color. Combinations of aggregation inhibiting agents also have useful features. Preferably a combination of pectin and lecithin is used in the preparation of the creamer-egg white / casein micelles.

Typically, other optional additives such as salts and end product ingredients including suitable flavors, colors and stabilizers may be present or added to the solution without being detrimental. In many cases (i.e. where the nature of the additive and its effect on the protein solution is allowed for) it may be particularly desirable to incorporate such end product components into the protein solution to avoid the need for additional pasteurization steps after primary processing.

The protein raw materials can optionally be treated to remove cholesterol, fat and other impurities that can impart a bad taste to the macrocolloid product. One such method comprises an extraction step in which the proteinaceous substance is contacted with a food grade solvent, preferably ethanol, in the presence of a suitable food grade acid. The protein material is then washed several times and filtered to purify the extracted protein product.

Suitable solvents include lower alcohols, hexane or the like, preferably ethanol. Suitable food grade acids include mineral acids such as phosphoric and food grade organic acids such as acetic, citric, milky and malic, particularly preferred is lemon.

When the heat denaturation process is complete, the product may optionally be homogenized. Such treatment is needed for a diluted (i.e. low protein concentration) and / or neutralized product such as e.g. coffee bleaches. This treatment is useful to break relatively loose intramolecular bonds that accidentally form during the product manufacturing process. If not aggregated (i.e. not assembled into particles substantially greater than 2μιη), those macrocolloid particles that are associated with each other (i.e. usually doublets or triplets) are however organoleptically perceived as single complex particles which cannot be distinguished from aggregates based on the sensations they cause in the mouth. Homogenization divides tc associations of particles into individual macrocolloid particles with the desired organoleptic characteristics. Homogenization of dilute products with a low macrocolloid concentration (e.g. coffee bleaches) is preferably carried out at a pH of 6 to 7. At these pH values, the distribution of electric charges on the surfaces of the macrocolloids helps to maintain

160 671 smooth dispersion of macrocolloids in an aqueous medium. During conventional homogenization, care should be taken not to expose the macrocoid particles to elevated temperatures as they may aggregate them into larger particles.

Particle size studies provide a measure of the organoleptic properties of the products produced by the process of the invention. One of the simplest and fastest techniques is to prepare an optical preparation in a way analogous to the preparation of clinical blood smears. According to this method, 10 g of a paste-type food sample is weighed into a Waring blender and 190 g of distilled water are added to make a 5% solution. The solution is then mixed at high speed for 2 minutes and the pH is then adjusted to 6.75-7.0. The sample is then subjected to high speed magnetic stirring while being sonicated for 1 minute using a probe acoustic generator (Braunsonic Model 2000 Sonicator, Burlingame, CA). In this way, any weak bonds that may exist between individual macrocolloid particles are broken. The solution is then diluted with deionized water to a concentration between 0.25% and 0.50%, depending on the concentration of the particles. This solution is then placed in an ultrasonic bath (Branscn 2200 Ultrasonic Bath, Shelton, CN) for 1 minute immediately prior to preparation of the formulation.

After shaking by hand for 10 seconds, 20 µm of the sample prepared as above is placed in the center of a microscope slide and placed in a Corning "slide spinner". The slide is centrifuged immediately after placing the sample on it. Once the slide is dry, usually within 30 seconds, it is ready for microscopic evaluation. The sample is observed under a Zeiss Axiomat Microscope equipped with a halogen light source (Zeiss, Thornwood, NY) and a Daga MTI video camera (Michigan City, IN) and camera control with a 50Χ lens and under a total magnification ranging between 1000 and 1600. This system is only suitable for qualitative analysis of particles having diameters greater than about 0.25 µηι. For this reason, all statistical particle measurements in this specification, unless otherwise stated, are for particles whose larger dimensions exceed 0.25 µm. However, particles with a size between about Ο, ΙΟμπι, and about 0.25μηι can also be seen and their presence detected by the usual method. Multiple fields (15 to 25) are then selected to subjectively evaluate all dimensions and shape of sample homogeneity / heterogeneity. Then, for the qualitative evaluation of the sample, the field that is most representative of the entire sample is selected. This image is projected onto a black and white high resolution TV monitor (Lenco, Jackson, MO) for quantitative analysis.

The image on the TV monitor is first digitized and then translated from the TV monitor to the computer monitor. During this digitization / translation step, the image is somewhat reduced with the side effect that some particles that were separated in the original image have fused together and therefore do not represent real particles. These fused particles are carefully corrected by comparing the old image (TV monitor) with the new image (computer monitor).

Typically 250 50 particles are measured in approximately one field. Fields are selected to include 500 particles for evaluation. Initially, the number of particles in the image is determined together with their respective lengths and widths. From these data are calculated, two additional variables, equivalent spherical (ES) diameter and volume, the following method: ES Diameter = (B ² XL) ^{1 '3.} ES Volume - 4 / 3π b2l. B means width and L means length.

Once the ES Diameter and Volume are determined for the entire particle distribution in the image, weighted (Dn) and volume weighted (D _v ) mean ES diameters are calculated. D _n is the average particle diameter which is calculated by summing the diameters of all particles in the distribution and dividing by the total number of particles. D _v (volume weighted mean diameter) is the weight of each particle relative to its volume, which indicates where the mean diameter lies with respect to volume or, therefore, with respect to weight. The maximum diameter (D _mM ) is simply the diameter of the largest particle present in the microscopic field.

This data can be plotted as a histogram with the E. S. diameter on the abscissa as a function of particle number as well as particle volume. From this data, it is also possible to directly determine the volume percentage of the particles above 2 µm as well as the maximum particle diameter.

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The method of the invention produces spheroidal particles by coagulating or denaturing a readily coagulating protein (preferably a protein that coagulates at or below 85 ° C), such as egg white protein (EWP), in the presence of a nucleus, the denatured, coagulating protein surrounds and encloses the nucleus, resulting in spheroidal particles of the core / shell configuration, in which the core is a nucleus and the coating is a denatured coagulable protein. The nucleus or nucleus may occupy less than 90% of the volume of the produced spheroidal particle, and typically less than about 50% of the volume of the particle.

The production of the particles can be carried out at nearly neutral pH, ie above the midpoint of the protein's isoelectric curve, when the protein is denatured in the presence of a seed. Proteins which will denature into macrocolloid particles are those which coagulate readily, i.e. egg white proteins. Casein micelles (NA) are used as crystallization seed.

Egg white protein is used as the coagulant protein to produce core / shell particles. Egg white protein / nucleus particles ("EWP" / "NA") according to the method of the invention are prepared by treating EWP in the presence of a nucleus at the elevated temperature and shear conditions described herein. The midpoint of the egg white protein isoelectric curve is a pH of 4.5 to 5.5, however, the pH in the denaturing medium can be raised above this point to a value between about 6 and 7, and preferably to a value between about 6.2 and 6. 6. The total protein content of the treated mixture typically ranges between about 5 and about 20% by weight. Polyhydric compounds (lactose) and aggregation inhibiting agents can also optionally be used.

In a preferred embodiment of the method according to the invention, spheroidal protein particles are prepared from a combination of egg white protein and a source of substantially non-aggregated or native casein micelles as a crystal seed. They are prepared by heating a mixture of egg white protein and a source of casein micelles under the shear conditions described above. Protein particles can also be produced at a pH greater than the isoelectric point of the egg white protein (see Example 1).

Casein micelles, which constitute the nucleating agent, are naturally occurring spheroidal protein particles found in the milk of mammals, typically 0.1-0.4 µm in diameter. Any source of casein micelles can be used in the process of the invention, but cow's milk is preferred due to the high concentration of casein micelles. Skim milk, condensed skim milk, and ultra-filtered skim milk are particularly preferred because they contain a reduced amount of fat which is undesirable in fat / creamer applications.

The total protein content of the reaction mixture subjected to heating and shear during the preparation of EWP / CM particles typically ranges between about 15 and about 20 wt%, but neither the total protein content nor the ratio of egg white protein to casein micelle protein are critical. Egg protein typically makes up from about 25 to about 99% of the total protein content, while the source of the casein micelles may be from about 1 to about 75% of the total protein, preferably from about 1 to about 40%. Preferably, concentrated egg white and a concentrated source of casein micelles are used. Thus, the preferred sources of egg white are freeze-dried egg proteins and ultra-filtered egg white, while the preferred sources of casein micelles are condensed skim milk and ultra-filtered skim milk.

EWP / CM protein particles are preferably prepared in the presence of a polyhydric compound and an aggregation inhibiting agent, both described above. A preferred polyhydric compound is a combination of sucrose and lactose (from condensed skim milk), and a combination of lecithin and pectin is preferably used as the aggregation inhibiting agent. Food grade acids can be used to adjust the pH, and water can be used to adjust the concentration of the ingredients. When ultrafiltered egg white and condensed skim milk are used to produce EWP / CM protein particles, a typical reaction mixture may have the following composition: ultrafiltered egg white protein 40-60 wt% (providing 8-12% of the total weight of the mixture) condensed skim milk -10-33% by weight (providing protein in an amount of 1-4% of the total weight of the mixture), cane sugar or glucose obtained from corn starch - 0-10% by weight, pectin comes from10

160 671 of vegetable - 0-0.5% by weight, lecithin - 0-1.0% by weight, food acid -0-0.3% by weight (to adjust the pH to 6 to 7) and supplementary water up to 100%.

Figures 1 and 1A show a preferred embodiment of a method for producing EWP / CM protein particles providing a fat replacement agent in accordance with the invention. The time, temperature, pressure, and pH conditions for each step are shown in Figures 1 and 1A and are identified by letters in circles in the diagram, respectively. In this embodiment, sugar and a resin-type aggregation inhibiting agent such as pectin or guar are dry mixed in a conventional dry mixer 1 and a premix is prepared A. The pasteurized liquid egg white is ultrafiltrated in a conventional ultrafiltration (UF) equipment. 3, preferably with a polysulfone membrane with a nominal molecular weight of about 10,000, which gives a concentrated egg white (pre-preparation B) with a protein content of 15-25% by weight. The lecithin is rehydrated in purified water (by reverse osmosis) in a vessel under vacuum 5 with good agitation and a premix C is prepared. A food grade dilute acid solution such as lactic acid or citric acid is prepared using purified water (Premix D) .

Premix A is rehydrated in purified water using a high shear mixer for continuous or batch operation 2. Pre-formulation B is added to the hydrated premix A and skimmed condensed milk in a sanitary batch 4 tank to bring the protein concentration to the desired level. i.e. 10-20% of total protein. Masterbatch D is added to the batch tank to adjust the pH to a value in the range between 6.0 and 7.0, preferably 6.2-6.6. Premix C is added to the reservoir to form a protein solution 11 which is heat treatable under shear conditions to form EWP / CM protein particles suitable for use as a fat / cream premix.

The produced protein solution 11 is vented in the sanitary vent 6 to minimize dispersed and dissolved oxygen. The shear heating process may be carried out in one high shear heating device, but is preferably carried out in two devices, a preheater 7 and a high shear heating device 8. A preheater is used to raise the temperature of the resulting solution proteins to 48-77 ° C, preferably to 60-74 ° C, so that the increase in temperature in the apparatus 8 leads to an outlet temperature suitable for pasteurization, i.e. 80-85.5 ° C, in accordance with the guidelines of the United States Food and Drug Administration America (FDA). The material exiting the high shear heat exchanger 8 is cooled in a conventional heat exchanger 10 to a temperature of 1.5-4.5 ° C in a few minutes. The resulting EWP / CM protein macrocolloid particle product is suitable for use as a fat or cream substitute. The above-described process for producing EWP / CM protein particles is preferably performed next to the foodproduct production line, which allows a creamer substitute to be introduced into the formulation line. Alternatively, if the produced material is to be stored for later use, a tubular pasteurizer 9 is introduced into the process between the high shear device 8 and the chill heat exchanger 10, and thus the product can pass through the pasteurizer 9 in sufficient time to pasteurize the creamer substitute. EWP / CM. After pasteurization, the product is cooled and stored at 1.5-4.5 ° C.

When the apparatus described in the aforementioned US Patent Application No. 127,710 is used as the high shear heat exchanger 8, a rotor blade rotation speed in the range between 3000 and 10000, preferably from about 5000 to 7500 rpm is sufficient. to produce a product that has the texture and flavor of heavy cream (fat).

Examination of electron micrographs suggests that EWP / CM protein particles are primarily particles that have an inner core of casein micelles and an outer shell of denatured egg white protein. A minor portion of the protein particles are denatured egg white particles and agglomerated casein micelle particles. In some cases, more than 1 casein micelle may be found in the coagulated protein particle.

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2, it can be seen that the EWP / CM 21 protein particles have a core of one or more casein micelle particles 23 (visible as dark elements inside the particles) and a coating of denatured egg white protein 25 (visible as the lighter outer part of the particles). The EWP / CM protein particles shown in Figure 2 were prepared using essentially the same method as described in Example 1 below. Figure 3 shows EWP / CM 31 protein particles that were produced by an in situ process. It is noteworthy that in Figure 3 the denatured EWP coating 35 typically occupies less total volume relative to the casein 33 micelles than in the EWP coating of the particles shown in Figure 2. The core / shell configuration of the protein particles is more clearly seen in Figure 4, which is a micrograph of a frozen dessert using a cream substitute according to Example 1. The different particles show the casein micelle core 41 clearly, and the lighter, less dense coating 43 of these particles is denatured EWP. Fig. 4 shows casein micelles 45 which do not have an EWP coating. Figures 2-4 can be compared with Fig. 5, which shows an electron micrograph of super premium ice cream (16% milk fat). In Figure 5, the relatively large white circles 51 represent fat globules and the small dark elements 53 are casein micelles.

The EWP / CM protein particles form a macrocolloid that is useful as a fat / cream substitute for making frozen desserts, and in addition to mousses, sauces, cupcake fillings, icings, and similar foods that normally contain cream. The EWP / CM macrocolloid, replacing cream in these products, is introduced by replacing cream with it during the manufacturing process of these products. Typically EWP / CM cream substitutes for fat cream in a 1: 1 wet ratio. This means replacing about 3g of fat / cream with about 1g of protein as the cream substitute contains water, polyhydroxy compounds, aggregation inhibitors and other ingredients. The optimal amount that can be used in a food product can easily be determined by the person skilled in the art through an organoleptic evaluation.

EWP / CM protein particles which have a fat / creamy mouthfeel typically from about 0.1 µm to about 3 µm in diameter, preferably from about 0.5 to about 2.5 µπι average diameter. In frozen products, the EWP / CM particles should be present in an amount of at least 1 X 10 ⁸ particles per cm ^{3 of the} final food product, preferably in the range between 1 X 108 and 1 X 10 ¹² / cm ³ or more.

The following examples illustrate the preferred methods of making the macrocolloids of the invention.

Example 1 relates to a preferred method of producing a substitute made of egg white and casein micelles. Example 2 is a frozen dessert that contains a cream substitute according to Example 1 in place of a fatty creamer. Example III relates to the optimization test of the used product according to Example II for cream-ice cream products. All these examples do not limit the scope of the invention.

Example 1 The following ingredients were used to prepare a cream substitute from egg white and casein micelles as described below:

Table l

Ingredient Weight percent (%) Comments Ultrafiltered egg whites 55.00 Share of 9.35% (17% protein) total weight of the mixture Condensed skim milk 22.65 Share 2.50% (11% protein) total weight of the mixture Lecithin 0.30 Sugar 5.00 Pectin (from apples) 0.35 Citric acid 0.17 To adjust the pH to 6.6 Water 16.53

100.00

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Stage A: Initial preparation.

Sugar and pectin were dry-mixed (Premix A). Pasteurized liquid egg white was ultrafiltered in a Dorr-Oliver Series S series ultrafiltration system with a polysulfone membrane, and ultrafiltered egg white was obtained with a protein content of 17% (Pre-preparation B). The lecithin was released using purified water by reverse osmosis in a STEPHAN vertical mixer / cutter model VCM 12 R and D (Masterbatch C). The prepared dilute solution of citric acid in purified water by reverse osmosis (Premix D).

Step B: Preparation of the ingredient pack.

As shown in Figures 1 and 1A, the sugar-pectin blend (Premix A) was hydrated in reverse osmosis purified water in a TRIBLENDER high shear mixer. Ultrafiltered egg whites (Pre-formulation B) and condensed skim milk were added to the hydrated sugar-pectin mixture in the set operation vessel under hygienic conditions, bringing the protein concentration level as shown above. Sufficient dilute citric acid (Premix D) was added to the mixture to adjust the pH of the mixture to 6.6. In order to complete the composition of the recipe, hydrated lecithin (Masterbatch C) was added to the mixture. The mix was deaerated in a D-16 VERSATOR deaerator to reduce dispersed and dissolved oxygen.

Stage C: Heat treatment.

The mixture was pumped into a set of heat treatment equipment where it was pre-heated to a temperature between 48.8 ° C-71.7 ° C prior to the heat treatment process. The mixture was then passed through the pipeline into the fluidization equipment described in US Patent Application 127,170, filed December 2, 1987, at a rate of 54,432 kg / hr. and at a temperature of 80 ° C-87.7 ° C. The stirrer speed of the device was set at 5000-7500 rpm in order to obtain a micronized protein product from egg white / casein micelles (EWP / CM) with the desired cream texture. The average residence time of the blend in the fluidizing equipment was approximately 30 seconds. The produced fat substitute was used directly to enter the technological line for the production of frozen milk desserts. When the frozen dairy dessert production process was complete, a tubular pasteurizer was used to pasteurize the fat substitute egg white / casein micelles according to FDA recommendations, i.e. 80.55-87.8 ° C / 25 seconds. The pasteurized fat substitute was then chilled to 1.66-4.4 ° C and stored at this temperature until use.

Example II. The fat substitute egg white protein / casein micelles prepared according to Example 1 was used as a fatty creamer ingredient in the preparation of a vanilla-flavored cream ice cream dessert. The frozen dessert was then assessed by a group of people in terms of its creamy texture and overall quality. Another group of people assessed the three commercial varieties of cream vanilla ice cream. All the creaminess ratings (creaminess, fatness, smoothness) showed that the frozen dessert product fully falls within the commercial grade ratings, both at the beginning and after 5 days of storage.

Example III. A study was carried out to optimize the amount of the protein fat substitute as well as the casein micelle of Example 1 required in the frozen dessert to obtain a texture similarity to that of a "super premium" cream ice cream containing about 16% milk fat. The best frozen dessert was made with the following set of main ingredients, shown in Table 2.

Table 2

Ingredient Weight percent (%) Total protein 9.72 Saccharose 11.4 EWP / CM fat substitute according to example I. 31.84 *

* Makes 38.8% of total protein

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It can be readily seen that the optimal amount of the fat substitute, egg white protein / casein micelles according to Example 1, which resembles super premium ice cream, is about 32% of the weight of the frozen dessert product. It is also apparent to the skilled person that the optimal amount of the fat substitute for a given application will vary depending on several ingredients such as e.g. type of food product, desired creaminess, protein content of the fat substitute - egg white protein / casein micelles, particle size micronized protein, presence or absence of aggregation inhibitors, polyhydric compounds, etc. Typical sensory studies were performed to determine the preferred formulation for each food group.

Typical ice cream desserts recipes using the fat substitute, egg white protein / casein micelles according to Example 1 contain the ingredients listed in Table 3 below.

Ta b e 1a 3

Ingredient Weight percent (%) Range Beneficial EWP / CM fat substitute according to example I. 25-40 31.8 UF skim milk (4x) 25-40 36.6 Solid non-fat milk 0- 3 1.6 Sugar 8-20 10.0 Egg yolk 0- 2 0.9 Stabilizers 0- 1 0.4 Solid corn syrup 0-10 8 Starch 0- 1 0 Flavoring agents * at your discretion 1.1 Water in a supplementary amount in a supplementary amount

* May contain fatty cream or fat as a carrier for fat-soluble agents

It is readily noticed that the improved whipped frozen dessert products described above with reference to the illustrative "ice cream" recipes are products that are physical and organoleptic in nature to full-fat products but have substantially lower caloric value and improved nutritional properties (i.e. high protein content). While the above exemplary ice cream cream formulation contains sucrose as a sweetening agent, it is evident that alternative sweeteners such as aspartame, alitame, acesulfame K, and sucrose (with appropriate bulking agents if necessary) can be used.

Likewise, although in the above recipe total milk fat has been replaced by a protein macrocolloid substitute, it is obvious that high quality products can also be made which include frozen desserts in which the macrocolloid only replaces a portion (e.g. 50%) of the usual fat and / or oil . Also, although only "cream ice cream" products are illustrated, it is also possible to advantageously produce reduced fat or fat free whipped frozen desserts (i.e. containing less than 1% fat) such as milk ice cream, creams, sorbet etc. as well as icings, pastes, spreads, sauces, dips, mousses, cupcake fillings, and similar foods that typically contain cream.

In practicing the method according to the invention, various modifications and changes are possible, which can be made by those skilled in the art from the above description of the preferred embodiments, with the limitations of the appended claims.

Claims (5)

A method for producing a cream substitute consisting of substantially non-aggregated spheroidal macrocolloid protein particles comprising a casein micelles core and an outer shell of denatured egg white protein, characterized by heating the egg white protein and a source of substantially non-aggregated micelles casein, at a pH ranging between about 6.0 and about 7.0 under shear conditions sufficient to form macrocolloidal casein particles surrounded by denatured egg white protein, optionally in the presence of a polyhydric compound and an aggregation inhibiting agent. 2. The method according to p. The process of claim 1, wherein the egg white is ultrafiltered egg white and the casein crumb source is condensed skim milk or ultra-filtered skim milk. 3. The method according to p. A compound according to claim 1, characterized in that the polyhydric compound is sugar, corn sugar, lactose or a mixture thereof, and the aggregation inhibiting agent is pectin, lecithin, xanthan gum, guar gum, date esters, carregenin, alginate, maltodextrin, calcium steroyl lactate or their calcium silicate. mixtures, especially sugar, lactose or a mixture thereof are used as the polyhydric compound, and a mixture of pectin and lecithin is used as the aggregation inhibiting agent. 4. The method according to p. 2, characterized in that the heat treatment is carried out at a temperature of Otot 8 ⁰ ° C ^{d k} oo O ^L O ^I n ^ st zastosowamu here ^COG shear of about ⁵⁰⁰⁰ to ⁷⁵⁰⁰ sec ^-1. 5. The method according to p. The method of claim 2, characterized in that the egg white protein and the source of non-aggregated casein micelles are heated, the protein: casein micelles weight ratio used is 1.5-99.