DD283557A5 - METHOD FOR PRODUCING A HATCHED ICE DENSITY WITH LOW CALORIE CONTENT - Google Patents

Abstract

The invention relates to a process for producing a low calorie battered ice desserts in which the fat and / or OEl contained therein is partially or completely replaced by a macrocolloid consisting essentially of non-agglomerated particles of denatured protein. The reduced-calorie, low-fat reduced-calorie ice-cream analogues obtained by the process of the present invention have increased nutritional value due to the increased protein content and also the physical and organoleptic properties of whole-fat ice creams. manufacture; Eisdesserterzeugnisse; low in calories; reduced fat; proteinaceous macrocolloid; Ice cream analog products}

Description

For this 4 pages drawings

Field of application of the invention

The present invention is applied in the field of food chemistry. It generally relates to processes for producing fat-free and reduced-fat products having the organoleptic properties of whole-fat products, and more particularly to frozen dessert products such as ice cream and related frozen dairy desserts.

Characteristic of the known state of the art

"Frozen desserts" is a term used to refer to a wide variety of products, including ice cream, frozen egg crust, ice milk, sorbet, water ice, milk ice confectionery, ice cream confectionery, frozen dietary dessert, mellorine and non-dairy dessert, all according to the Frozen desserts that are not Federal standards include ice cream puddings, mousses, and ice shakes, and frozen dairy desserts have minimum standards for milk fat and / or milk solids. For example, ice cream may not contain less than 10% milk fat and 20% total milk solids (composed of total milk fat and non-fat milk solids, "MSNF"); ice milk must contain from 2 to 7% milk fat and not less than 1% total milk solids, and sorbet must contain 1 to 2% milk fat and 2 to 5% total milk solids, see generally Redfern, RS, and Arbuckle, W: S, "Lee Cream Technology Manual", 4th Edition, 1985, Redfern & Assoc. Ltd., Raleigh, North Carolina 27622, the contents of which are incorporated herein for reference for purposes of illustrating the field of application of the invention.

Ice cream and other whipped frozen dairy desserts are rather complicated foam feeds consisting of air bubbles surrounded by a partially frozen emulsion in which ice crystals and solidified fat globules are embedded in the unfrozen water phase. The estimates of the size of the coarsely dispersed structural components of ice cream are different. For ice crystals sizes between 20 and 60pm in diameter and an approximate distance of 7 μιπ are given; the size of the air cells is specified between 10 and 175 μm at a distance of about 125 μm; and the size of solidified fat globules is reported as 0.2 to 2.0 цt, forming agglomerates that form a "skin" around the trapped air cells See "Fundamentals of Dairy Chemistry", 2nd edition , 1983, Webb, BH, et al., Eds., Avi Publishing Company, Inc., Westport, Connecticut, pp. 896-913, the contents of which are incorporated herein for reference for purposes of illustrating the field of application of the invention.

It is well known that the fat content of frozen dairy desserts plays an essential role not only in the body and the structure of the product, but also in its taste properties. The suppleness of the structure of ice cream is essentially inversely proportional to the average size of the ice crystals. In fact, in all frozen dessert compositions, an increase in milk fat content causes both a reduction in the size of the ice crystals and a decrease in the spacing between the crystals. Despite the expense and high calorific value associated with the use of milk fat, and despite the susceptibility of milk fat to oxidation, which can lead to undesirable flavors, and its tendency to form foam or butter-like structural effects, whatsoever full-fat food products are generally preferred to ice milk, sorbets and the like are highly preferred. In fact, the so-called "premium grade" ice cream varieties are essentially characterized by having 15 to 18% higher milk fat content than that of the standard, and are produced as a product of correspondingly higher friability and smoothness and improved body and structure compared to ice cream and cream Dairy products of standard quality with lower fat content called.

While attempts have been made to develop formulas for frozen dessert products in which some or all of the milk fat content normally present is replaced by a non-fat material, none of the products so produced has been accepted with substantial success as a substitute for a whole-fat ice cream or whole-fats milk. See, for example, U.S. Patent No. 4,510,166 to ice cream recipes in which starch gels have been proposed as a fat replacer, and U.S. Patent Nos. 4,421,778 and 4,552,773 to foam feeds employing crystalline fats tending to beta phase. See also British PS915389 and U.S. Patents Nos. 3,510,316,355,683,4400,405 and 4,631,196.

Object of the invention

The process of the invention provides fat-free and reduced-fat frozen dessert products having the physical and organoleptic properties of full-fat frozen dairy desserts.

Ideally, such products would equal or exceed the nutritional value of standard frozen food products, but should have a lower calorific value. There is also a need for a fat or cream substitute ingredient that can be manufactured, stored and used in the preparation of a variety of low / no fat foods, including frozen foam desserts.

Explanation of the essence of the invention

It is an object of the present invention to provide a process for producing fat-free and reduced fat frozen foam products in which part or preferably all of the milk fat, vegetable fat or oil contained therein is replaced by a proteinaceous macrocollide consisting of denatured protein particles. Products according to the invention have the physical and organoleptic properties of whole fat products, although fat / oil droplets or globules are absent or substantially reduced in content, which is known to play a critical role in the formation of air cells and the development and maintenance of air cells Ice crystals play a small average size in frozen foam desserts. The ability to replace fats or oils partially or wholly with proteinaceous macrocolloids allows the preparation of highly desirable reduced calorie products but very high nutritional content due to the presence of additional protein. The preparation of frozen dessert products of the invention does not require devices or methods other than those normally used in the preparation of frozen dairy desserts, and the proteinaceous macrocolloid may in all cases be incorporated into the dessert formulas as a direct substitute for milk fat or vegetable fats or oils. Thus, the present invention provides improved frozen foam dessert foods in which the improvement is that fat in the premixed compositions is partially or completely replaced by a macrocollid of substantially uncompacted particles consisting of denatured protein having an average particle diameter of about 2.0 цt in the dry state, wherein less than about 2% of the total number of particles exceeds a diameter of 3.0 ц t and wherein the majority of said particles is generally spherical, as evidenced from about 800 times magnification under a standard light microscope, and these Particles in the hydrogenated state form this macrocolloid having a substantially smooth, emulsion-like organoleptic character. Preferred products of the invention are frozen foam desserts of the type that would normally contain milk fat, and wherein the protein macrocolloid completely replaces the normally present fat, yielding, for example, ice cream analogous products having the physical properties and organoleptic character of top quality ice cream products contain less than about one percent fat.

Presently preferred proteinaceous macrocolloids for use in the practice of the invention are derived from undenatured, substantially soluble proteins derived from animal, vegetable and microbial sources, whey, protein albumin, soybean oil and bovine serum albumin protein sources being presently most preferred. Desirable macrocolloids include those described in U.S. Patent 4,734,287 to Singer et al. a. and in US patent application serial no. No. 127955 of December 2, 1987, which is a partial continuation of said US Patent, both of which are incorporated by reference. Macroccolloid products for use in the practice of the present invention are conveniently prepared by the use of a device such as disclosed in U.S. Patent Application Serial No. No. 127710 of December 2, 1987 to Singer et al., Which is owned and related to and entitled "Fluid Processor Apparatus," the disclosures of which are expressly incorporated herein by reference However, they may also be made using any suitable device which can apply controlled heat and high shear conditions to the protein solution used as the starting material which is subjected to the macrocolloid-forming treatment When used in an ice cream dessert according to the present invention, and if the cholesterol and lipid content of the proteinaceous starting material is to be reduced, a pretreatment may be carried out by the methods described in the commonly owned US Pat United States patent application, serial no. 127402, dated December 2, 1987 by Singer et al. entitled "Methods for Extraction of Cholesterol and Lipids", which is incorporated by reference in the present application.

In another aspect, the present invention provides novel methods for the preparation of reduced calorie ice cream products, in particular dairy products such as ice cream, ice milk, sherbet and the like, which include the step of replacing fat and / or oil normally present in the Product by a preformed proteinaceous macrocolloid as described above. Preferably, at least 50% of the fat and / or oil is replaced and, at best, this ingredient is replaced in its entirety leaving a fat content consisting essentially only of the fats present in standard flavoring agents such as cocoa or other fatty ingredients such as egg yolk solids frozen egg products.

In another aspect, the present invention provides for the preparation of calorie-reduced, battered ice cream products using non-fat or substantially fat-free premixes, including heat coagulable protein sources such as egg white, whey protein, soybean oil protein, and the like. After subjecting these premixes to a heat treatment (e.g., pasteurization treatment) and relatively high shear mixing prior to freeze processing, particles of denatured protein are formed in the mixture in situ and the particles so formed act as a replacement for the FetWoI beads in the manufacture ice cream product. Premixes made according to the invention are characterized by a protein content of between about 5% and about 20% (and preferably between about 7.5% and about 12.5%), with about 25% to about 100% (and preferably about 50%) of the total protein incorporated from heat coagulatable protein. It has been found that the pasteurization in the continuous process at high temperatures over a correspondingly shorter time (eg 20 to 25s at 176 ⁰ C [80 "C]) gives the best end products.

Whether prepared by the direct incorporation of macrocolloid materials or by the in situ formation of protein particles in a masterbatch, preferred battered ice cream products of the invention preferably contain denatured protein particles in the size range of from about 0.01 to about 3.0pm (and preferably about 0.1 цt up to about 2.5 μιη) in diameter, with particles having a diameter in the range of about 0.5 цt up to 2.5 цt in amounts of at least 1 χ 10 ⁸ particles / cm ^{3 of} the final product , In general, it is preferred that between 1 × 10 ⁸ and 1 × 10 ¹² or more such particles are present, and it is best if more than 1 × 10 ^{9 of} such particles are present, whereby the final products of the full fat products in terms The creaminess, suppleness and structure are the closest.

It is therefore within the scope of the present invention to prepare fat-free or substantially fat-free premixes for whipped ice desserts containing 5 to 20% protein, with heat coagulatable between 25% and 100% of the total protein content, and these premixes of heat pasteurization and a high shear mix In order to form in these a population of at least 1 × 10 ⁸ particles / cm ^{3 of} denatured protein particles having a diameter from 0.5 to 2.5%. Thus prepared premixes, after "completion" in an automatic ice cream disperse ice freezer, give ice cream analog products having the structural properties of full fat ice cream, ice milk and the like.

According to another aspect of the present invention, a cream substitute ingredient of coagulatable protein such as egg white and a nucleating agent such as casein micelles, e.g. By heating the egg whites and casein micelles under shear conditions to provide substantially uncompacted, denatured protein macrocolloidal composite particles, which particles are substantially spherical and have an average particle size distribution which gives an emulsion-like, organoleptic appearance when taken orally, d. that is, between about 0.1 and about 3.0 macrometers in diameter, with less than about 2% of the total number of particles exceeding 3.0 in. diameter. These protein particles, when hydrogenated, form a macrocolloid having a substantially smooth, emulsion-like organoleptic character, ie, a greasy or creamy mouthfeel, and when viewed in cross-section, can be seen to consist of a "core" of nucleating material and a " Shell "consist of coagulatable protein. The coagulatable protein / nucleating agent ingredient is used as a fat / cream substitute for making low or no fat fat whipped desserts and may also be used as a cream substitute ingredient in the manufacture of other low or absent fat food products such as sauces, cream pie fillings, dips, Spreads, mousses and glazes, to be used.

Other aspects and advantages of the invention will be readily apparent from consideration of the following detailed description of illustrative embodiments.

In the drawings show

Figures 1 and 1A are a schematic flow diagram of the method that may be used to prepare a protein / casein micellar cream substitute ingredient according to the present invention; Fig. 2 is an electron micrograph showing the macrocolloidal protein protein / casein micelle particles, the majority of the particles having a casein micelle core and an outer shell of denatured protein protein; Fig. 3 is an electron micrograph depicting the macrocolloidal protein protein Z-casein micelle particles formed during the in-situ process of preparing a whipped egg desserts as described below; Fig. 4 shows an electron micrograph of an ice cream analog product containing protein protein / casein micellar macrocolloid as a substitute for fatty creams, and

Fig. 5 an electron micrograph of an ice cream of the highest quality.

All micrograins have a magnification of 32,000 and they contain a reference standard of 1 micron. Detailed description:

In accordance with the present invention, it has been found that proteinaceous, water-dispersible macrocolloids, which can be prepared from a variety of proteinaceous substances and which in the hydrogenated state have a substantially smooth, emulsion-like, organoleptic character, as fat and / or oil substitutes in whipped ice cream products how ice cream can be used. The proteinaceous, water-dispersible macrocolloids consist essentially of non-agglomerated denatured protein particles characterized by having, in the dry state, an average particle diameter distribution between about 0.1 micron and about 2.0 цt, wherein less than about 2% of the total number of particles exceeds 3.0 microns in diameter. The particles are also characterized as being generally spherical when viewed at about 800X magnification under a standard light microscope.

The macrocolloid materials can be prepared by controlled denaturation from a wide variety of proteinaceous starting materials which are substantially water-soluble and substantially undenatured prior to processing.

The particularly desirable organoleptic qualities of the macrocolloid substances used in accordance with the present invention depend primarily on the size and shape of the macrocolloid particles. In particular, it has also been found that dispersions of larger, denatured protein coagulates (i.e., more than about ЗЗt dry in diameter) give an undesirable, chalky or chalky mouthfeel. This type of mouthfeel may be identified as a less crude variation of the grainy mouthfeel of known, heat denatured proteins (about 15-175K t). It appears as if a well-defined threshold of perception is exceeded as the number of particles of protein coagulum with diameters greater than about 2 to 3 цt increases in the largest dimension.

Also important is the shape of the particles. Fibrous particles generally greater than about 5 microns in length and generally less than about 1 square in diameter produce a slurry that is smooth but dilatant; As more force is applied between tongue and palate, the feeling of a solid substance is increasingly perceived. The resulting impression is not kremartig. If the fibers become shorter and approach more of the spherical shape, this impression is reduced.

Additionally, particles that are generally spherical tend to give a smoother, more emulsion-like perception. If an increased level of macrocolloid particles is generally spherical or if the macrocolloidal portions are perfectly spherical, it is possible that a slightly greater proportion of the particles may have a diameter greater than about 2 цt, without adversely affecting the organoleptic character of the mochrocolloid mixture effect. However, as already indicated above, rod-like particles with a diameter of more than about 1 micron tend to cause a calcareous to powdery mouthfeel.

Particle sizes of about 0.1% contribute to a greasy mouthfeel which is unpleasant when perceived as the dominant key property. Since the perceived transition between an emulsion mouthfeel and a greasy mouthfeel appears to be more gradual than the transition between the former and the calcareous mouthfeel, larger proportions of particles on the order of 0.1 цt in diameter are acceptable in the macrocolloids of the invention. Thus, provided that the average particle size is not less than 0.1 цt, the emulsion-like character is predominant, even if their distribution should have a considerable proportion of individual particles with a diameter below 0.1 цt.

Proteins which are useful in the preparation of macrocolloids include such diverse and diverse sources as vegetable oilseed whey, mammalian mammals, blood serum and avian eggs. Preferably, the present method relates to spherical proteins when in their original state. From the point of view of conventional protein classification, the useful proteins include those which are soluble in aqueous solvent systems and are selected from the simple proteins formed and derived by coupling. Suitable simple proteins include albumins, globulins and glutinsins. Suitable proteins formed by coupling include nucleoproteins; Glycoproteins and muccoproteins (also collectively referred to as glucoproteins); Phosphoproteins (sometimes also classified as simple proteins); chromoproteins; Lecithoproteins and lipoproteins. Thermo-coagulable derived proteins are also suitable.

Not suitable are such simple proteins as the albuminoids (also known as scleroproteins), for example elastins, keratins, collagens and fibroins, all of which are insoluble in their original state. Protamines and histones are not heat coagulatable and are therefore unsuitable as raw materials for heat denaturation treatment.

Suitable proteins formed by coupling are both soluble and heat coagulatable. Similarly, derived proteins (ie, the products of various proteoclastic or denaturing processes), which remain soluble and heat-coagulatable regardless of their derivation, are also suitable as raw materials, provided, of course, that they are not initially incompatible with the manifestation of the desired , organoleptic properties in the final product of the present process. In general, however, many proteins lack metaproteins (also known as protein proteins), proteins, proteoses, peptones and peptides (also known as polypeptides) coagulate one or both of these prerequisite properties.

The preferred protein for use in the present invention may be varied according to the considerations of availability, cost and taste associated with the protein as well as the nature of contaminants in the and other components of the protein source. Among the preferred proteins are spherical proteins such as bovine serum albumin, egg albumen, and soy protein, with milk whey and ovarian protein being particularly preferred. Protein sources that undergo treatment often contain various impurities. It is therefore desirable that, when proteins suitable for the invention are naturally associated with insoluble components, these components may be below the limit of 3.0 μσι or may be removed prior to processing or may be made smaller than said limit during processing can be.

Once a particular protein source is selected, the protein solution is treated for a relatively short time under relatively specific conditions of temperature, shear, and pH. Depending on the protein, the presence of specified amounts of polyhydroxy compounds (e.g., sugars), agglomeration blocking agents and other optional ingredients will aid in optimizing the yield of the desired products. The macrocolloids are prepared by a controlled heat denaturation process during which high shear is applied to prevent the formation of significant amounts of large particle size protein aggregates. The denaturing process is preferably carried out at a pH below the midpoint of the isoelectric curve of the selected protein and preferably at a pH which is about one pH unit below the midpoint of the isoelectric curve. The process may be carried out at lower pHs, with the requirement that the processing pH be not so low as to induce acid degradation of the protein, and that the limitation be that the pH be generally should not be less than about 3. As will be described below, it is also possible to operate at pH values which are greater than the mid-point on the isoelectric curve if a nucleating agent is also present during denaturation.

The exact temperatures and shear conditions used in macrocolloid production are routinely selected, ranging from the time sufficient to form denatured, proteinaceous macrocolloidal particles having a diameter greater than about 0.1 pm, while at the same time forming significant amounts of fused, protein-containing particulate aggregates of more than 2kts are avoided. Preferred shear conditions for processing a given protein solution are best determined using the "oversize" particle assay.

Particle size testing is a measure of the organoleptic quality of the products of the present invention. One of the simplest and fastest methods available to those skilled in the art is the preparation of an optical preparation analogous to the preparation of clinical blood smears. Using this method, first prepare an appropriate dilution of the dispersed macrocolloid and tune to a pH of between 6.5 and 7. Then, by rapid magnetic stirring, sonication or homogenization, complete dispersion of weak accumulations, which may be present between the individual macrocolloid particles, is made. Then, a small amount (e.g., about δμΙ) of the diluted neutralized dispersion is applied to a glass microscope slide of the type often used in biological studies and allowed to dry. The sample is viewed at the known magnification according to known methods using an "aligned" eyepiece, then the dispersed macrocolloidal particles of the sample are visually compared to the mesh on the eyepiece to give a good estimate of the statistical appearance of oversize or agglomerated particles within of the population as a whole.

An alternative method for analyzing the particle size distribution involves the use of an image analysis computer, such as a QUANTIMET 720, as available from the Cambridge Institute, UK. Another method involves the use of the particle size analyzer MICROTRAC. The general aspects of this approach are described in an article entitled, Particle Size Analysis and Characterization Using Laser Light Scattering Application by J.W. Stitley et al. in Food Product Development, December 1976. As will be apparent to those skilled in the art in light of the present disclosure, sedimentation or settling methods may also be used to determine particle sizes. However, one must not forget that gravimetric methods must take into account the protective colloidal effects of, for example, the processing aids used during the heat denaturation treatment described above. An example of a gravimetric determination of the percentage of oversized protein aggregates is summarized below:

1. A five percent dispersion of the macrocolloid of the present invention is prepared and neutralized to a pH of between 6.5 and 7;

2. A high fructose cereal syrup having a weight of 1.351, a pH of 3.3, a total nitrogen content of 0.006% and a solids concentration of about 71% is added in a 1 to 4 ratio of the neutralized 5% macrocolloid dispersion;

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

4. Thereafter, the mixture is centrifuged at 478 g at about 15 ° C for 20 minutes. The oversized protein aggregates, i. That is, particles having a diameter substantially greater than 2 pm may be expressed as a percentage of the weight of the protein contained in the centrifuging pellet divided by the weight of the protein in the macrocolloidal dispersion prior to centrifugation.

These experiments can be applied both to the macrocolloidal dispersions and to the protein materials used as raw materials in the preparation of these macrocolloids. As those skilled in the art will readily appreciate, capacitance-based particle size analyzers, such as known Coulter counter analyzers, are not suitable for the present application, taking into account the charge of the macrocolloidal particles at particular pH values, unless this macrocolloid is diluted with a saline solution (NaCl) of sufficient concentration that the salt ions overcome or "flood" the natural charge on the macrocolloidal particles, however, according to the preferred conditions of preparation of the macrocolloidal preparations, the aqueous protein solution becomes high temperature for a very short time Shear from 7500 to 10000s " ¹ or more subjected. For example, it has been found that a Waring mixer drive equipped with a miniaturized "Henschel" mixer (ζ.Β.11 capacity) gives a processing speed of 5000rpm and thus sufficient shear. The preferred processing temperatures are between about 80 ^° C. and about 120 ^° C., with processing times of between about 3 seconds and about 15 minutes or longer, again times between about 10 seconds and about 2 minutes being preferred. At lower temperatures, the processing times are longer, wherein the treatment at 80 ° C requires 15 min, while the processing times are at temperatures between 9O ⁰ C and 95 ° C at about 5 min. In contrast, the processing time at 12O ⁰ C can only be about 3s. High processing temperatures are supplemented by increased rates of heat transfer. Therefore, if the type of processing equipment permits, processing at high heat transfer rates / high denaturation temperatures over very short periods of time is preferred. It should be noted, however, that at temperatures above 120 ⁰ C and the correspondingly shortened product residence times, the resulting makrokollodiale product is "thinner" and may be less desirable.

Methods for the preparation of the macrocolloids utilize an aqueous protein solution characterized by having a protein concentration of about 10% to 20%, with protein concentrations between about 15% and 18% being preferred. Protein concentrations less than 10% tend to form a stringy mass. The stringy mass remains in a stable dispersion and has unfavorable organoleptic qualities. Solutions with a protein concentration above 20% tend to become extremely viscous, rendering the delivery of the required shear rates to the protein solution impractical.

The aqueous protein solutions may also contain up to 100 parts by weight (of the protein) or more of a polyhydroxy compound, preferably a mono- or disaccharide. These compounds may be "naturally" present in the protein precursors (eg, lactose present in sweet milk whey protein concentrates) or added to the solutions prior to denaturation processing. "The preferred polyhydroxy compounds include reducing sugars such as lactose, glucose, fructose, and maitose, with lactose being particularly preferred Suitable non-reducing sugars include sucrose and lactic acid.

It is believed that the high level of shear applied in the prepared processing prevents the formation of large denatured protein aggregates during denaturation. Optionally, agglomeration blocking agents can be added to the aqueous solutions to facilitate preparation of the desired products. The coagulation blocking agent is selected or concerted in concentration such that it in turn does not alter the pH of the mixture in a manner that is outside of optimum processing specifications. Suitable agglomeration blocking agents include hydrogenated anionics such as xanthan gum (normally included in an amount of 0.1 to 1.0% by weight of the protein concentrate), data semester (0.5% to 2.0% by weight of the protein concentrate, regardless of the fact that data esters cause a smack in the final product) and lecithin (1% to 10% of the weight of the protein concentrate). Other suitable agglomeration blocking agents are carrageenan, alginate and calcium stoyl lactylate.

Maltodextrins prepared by enzymatic or acid hydrolysis of starch represent another chemical that blocks agglomerations in the practice of the invention. The preferred concentration is 10% to 50% of the weight of the protein concentrate. It is believed that these substances have a protein-sparing effect, which also applies to high fructose syrup, although the latter is not quite as effective in this regard as the former. It will be appreciated that these blocking agents are carbohydrates, and hence calorie sources, a factor that may speak against their selection for use in applications such as reduced calorie foods. Plant gum pectin is another suitable agglomeration blocking agent for use in the present invention. Citrus pectin is preferred in fruit-flavored products, whereas "pure" -taste products, such as the analogues of custard ice cream, should advantageously use pectin derived from others as sources of citrus, for example apple pectin Hydrogenated lecithin and hydrogenated xanthan gum are examples of the differential actions of various blocking agents, both of which introduce lubricity into the mouthfeel of the final product, but lecithin, which is one or less on the other hand, the macrocolloid particles produced with xanthan blocking agents are smaller and smoother particles, both of which have a whitening effect on the final product in that they appear to help form a uniform dispersed system, thereby increasing the light scattering effect perceived as whiteness. It has also been found that combinations of agglomeration blocking agents have useful properties. It is preferable to use a combination of pectin and lecithin in the preparation of the protein / casein micellar cream substitute ingredient described herein.

Other optional ingredients, such as salts and components of the final product, including suitable flavorants, colors and stabilizers, may generally be present or added to the solution without deleterious effect. In many cases (i.e., if the nature of the additive and its effect on the protein solution permits), it may be particularly convenient to include these end product components in the protein solution to avoid the need for subsequent additional pasteurization steps after processing.

Protein precursors may optionally be treated to remove cholesterol, fat and other contaminants that may be offensive to the macrocolloidal product. One such method is an extraction step in which the protein material is contacted with a food grade solvent, which is preferably ethanol, and in the presence of a suitable food grade acid. Then the protein material is subjected to several washing and filtering steps, yielding the extracted protein product. Suitable solvents include lower alkenols, hexane or the like, with ethanol being particularly preferred. Suitable food grade acids include mineral acids such as phosphoric acid and food grade organic acids such as acetic, citric, lactic and malic acids, with citric acid being particularly preferred. The extraction method is particularly useful in the removal of cholesterol and fat from such protein sources as whey protein concentrate. In preferred extraction procedures which result in optimal elimination of fat and cholesterol, the whey protein concentrate is maintained for six hours at 52 ° C with a mixture of 90-97% alcohol (preferably about 90% ethanol) and 3-10% water (preferably about 9%) %) and about 0.01-0.20% acid (preferably about 0.084% citric acid). In alternative methods, which yield highly desirable flavor and processing characteristics, the whey protein concentrate is extracted for four hours at 40 ⁰ C with a mixture of ethanol, water and citric acid with respective concentrations of 94.95%, 5.0%, and 0, 05%. According to these methods, whey protein concentrate containing up to 4.0% fat and 0.15% cholesterol prior to extraction, then less than 2% fat and less than 0.02% cholesterol.

After the heat denaturation process is completed, the product may optionally be subjected to a homogenization treatment. Such treatment is desirable when the products are diluted (i.e., have a lower protein concentration) and / or neutralized, for example coffee whitening agents. This treatment causes disruption of the relatively loose interparticle compounds that occasionally form during processing. While not coagulated (that is, not fused to particles substantially larger in diameter than 2 pm), these macrocolloids are organoleptically separated as single when associated or linked together (ie, usually as doublets or triplets) Composite particles are perceived that can not be distinguished on the basis of the respective mouth feeling from agglomerations. The homogenization treatment separates these particle compounds into individual macrocolloidal particles having the desirable properties of mouthfeel. The homogenization treatment of dilute products with low macrocolloid concentration (e.g., coffee whitener) is preferably carried out at a pH of 6 to 7. At these pH values, the distribution of electrical charges on the surfaces of the macrocolloids helps to maintain uniform dispersion of the macrocolloids in the aqueous medium. While any homogenization treatment known in the art may be used for this purpose, care must be taken that the macrocolloidal particles are not exposed to temperatures as high as might cause agglomeration into larger particles.

The particle size test proves to be a measure of the organoleptic quality of the products of the present invention. One of the simplest and fastest methods for preparing an optical preparation in the same way as preparing a clinical blood smear. Using this method, weigh 10 g of a pasty food sample into a Waring blender and add 190 g of distilled water to make a 5% solution. The solution is then mixed at high speed for 2 minutes, then the pH is adjusted to 6.75-7.0. The sample is then subjected to a magnetic stirring at high speed for one minute using a sonicator (Braunsonic Model 2000, Burlingame, CA) during sonication. This procedure breaks up any "weak" compounds that might be present between each macrocolloid particle. Subsequently, the solution is further diluted with deionized water to between 0.25% and 0.50% depending on the particle concentration. This solution is then placed in an ultrasonic bath (Branson 2200 Ultrasonic Bath, Shelton, CN) for one minute immediately prior to preparation of the preparation. After shaking sample 10s by hand, 20 μΙ of it is placed on the center of a microscope slide, which is inserted into a corresponding coming-sling. The slide is spun onto the slide immediately after application of the sample. Once the slide is dry, which is usually the case within 30 seconds, it can be examined microscopically.

The sample is examined with a Zeiss Axiomat microscope equipped with a halogen light source (Zeiss, Thornwood, NY) and a Dage MTI video camera (Michigan City, IN) and camera control, with a 50X magnification lens and an overall magnification between 1000 and 1600 are used. The system can only perform a quantitative analysis on particles larger than about 0.25 μm in diameter. For this reason, all statistical measures of particle size, unless otherwise indicated, refer to particles having major dimensions greater than 0.25 μm. Nevertheless, the viewer can see particles between about 0.10 pm and about 0.25 pm, and their presence is routinely noted. Numerous fields (15 to 25) are scanned to subjectively evaluate the overall size and shape homogeneity heterogeneity of the sample. After the qualitative assessment of the sample, a field is selected that appears to be represented for the entire sample. This image is then projected onto a high definition black and white television receiver (Lenco, Jackson, MO) for quantitative analysis.

The image on the television monitor is first digitized and then transferred from the television monitor to the computer monitor. During the digitizing-transferring step, the image is slightly reduced in size, which has the side effect that some of the particles separated on the original image merge with each other and hence are not representative of the true particles. These seemingly fused particles are then carefully discarded by comparing the old (television monitor) image with the new (computer monitor) image.

Typically, about 250 ± 50 particles are measured in a field. As many fields as necessary are scanned to include 500 particles in the assessment. Initially, the number of particles in the image along with their corresponding length and width is determined.

From these data, two additional variables, the equivalent spherical (E.S.) diameter and the volume, are calculated as follows:

ES diameter = (B ² χ L) ^1/3 ES volume = Ѵз B ² L.

Where B is equal to the width and L is equal to the length.

When the ES diameter and ES volume are determined for the total distribution of the particles in the image, number-weighted (D _n ) and volume-directional (D _v ) average ES diameters are calculated. D _n is the average particle size diameter formed over the number and is calculated by summing the diameter of all particles in the distribution and dividing by the total number of particles. In contrast, D _v (volume-weighted mean diameter) estimates each particle in proportion to its volume, indicating where the mean diameter is based on volume or, implied, mass. The maximum diameter (D _max ) is simply the diameter of the largest particle present in the microscopic field.

These data can be represented in the form of a histogram with the ES diameter on the abscissa as a function of the number of particles and the volume of the particles. From these data, the percentage of the particle volume with more than 2 μιτι and the maximum diameter of the particles can be determined directly. According to another aspect of the present invention, spheroidal particles as described above are obtained by coagulating or denaturing easily coagulatable protein (preferably a protein coagulating at a temperature of 85 ^° C. or below), such as protein protein (EWP), bovine serum albumin (BSA) and defatted whey protein, in the presence of a nucleating agent, whereby the coagulatable protein coagulates and envelops the nucleating agent, resulting in spheroidal particles having a core-shell configuration in which the core is the nucleating agent and Shell is the denatured coagulable protein. The core or coagulant may account for less than about 90% of the volume of the resulting spheroidal particle and will typically occupy less than about 50% of the volume of the particle. The rest of the particle is formed from the denatured protein, eg denatured protein protein.

It has been found that particle formation can be performed at an approximately neutral pH, that is, above the midpoint of the isoelectric curve of the protein when the protein is denatured in the presence of a nucleating agent. The coagulatable proteins that denature to macrocolloidal particles are the proteins that are easily coagulated, i. h., protein protein and bovine serum. Sweet whey protein concentrate does not form a core-shell configuration with a nucleating agent (casein micelle) since the whey protein has a higher coagulation temperature. The nucleating agent (NA) may be any organic or inorganic microparticulate substance smaller in size than the desired size of the proteinaceous macrocolloidal particles of the final product to be used as a fat / cream substitute. Typically, the core forming agent will also have a spherical shape, although this shape is not critical, especially if the nucleating agent is to account for less than about 25% of the volume of the macrocolloid fat cream substitute particles of the finished product. The nucleating agent serves as a seed to promote the formation of protein protein particles around the nucleating agent.

Suitable nucleating agents include casein micelles, microcrystalline cellulose, silica, reduced iron, zein, and water-insoluble proteins. The nucleating agent is a colloidal form, for example, colloidal iron, colloidal zein, colloidal proteins, and colloidal, fumed silica. It is also possible to use mixtures of different nucleating agents

 A preferred nucleating agent is micellar casein.

Protein protein is a preferred coagulatable protein for the production of a particle in core-shell configuration. Proteinaceous protein nucleating agent particles ("EWP / NA" particles) of the invention are prepared by processing the protein protein in the presence of the core forming agent at elevated temperatures and under shear conditions as described herein to form macrocolloidal proteinaceous particles. Although the midpoint of the isoelectric curve of protein protein is pH 4.5-5.5 as pH, the pH in the denaturation medium can be raised above the mid-point in the isoelectric curve The total protein content of the mixture undergoing processing is generally between about 5 and about 20% Polyhydric compounds (lactose) and co-baffle blocking agents are also optionally added used.

In a preferred embodiment of the present invention, spheroidal protein particles are prepared from a combination of protein protein and a source of substantially non-aggregated or natural kadein micelles as the nucleating agent. These proteinaceous casein micellar particles ("EWP / CM" particles) are prepared by heating a mixture of egg white protein and a source of casein micelles under shear conditions as described above, in contrast to the case where macrocolloid particulates of egg white protein are absent of a nucleating agent (see, for example, Example 3, below), it has been found that the proteinaceous casein micellar particles can also be prepared at a pH above the midpoint of the isoelectric curve of the protein protein (see Examples 6 and 7, below). ,

Casein micelles, which are presently preferred nucleating agents, are naturally occurring, spheroidally-shaped protein particles found in mammalian milk, generally between 0.1 and 0.1 microns in diameter. Any source of casein micelles is acceptable for the practice of the present invention, but cow's milk is preferred because it contains casein micelles in high concentration. Skim milk, condensed skimmed milk, and ultra-filtered skim milk are particularly preferred because they contain lower levels of fat, which is desirable for fat / cream replacement applications.

The total protein content of the reaction mixture, which is exposed to the heat and fuse conditions in the formation of protein-casein micellar particles, is typically between about 15% and about 20%, but the total protein content and protein protein to casein micellar protein ratio are not more critical Meaning. The protein is usually involved in 25% to about 99% of the total protein content, while the casein micelle source can be between about 1% and about 75% of the total protein level, preferably between about 1% and about 40%. It is desirable to use concentrated protein and a concentrated source of casein micelles. Therefore, freeze-dried egg whites and ultra-filtered egg whites are preferred sources of protein, while condensed skimmed milk and ultra-filtered skimmed milk are the preferred casein micelle sources.

The proteinaceous casein micellar protein particles are preferably prepared in the presence of a polyhydric compound and a clumping blocking agent, both of which have been described above. Preferably, a combination of sucrose and lactose (both from condensed skim milk sources) is the component of the polyhydric compound, while a combination of lecithin and pectin forms the component of the agglomeration blocking agent. Food grade acids can be used to control the pH and water is used to adjust the concentration of the ingredients. When ultrafiltered protein and condensed skimmed milk are used to make the protein-casein micellar protein particles, the following would be a typical reaction mixture: ultrafiltered protein protein 40% to 60% (giving protein in an amount of 8 to 12% of the total weight of the mixture) condensed skimmed milk 10% to 33% (giving protein in an amount of 1 to 4% of the total weight of the mixture). Cane or cereal sugar 0 to 10%, pectin of plant origin 0 to 0.5%; Lecithin 0 to 1.0%; Food grade acid 0 to 0.3% (to balance the pH at 6 to 7) and water up to 100%. Figures 1 and 1A illustrate a preferred embodiment of a process for the preparation of proteinaceous casein micellar protein particles to provide a fat replacement ingredient of the invention. The time, temperature, pressure, and pH conditions for each step are shown in Figures 1 and 1A, and correspond to the letters in the flowchart enclosed in a circle. In this embodiment, a sugar and a rubber agglomeration blocking agent, such as pectin or guar, are dry blended in a conventional dry blender 1 to give a premix A. Pasteurized liquid protein is ultrafiltered in a conventional ultrafilter device 3, the filter device preferably having a polysulfone membrane having a nominal molecular weight cut-off of about 10,000, resulting in a concentrated protein (precursor B) having a protein weight concentration of 15% to 25%. Lecithin is hydrogenated in purified water (counter-osmosis) using a mixing tank under vacuum, 5, to give premix C. A dilute solution of a food-grade acid such as lactic acid or citric acid is prepared with purified water (Premix D). Premix A is hydrogenated in purified water using a high shear direct or batch mixer 2. The pre-preparation B and the condensed skimmed milk are added to the hydrogenated premix A in a sanitary batch tank 4 to bring the protein concentration to the desired value, i.e., 10% to 20% total protein. Premix D is added to the batch tank to control the pH to the range of 6.0 to 7.0, and preferably 6.2 to 6.6.

Premix C is added to the batch tank, resulting in a prepared protein solution 11 ready for thermal processing under shear bonding to form protein-casein micellar protein particles suitable as a fat / cream substitute food ingredient.

The prepared protein solution 11 is degassed in a hygienic degassing unit 6 in order to minimize the dispersion and dissolved oxygen. The heating / shearing process may be carried out in a single high shear thermal processing plant, but preferably it is carried out in two plants consisting of a preheater 7 and a high shear thermal processing plant 8. The preheater 7 is used to bring the temperature of the prepared protein solution to 48 ° C-77 ° C (120 ^o F 170 ^o F) and preferably at 60 ° C-74 ° C (140 ° F-165 ° F), such that the temperature rise in the high shear thermal processing plant 8 is an exit temperature suitable for pasteurization, ie 176 ° F-186 ° F (70 ° C-75.5 ° C) according to the guidelines of the US Food and Drug Administration (FDA ), reached. The heat from the processing plant exiting high shear 8 material is in a conventional heat exchanger 10 (1.5 ° C-4.5 ° C) is cooled within a few minutes at a temperature between 35 ⁰ and 40 ⁰ F F. The resulting macrocolloid protein-casein micellar protein particulate product can be used as a fat or cream substitute ingredient. The process described above for producing proteinaceous casein micelle protein particles is preferably carried out adjacent to a food processing plant into which the protein cream substitute can be fed directly. If, on the other hand, the resulting material is to be shipped or stored for future use, a pick-up tube 9 is inserted into the process flow between the processing unit 8 and the cooling device 10, so that the product can be guided through the pick-up tube 9 over a period of time which is sufficient to allow the product To effect pasteurization of the protein protein casein micelle cream substitute. After pasteurisation, the product is cooled and stored at 35 ° F-40 ° F (1.5 ° C-4.5 ° C).

When the high shear heat exchanger 8 is the equipment described in the above-referenced U.S. Patent Application, Serial no. 127710, a blade circulation speed of about 3000 to 10,000 rpm, and preferably about 5000 to 7,500 rpm, is sufficient to give a product having the consistency and mouthfeel of heavy cream (fat) ,

From consideration of the electron micrographs, it is apparent that the protein-casein micellar protein particles consist predominantly of particles having an inner core of casein micelle and an outer shell of denatured protein protein. A minor proportion of the protein particles are denatured protein protein particles and aggregated casein micellar particles. In some cases, more than one casein micelle is contained in the coagulated protein particle.

Reference is made to Fig. 2. Protein protein-casein micellar protein particles 21 are shown to have a core of one or more casein micelle particles 23 (which are visible as dark bodies in the particles) and a shell of denatured protein protein 25 (which is visible as a brighter outer portion of the particles). The proteinaceous casein micellar protein particles of Figure 2 were prepared using essentially the same procedure as described below in Example 7. Fig. 3 shows protein-casein micellar protein particles 31 prepared in an in situ method according to the methods described in Example 6. It is noteworthy that in Fig. 3 the denatured protein protein shell 35 generally accounts for a smaller fraction of the total volume of the particles relative to the casein micelles 33 than the protein protein envelopes of the particles in Fig. 2. The core-shell configuration of the protein particle is more clearly shown in Fig. 4, which is a micrograph of an ice desserts using the cream substitute of Example 7. The casein micelle core 41 can be readily seen in various particles, while the lighter, less dense shell portion 43 of these particles consists of denatured protein protein. Also visible in Fig. 4 are casein micelles 45, which have no protein protein coat. Figures 2 and 4 can be compared with Figure 5, an electron micrograph of top quality ice cream (about 16% butterfat). In Fig. 5, the relatively large white circles represent fat globules and the small dark bodies 53 are casein micelles.

The protein-casein micellar protein particles form a macrocolloid which is useful as a FetW cream substitute ingredient for ice desserts and also in mousses, sauces, dips, cream pie fillings, glazes, and similar foods that normally contain cream. The protein-casein micellar macrocolloid takes the place of the cream in these food recipes, using simply the macrocolloid instead of the cream during the preparation process. Typically, the protein-casein micellar cream substitute ingredient is used based on a wet ratio of about 1: 1 instead of fat cream. This represents a replacement of about 3 grams of fat / cream by about 1 gram of protein since the proteinaceous casein micellar cream substitute ingredient contains water, polyhydric compounds, agglomeration blocking agents and other ingredients. The optimum amount of protein-casein / meal cream substitute to be used in a given food application is readily determined by one skilled in the art from routine taste studies.

The protein protein-kadein micelle protein particles generally have a diameter of from about 0.1 to about 3 ц t, and preferably have a mean diameter of from about 0.5 to about 2.5 ц t to cause the mouthfeel of fat / cream. It is also desirable that the protein-casein micellar particles be present in frozen foods in amounts of at least 1 x 10 ⁸ particles / cm ^{3 of} the food product, and preferably from 1 x 10 ⁸ to 1 x 10 ¹² or more particles / cm ³ .

embodiments

The following examples relate to preferred methods and methods for the preparation of macrocolloids for the practice of the present invention. Example 1 relates to a preferred method for the preparation of macrocolloid material extracted from whey. Example 2 relates to the preparation of macrocolloid material from bovine serum album. Example 3 relates to the preparation of macrocolloid material from egg albumin, while Example 4 relates to the use of soy protein for the preparation of the macrocolloid material. Example 5 deals with the preparation of ice-cream type ice cream desserts in which such macrocolloidal products as those of Examples 1 to 4 are included in the formulas of the premixes of ice cream instead of the butterfat component normally contained. Example 6 relates to ice cream-like products prepared from premixes incorporating heat coagulatable protein and in which denatured protein particles are formed in a sufficient number and within the desired range of sizes in situ during pasteurization mixing of the premix. Example 7 deals with a preferred method of making a protein-casein micellar cream substitute ingredient according to the present invention. Example 8 refers to an ice cream dessert containing the cream substitute of Example 7 as a substitute for greasy cream. Example 9 is an optimization study for the use of the product of Example 7 in a food-like product. These examples should not be considered as limiting the scope of the present invention.

Example I:

An extraction procedure was performed for the removal of fat and cholesterol from the Whey Protein Concentrate (WPC concentrate) as a source of protein prior to denaturation processing. More specifically, a reaction vessel was charged with 181 kg of absolute ethanol (Pos. No. 16468x, 16995x, AAper Alcohol & Chemical Co., Shelbyville, KY). Then, water (8.58 kg) and 10% citric acid solution (954 g, Miles, Elkhart, IN) were added and the solution was stirred for about two minutes. Then, the pH of the solution was measured to prove that it was 5.0 ± 0.5.

Then 140 pounds (63.5 kg) whey protein concentrate WPC-50 (Lot 6302-2 Fieldgate, Litchfield, MI) was added to the reaction vessel and the reaction vessel was sealed airtight. In the reactor jacket steam was introduced, and the temperature of the reaction vessel was maintained for 4 hours at 40-42 ⁰ C. The protein slurry was removed from the reaction vessel and filtered on a continuous band filter, whereby the thickness of the filter cake could reach 1 inch (25.4 mm). The recorded filter cake weighed 116kg. Into the reaction vessel was charged 127 kg of 95% ethanol, and the wet cake was added to the reaction vessel to form a slurry, which was mixed for 20 minutes. The slurry was then removed, filtered as above, and the collected filter cake re-added to the reaction vessel with 127 kg of 95% ethanol. The slurry was mixed for 20 minutes and then carefully filtered to remove as much liquid as possible. The wet cake had a weight of 104.5 kg.

The wet filter cake was then placed in trays with a uniform thickness of 1 inch (25.4 mm) or less. Then, the material was dried in vacuo for 12 hours at a temperature of 45 ⁰ C ± 1 ⁰ C to yield 51.5 kg whey protein concentrate at a yield of 80.9%. Assuming that about 3.5 kg of the material was lost in the drying plant, the percentage of volatiles in the first wet cake could be calculated as 47.4%.

The resulting material had a protein concentration of 56.91% and a solubility of 93% as measured by the method of solubility determination described above. The protein was then used to prepare a composition containing lecithin ("Lecigran F", Riceland, Little Rock, AR), 37% hydrochloric acid (food grade, JT Baker, Phillipsburg, NJ), xanthan ("Keltrol T", Kelco, San Diego, CA) and water.

Table 1 Dairy protein composition

component % Weight (g) WPC-50 34,500 690.00 lecithin 0.932 18.64 hydrochloric acid 1,590 31.80 xanthan 0,186 3.72 water 62.792 1 255.00 100000 2,000.00

The components of the composition shown in Table 1 were added to a high shear mixer and degasser (Kady Mill, Scarborough, ME) in the following order: water, hydrochloric acid, lecithin, xanthan and whey protein concentrate. The mixture was degassed, care being taken to minimize the conversion of mechanical energy to heat before transferring it to the batch processor of the above-referenced U.S. Patent Application, Serial no. 127710 (Attorney's Docket No. 10057). Then, the processing vessel was filled with the premix, which had a pH of 4.15, hermetically sealed, and the temperature recorder was turned on. The engine was actuated and the speed of the bucket was tuned to 5080 rpm. After a few seconds, a heat medium at a temperature of 100 ° C was circulated through the jacket of the container. Within 4,3min the product reached a temperature of 122 ⁰ C, at which time the heat medium was replaced by a flow of cold water, within 2 minutes the product at 40 ⁰ C cooled. The product obtained in the process described above was then tested for organoleptic and physical properties. The product had a smooth and creamy consistency with 64% of the protein converted to macrocolloidal particles and 0% of the particles exceeding 3μπη. The spherical particles had a volume weighted mean diameter (D _v ) of 0.99pm, an average particle diameter (D _n ) of 0.78ct, and a maximum diameter (D _max ) of 1.50ct.

Example 2

In this example, bovine serum albumin (BSA) was used to make a protein macrocolloid product. Bovine serum albumin identified as "Bovine Albumin, Fraction V" was purchased from US Biochemical Corp. (Cleveland, OH) The material was a lyophilized powder having a protein content of 97% and a solubility of 99%, as described above Solubility Determination Other components of the composition included lecithin ("Lecigran F", Riceland, Little Rock, AR), 37% hydrochloric acid, food grade (JT Baker, Phillipsburg, NJ), xanthan ("Keltrol T", Kelco, San Diego, CA), lactose (alpha-lactose monohydrate, Sigma St. Luois, MO) and water.

Table 2

Composition with bovine serum albumin

component % Weight (g) Bovine Serum Albumin 13.080 121.64 lecithin 2,100 19,53 hydrochloric acid 0,770 7.16 xanthan 0,200 1.86 lactose 7,560 70.31 water 76.290 709.50 100000 930.00

The composition listed above in Table 2 was prepared in a high shear mixer and degasser (Kady Mill, Scarborough, ME) with the xanthan gum prehydrogenated. In the order of water, hydrochloric acid, lecithin, xanthan, lactose and bovine serum albumin, the mixer was filled and the mixture was degassed before being introduced into the processing equipment as in Example 1. The processing vessel was filled with the premix, which had a pH of 4.19, hermetically sealed, and the temperature recorder was set. The engine was operated and the speed of the bucket was tuned to 5080 rpm. After a few seconds, a heat medium with a temperature of 80 ⁰ C was circulated through the jacket of the container.

Within 4.8 minutes, the product reached a temperature of 126 ⁰ C, at which time the heat medium was replaced by a stream of cold water. The product was cooled to 40 ^° C. in 2 minutes. The shear rate of the processing plant is reflected in the difference of 46 ⁰ C between the temperature of the product and the temperature of the heat medium. This extra heat was dissipated from the conversion of mechanical energy to heat at a rate of 380 J / s.

The product obtained in the above-described process was then examined for its organoleptic and physical properties. The product had a thick consistency, similar to that of the macrocolloid material made from the whey protein concentrate, and a creamy structure with high suppleness. 71% of the protein has been converted to macrocolloidal particles. The particles were predominantly spheroidal, although some rod-like and fibrous particles were also present. These rods and fibers had dimensions exceeding ЗЗt, making up about 2.25% of the particles in number. When the rods and fibers were excluded from analysis of the microscopic image, the spheroidal particles had a mean volume weighted diameter (D _v ) of 1.03 μπι, an average particle diameter (D _n ) and 0.66 ц t and a maximum diameter (D. _max ) of 1,75 цт.

Example 3

In this example, protein albumin was used to prepare a protein macrocolloid product. It was found that a combination of fresh egg white and spray-dried egg white gave the desired product. Fresh egg whites were separated by hand on the day the premix was made. In addition fresh eggs were bought locally. It was found that this protein contained 98% soluble protein, but the protein concentration was less than 10%. Due to the initial protein concentration, the processing of all fresh protein may result in stringy masses of the denatured protein product. Spray dried protein was purchased from Henningsen Foods (White Plains, NY) (type P-110 protein solids) and had a minimum protein content of 80%. The protein solubility of the spray-dried protein powder was only 83%, and processing only this material can result in an unacceptably high number of oversized particles. To avoid the limitations of using the individual starting materials alone, the fresh and the spray-dried egg whites were combined to give a suitable egg albumin protein source.

Lecithin, xanthan, hydrochloric acid and lactose were obtained from the sources mentioned in Example 1 and were used in the amounts listed in Table 3 below.

Table 3 Composition with protein albumin

component % Weight (g) Fresh egg white 70.21 1,168.92 Spray dried egg whites 13.44 223.72 lecithin 2.97 49.54 xanthan 0.30 4.95 hydrochloric acid 2.37 39.43 lactose 10.71 178.35

100.00 1664.91

Fresh egg white, lecithin, xanthan, lactose, spray dried egg white and hydrochloric acid were added sequentially and in the amounts shown in Table 3 to a high shear mixer in which they were mixed and degassed. The resulting masterbatch had a pH of 3.6 and was introduced to the processor as in Example 1. The treatment was carried out at a bath temperature of 80 ° C for 4.33 min at a blade speed of 5080U / min. The product maximum temperature was 125 ^° C.

The product obtained by the method described above was thick and creamy. 88.9% of the protein had been converted to macrocolloidal particles, which had a pronounced tendency to cluster loosely. Analysis of particle sizes showed that they were within the desired size range of D _v = 1.22μπη and only 4% of the particles were above 2μνη . Essentially all particles were spheroidal.

Example 4

In this example, soy protein was used to make a protein macrolloid product. Soy protein was obtained from Ralston Purina (SN 1631-32-1, St. Louis, MO) and had a protein content of 61.4% and a solubility of 81% as determined by the above method. Lecithin, xanthan, hydrochloric acid and lactose were obtained from the sources mentioned in Example 1 and were used in the amounts listed in Table 4 below.

Tabejle 4 % Weight (g) 22.036 99.16 Soy protein composition 3,000 13.50 component 0,100 0.45 soy protein 2,196 9.88 lecithin 10,800 48.60 xanthan 61.868 278.41 hydrochloric acid lactose water

100,000 450,00

The mixture was prepared by adding water, hydrochloric acid, lecithin, xanthan, lactose and soy protein, one at a time, to a high shear mixer where it was mixed and degassed. The resulting premix had a pH of 3.74 and was introduced to the processing plant of FIG. The bath temperature was maintained at 110 ° C. The heating was for 4.30 min, the circulation speed was set at 5080 rpm. The maximum temperature reached by the product was 119 ° C.

The product developed a bright, tan coloration during cooking and was supple, creamy and thick with a slightly beany taste typical of soy products. 71% of the protein was converted to macrocolloidal particles. Analysis of the particle size showed that the particles were within the desired size range, with D _v equal to 1.46μιτι and D _max equal to 2.5μm. All particles were essentially spheroidal.

Example 5

A ice-cream type ice cream dessert was prepared from a macrocolloidal whey product using the following procedure. An extraction procedure according to Example 1 was subjected to 150 pounds (about 68 kg) whey protein concentrate WPC-50 (Fieldgate Brand, First District Assoc, Litchfield, MN 55355, Item 6302-2). 117 pounds (about 53.1 kg) of extracted protein were obtained. The extracted whey material was 97.6% soluble (by the method described above), had a protein content of 56.7%, a fat content of 1.9% and a cholesterol content of 53.1 mg / 100 g.

The extraction-treated whey protein concentrate was then blended thoroughly with lecithin ("Lecigran F", Riceland, Little Rock, AR), 37% food grade hydrochloric acid (JT Baker, Phillipsburg, NJ), xanthan ("Keltrol T", Kelco, San Diego, CA) and water in the proportions given in Table 5 below to give a protein pre-mix with a pH of 4.28.

Table 5 % Weight (Pound-0.4535 kg) Whey protein composition 34,500 48,300 component 0.932 1,305 Whey protein concentrate WPC-50 1,595 2,233 lecithin 0,186 0.260 Hydrochloric acid (37%) 62.787 87.902 xanthan water

100,000 140,000

The protein premix was degassed at a rate of about 55 pounds (about 24.943 kg) per hour / pair of Votator scraped surface heat exchangers (3XII χ 12 inches-76.2 mm χ 304.8 mm) (Chemetron Corp., Louisville, KY) operating at 980 rpm. The product was in the first heat exchanger at about 60 ⁰ C (about 15 ° C) introduced and constant to a temperature of about 19O ⁰ C (about 87 ° C), whereupon the product was passed through piping to a second heat exchanger to The processing equipment worked for about three hours and twenty minutes, with samples taken at different times for analysis, the macrocolloidal samples were subjected to size and other analyzes, and the results are shown below in Table 6. Viscosity was determined using a cone-plate viscometer (Haake, Saddlebrook, NJ).

ТаЬеНвб Time Prod.- flow Visc. Pr. Temp. rate (CP) No. CF) (L / h) 00:00 182 55 227 1 12:03 2 12:11 3 12:30 4 12:33 183 55 5 1:00 184 55 246 6 1:02 7 1:10 8th 1:39 187 55 407 9 1:41 10 1:49 11 2:18 190 55 283 12 2:44 190 86 266 13 2:47 14 3:01 199 86 278 15

-14- 283 557 D _m «x Bemerkun (around) gene

0.70 1.06 1.75

0.74 1.05 2.00

0.76 1.22 2.00

0.78 1.14 2.00

0.85 1.30 2.50

0.73 1.16 2.00 bad

16 3:15 teQua-

17 3:20 187 55 258 0,79 1,30 2,00 lity

The whey macrocolloid protein product prepared after sample 7 was then used to make a ice-cream type ice cream desserts. The "ice cream" composition consisted of 2000g of whey macrocolloid product as a replacement for heavy cream in a formulation containing condensed skim milk (30% solids), sucrose (Baker's Special), stabilizer (Fanci Freeze 1065, Celanese Corp., Louisville, KY), sodium hydroxide solution The ingredients of Table 7 were mixed in the following order: sucrose and the stabilizer were dry blended and added to a mixture of water (19767.7 g) and condensed skimmed milk with high shear mixing to give a component, The whey macrocolloid was diluted with water (550g) and then combined with high shear mixing with a dilute mixture of sodium hydroxide and water (110g) to form a neutralized, macrocolloid "cream". The final mixture was then made by adding the macrocolloid "cream" to the sucrose stabilizer milk solids component.

Table 7 % Weight (g) frozen composition 19.60 2156 component 0.40 44 sucrose 25.86 2,844.6 stabilizer Ό, 97 1,976.7 Condensed skimmed milk 20.00 2200 water 5.00 550 Whey macro colloid 1.17 128.7 water 10.00 1100 Haoh solution (10%) water

The weight was preheated to 135 ° F (about 57 ° C) in a pasteurizer (APV plate heat exchanger, APV, Tonawanda, NY), homogenized, pasteurized at 155 ° F (about 67 ° C) for 30 minutes, at 52 ° F ( about 11 ^° C) and allowed to stand overnight before freezing. Then, the "ice cream" mixture was flavored with freeze-dried sliced strawberries and strawberry and vanilla flavor to make a strawberry ice cream The ingredients were mixed by hand in the amounts shown in Table 8.

Table 8 % Weight (g) Recipe for strawberry "ice cream" 98.23 4400 component 0.20 8.8 ice cream mix 0.10 4.4 strawberry flavor vanilla flavor 1.47 66.0 Cut, freeze dried strawberries

100.00 4479.2

The cooled mixture was then poured into an automatic ice cream mixer (Coldelite, NJ), and edited about 20 minutes, whereupon the product was taken out (at a temperature of about 18 F to about ⁰ -8 ⁰ C).

Two pieces of the strawberry, ice cream "composition were prepared, giving a total of 2.9 gallons (about 111) of finished" strawberry ice cream "characterized by a creamy (not icy) structure. The product was compared to two different commercial ice-cream products in blind comparisons by groups of 60 untrained persons on the basis of two highest quality strawberry rice ice creams, each containing 14% to 16% butterfat. When comparing the structures, the overall appearance of the three products was approximately comparable, while no significant differences were found in the creaminess, pliability and structure comparisons at a significance value of .alpha. = 0.05, as shown by the results shown in Table 9 have been.

Table 9 Structural comparisons of strawberry ice cream

sample Highest sample Highest product Quality no. 1 product Goodness no. 2 (n = 26) (n = 26) (n = 27) (n = 26) overall impact 6.7 7.7 6.7 7.1 (9 = extremely good) creaminess 3.3 3.0 2.9 3.0 (5 = too creamy) suppleness 3.9 3.9 3.6 3.9 (5 = extraordinarily smooth) structure 3.2 3.0 2.8 2.8 (5 = too close)

Three top quality ice cream flavors and a standard quality (supermarket brand) ice cream, vanilla ice cream, were subjected to comparative analysis with a vanilla "ice cream" prepared essentially according to Example 5 using a milk whey macrocolloid as a complete substitute for milk fat Results of the comparative analysis are given below in Table 10

Approximate analysis for ice cream desserts Based on 100g of the product

ice cream Per moisture Fat, ash C-Fa coal ka highest sor ton, tigk .. G G ser, hydrate lo te, No. 1 G G G G rien ice cream sample highest sor 1. te, No. 2 4.1 57.5 17.0 0.8 <0.1 20.6 252 ice cream highest sorting Second te, No.3 4.6 55.1 15.9 1.0 <0.1 23.4 255 ice cream standard Grade Third Product, 2.8 59.3 15.4 0.7 <0.1 21.8 237 Example 5 3.0 62.4 9.8 0.8 <0.1 24.0 196 4th 7.1 66.5 0.5 1.2 <0.1 24.7 132 5th

Examples:

A chocolate-flavored ice cream dessert of the invention was prepared by forming the denatured protein particles in situ by combining a premix of the ingredients listed in Table 11.

tables Liquid protein Wt .-% % of the protein component Condensed skimmed milk (30.15% solution) weight sugar 40,000 4,056 A water 26,250 2,862 B Non-fat dry milk 16,000 - C Liquid egg yolk 7,940 - D Citric acid (10% solution) 3,700 1,338 e Frodex 36 (grain syrup solids) 0.900 - F Celtose (alginate) 1,800 - G Kassiaschotengummi 1,230 - H 0,250 - I 0,080 - J

К Какао (Gerkin's Sienna) 0.875

L Cocoa (Bersdorp Royal Dutch) 0.875 -

M vanilla 0,080

N cream flavor (Naarden) 0,020 _ ^

100,000 8,256

A dry blend of components E, H and I and sugar component C was prepared. The condensed skim milk B and water were added to a Liquivertor mixer, and the dry mix and other dry ingredients E, J, Kund L were added with mixing to dissolve and disperse all components. Subsequently, the egg yolk, F, was added with constant mixing. After all the components were well dissolved, the liquid egg white A was added and mixed briefly, then the citric acid solution was added in an amount sufficient to reach a total mixture pH of 6.2 to 6.5. After checking and adjusting the pH to the required extent, the agitator was switched off. The premix prepared above was then pasteurized under high temperature conditions for a short time (HTST conditions) with stirring and high shear application by two alternative methods. Approximately one-third of the mixture was first heated by introduction into a heat exchanger with a 3ZoII χ 12ZoII (76.2mm x 304.8mm) eccentric scraper blade operating at 450 RPM. After reaching a temperature of about 140 ^° F (about 60 ^° C), the mixture was placed in a continuous apparatus such as shown in Fig. 2 of the related U.S. patent application, Serial no. 127710, whose vane recirculation number was set at about 5000 rpm. After a temperature of about 180 ⁰ F was (about 82 ⁰ C) is reached, the mixture was filtered through a "capture" tube of metal, which was isolated and an outer diameter of 1/2 inch (12.7 mm) and an inside diameter of 3/8 inch (9.525 mm), had conducted, in which the temperature of the mixture at about 176 ⁰ F (about 80 ⁰ C) was maintained, the mean residence time of the tube passing mixture was determined to be about 20s. the cooling of the mixture after pasteurisation was achieved by a first heat exchanger with an eccentric Votator scraper area of 3ZoIIχ12ZoII (76.2mmχ3030.8mm) operating at a speed of 1000rpm to give a temperature drop of 176 °F ( 80 "C) to 80 ° F (about 27 ⁰ C), followed by passage through a heat exchanger with a concentric Votator scraping surface of 3ZoII χ 12ZoII (76.2mm χ 304.8mm), which at a speed of about 300 rpm worked to drop the temperature to sth a 38 ° F (about 3.3 ° C) effect. Then the aromatics, M and N, were added and after an optional rest phase, the flavored mixture was frozen in a conventional ice cream freezer. Preference is given to the use of a Freezers, which is equipped with a striking mechanism with high displacement and is characterized by a high freezing capacity.

About two-thirds of the premix was subjected to high shear processing, using only heat exchangers with Votator scraping surface. The mixture was thus passed through an eccentric votator of 3 inches χ 12 inches (76.2 mm χ 304.8 mm) working at about 1000 to 1 lOOU / min to raise the temperature to about 180 ° F (about 82 ° C). to increase, then the mixture wherein the temperature was maintained an average Zeitspänne of 20 to 22 s at 176 ° F (8O ⁰ C) was passed through a holding tube, as described above. The subsequent passage through a second eccentric votator, operating at about 1000 to 1 lOOU / min, resulted in a temperature drop of the product to about 6O ⁰ C (about 16 ° C), and the final lowering of the temperature of the product to about 4O ⁰ F (about 4.5 ⁰ C) was reached using a concentric votator, operating at about 300U / min. Subsequently, the mixture was subjected to the same processing as above.

The products prepared in the two high shear pasteurization processes described above were tasted, and the first flavor test product and the first alternative process product were somewhat more advantageous in smoothness creaminess and texture. The practice of the invention in the preparation of ice cream products by the production of fat-free or substantially fat-free and coagulatable, protein-rich premixes generally provides for the preparation of premixes containing up to 20% protein, of which 25% to 100% in the form of a heat coagulatable Protein are present. For example, the composition in Table 11 gives a premix containing 8.256% protein. Of this protein, 4.20% (derived from the condensed skimmed milk and non-fat dry milk components) are essentially non-heat coagulatable while 4.056% (derived from the liquid proteins) are heat coagulatable. Analysis of the ice cream analog product for the presence of denatured protein particles is performed as follows. It is determined the number of particles with a diameter of 0.1 μιτι to 3.0 μ, which would fill a cubic centimeter volume. The calculated values are given below in Table 12.

Table 12 Calculated number of particles occupying 1 cm ³ volume, classified according to different particle sizes

Micrometer range Number of' 0.0-0.1 1.53 χ 10 ¹⁶ 0.1-0.2 5.66 χ 10 ¹⁴ 0.2-0.3 1.22 x 10 ¹⁴ 0.3-0.4 4.45 x 10 ¹³ 0.4-0.5 2.09 X 10 ¹³ 0.5-0.6 1.15 x 10 ¹³ 0.6-0.7 6,95 x 10 ¹² 0.7-0.8 4,53 x 10 ¹² 0.8-0.9 3.11 x 10 " 0.9-1.0 2.23 X 10 "

Micrometer range number of 1.0-1.1 1.65 X 10 " 1.1-1.2 1.25 x 10 ¹² 1.2-1.3 9.80 X 10 ¹¹ 1.3-1.4. 7.76 x W ¹¹ 1.4-1.5 6.26 X 10 " 1.5-1.6 5.13 x 10 ¹¹ 1.6-1.7 4.25 X 10 ¹¹ 1.7-1.8 3.56 x 10 ¹¹ 1.8-1.9 3.02 X 10 ¹¹ 1.9-2.0 2.57 X 10 " 2.0-2.1 2.22 x 10 " 2.1-2.2 1.92 X 10 " 2.2-2.3 1.67 X 10 " 2.3-2.4 1.47x10 " 2.4-2.5 1.30 X 10 " 2.5-2.6 1.15 X 10 " 2.6-2.7 1.03 X 10 " 2.7-2.8 9.18 x 10 ¹⁰ 2.8-2.9 8.25 X 10 ¹⁰ 2.9-3.0 7.44 X 10 ¹⁰

The product samples were analyzed using a Horiba particle size distribution analyzer (Model CAPA700, Horiba Ltd., Miyanohigashi Kisshoin Minami-Ku Kyoto, Japan) to determine the relative proportion of each micron range given in Table 12 in total particle number (within the range of 0 1 μηι to 3,0 цт) to determine.

In addition, the product samples were subjected to ultracentrifugation analysis using a Beckman ultracentrifuge (Model No. L8-70M, Beckman Instruments, Inc., Palo Alto, CA). More specifically, samples were diluted with water to prepare 20% dispersions. These were shaken by hand and then sonicated for 30s at 100W to evenly disperse the diluted samples. Subsequently, the diluted samples were centrifuged at 25,000 rpm for 25 minutes at 22 ° C using a SW 28 rotor. Thereafter, the volume of the supernatant layer was measured and the volume occupied by the particles was determined by subtracting total volume to determine the percentage of the original, undiluted sample occupied by particulate matter. For any given sample, the number of particles within a certain size range can be determined by multiplying the values in Table 12 by the percentage of size distributions with the percentage of sample occupied by all particles as determined by ultracentrifugation. As already stated, ice cream products according to the present invention are uniquely characterized in that denatured protein particles having a diameter in the range from 0.5 to 2.5 μιτι are present in a number of more than 1 χ 10 ⁸ . It is advantageous if the products of the invention contain 1 × 10 ^{9 and up to} 1 × 10 ¹² or more of such particles.

Electron microscopic analysis of the particles formed in this example (Figure 3) shows that core-shell formation is present in a number of particles, with the egg-protein shell having a thinner layer than that of the particles used in the embodiment have been formed in Example 7.

Example 7

In the preparation of a protein-casein micellar cream substitute ingredient as described below, the following components were used:

Table 13 Weight percent (%) Remarks component 55,00 Share of 9.35% Ultrafiltered proteins on the total weight (17% protein) derZusammensetzg 22.65 Proportion of 2.5% Condensed skimmed milk on total weight (11% protein) derZusammens. 0.30 lecithin 5.00 sugar 0.35 Pectin (derived from apple) 0.17 ZurpH value Dist. citric acid 16.53 / at 6,6 water

100.00

Step A: Preparation

Sugar and pectin were mixed dry (premix A). In a Dorr-Oliver S-Series ultrafiltration system with a polysulfone membrane, pasteurized liquid egg whites were ultrafiltered to yield ultrafiltered proteins with a protein content of 17% (pre-preparation B). The lecithin was hydrogenated with reverse osmosis purified water in a STEPHAN vertical cutter Z-mixer VCM12 R & D model (premix C). A dilute solution of citric acid in reverse osmosis water was prepared (premix D).

Step B: Preparation of the batch

As shown in Figures 1 and 1A, the sugar-pectin mixture (premix A) was hydrogenated in reverse osmosis water in a high shear TRI BLENDER * mixer. To the hydrogenated sugar-pectin mixture in a hygienic batch tank, enough ultrapure protein (precursor B) and condensed skimmed milk are added to bring the protein concentration to the above mentioned targets. A sufficient amount of dilute citric acid (premix D) was added to the mixture to bring the pH of the premix to a pH of 6.6. To the mixture was added the hydrogenated lecithin (premix C) to complete the composition of the batch; this batch composition was then degassed in a VERSATOR degasser D-16 to reduce the amount of dispersed and dissolved oxygen.

Step C: Heat treatment

The batch composition was pumped into a series of heat processing units to preheat the batch before the heat processing treatment to a temperature between 120 ° F and 160 ⁰ F (49 ° C-71 "C). Then, the flow of the batch composition by hygienic pipe connections has been in the liquid processing system U.S. Patent Application Serial No. 127,170, issued December 2, 1987, at a flow rate of 120 pounds / hr (43.4 l / hr) and at a temperature of 176 ^o F-190 ° F (80 ° C) C-88 ° C) The blade of the processing equipment was set at 5,000 to 7,500 rpm to obtain a microparticulate protein casein micellar product (EWP / CM product) having the desired creamy structure Batch composition in the processing plant was about 30 seconds The resulting egg white casein micelle fat substitute was used immediately (in one process) to make a dairy desserts. When the process of making the dairy desserts was completed, a picking tube was used to pasteurize the egg white casein micelle fat substitute according to the FDA method, ie, at 177 ° F-190 ° F / 25 s (about 81 ° C-88 ° C / 25s). The pasteurized fat substitute was then cooled to 35 ° F-40 ° F (about 1.7 ° C-4.5 ° C) and stored at this temperature for future use.

Examples

The protein-casein micelle fat substitute prepared in Example 7 was used instead of creamy fat in the preparation of ice-cream type ice desserts (vanilla flavor) as an ingredient. This ice cream dessert has been judged by its creamy texture and overall acceptability by a number of consumers. At the same time, a group of three standard varieties of vanilla ice cream was assessed by separate groups of consumers.

The average ratings were creaminess (creaminess, flavor and suppleness) and the ratings for this ice cream product were always within the range of the commercial variety ratings, both initially and after five days of storage.

Example 9

An optimization study was conducted to determine the amount of the protein-casein micellar fat substitute of Example 7 required in an ice cream dessert intended to simulate a top-quality ice cream with a fat content of 16% butterfat. For the best prepared ice cream dessert, the following ratios existed between the major components given in Table 14.

Table 14

Component weight percent (%)

Total protein content 9.72%

Sucrose 11.4%

Protein Protein Kaseinmizellen-

Fat substitute out of B.7 31.84% ·

* Represent 38.8% of the total protein content.

It will be readily appreciated that the optimal amount of protein-casein micelle fat substitute of Example 7 required to simulate highest quality ice cream is about 32% of the weight of the ice cream product.

It should also be apparent to those skilled in the art that the optimum amount of protein-casein micellar fat substitute in a given formulation will depend on various factors such as the type of food product, the desired creaminess, the protein content of the protein-casein micelle fat substitute, the particle size of the microparticulate protein , the presence or absence of agglomeration blocking agents, polyhydric compounds and the like.

Routine taste tests are performed to determine the preferred composition of each food category.

Typical ice-cream dessert type compositions employing the proteinaceous casein micelle fat substitute of Example 7 as an ingredient contain the components listed in Table 15 below.

Table 15 Weight percent (%) Prefers component Area 31.8 Protein Protein Kaseinmizel- 25-40 len fat substitute from B, 7 36.6 Ultra-filtered skim milk 25-40 1.6 (4x) 0-3 10.0 Milk solids, fat free 8-20 0.9 sugar 0-2 0.4 Egg yolk 0-1 8th stabilizers 0-10 0 Corn syrup solids 0-1 1.1 Strength in requir. amount compensation Flavors · compensation water

• May contain fat cream or fat as a carrier for fat-soluble flavorings.

It will be readily appreciated that the improved battered ice cream products of the present invention, as described above with reference to illustrative "ice cream compositions", are products having physical and organoleptic properties of full fat products but a significantly lower caloric content and a higher nutritional value in qualitative terms Although the above illustrative 'ice cream' product formulations contain sucrose as a sweetener, it will be readily apparent to those skilled in the art that many other high potency sweeteners such as aspartame, alitame, azesulfame Kund sukralose (together with appropriate Fillers, if necessary) can be used as a substitute for sucrose in the preparation of the products according to the invention.

While the above illustrative "ice cream compositions" involve complete replacement of the milk fat with proteinaceous macrocolloidal preparations, it is to be understood that the high quality products of the invention also include desserts where the macrocolloid is only a fraction (eg, 50%). Similarly, even though "ice cream products" have been represented, the present invention may also advantageously be used in the preparation of reduced-fat or fat-free (ie, less than 1% fat) ice desserts such as ice milk, Egg cream, sorbet and the like and in glazes, spreads, sauces, dips, mousses, cream cake fillings and similar food products are normally used, which contain cream. It will be appreciated that various modifications and variations will become apparent to those skilled in the art upon consideration of the foregoing descriptions of the presently preferred embodiments of the invention, and thus limitations are limited to those formulated in the appended claims.

Claims (9)

1. A process for the preparation of a whipped low-calorie desserts, characterized in that a) the fat and / or oil contained therein is partially or completely replaced by a macrocolloid consisting of substantially non-agglomerated particles of denatured protein having an average distribution of the diameter of the particles in the dry state between about 0.1 μm and about 2, 0 цt, wherein less than about 2% of the total number of particles exceeds a diameter of 3.0 цt, and wherein the majority of these particles are generally spheroidal at about 800 times magnification under a standard light microscope, the particles in the hydrogenated state of this macrocolloid form having a substantially smooth, emulsion-like organoleptic character, or b) preparing a premix containing between 5% and 20% protein, of which 25% up to 100% heat coagulatable protein, and that this premix is subjected to heat pasteurization and high shear conditions to produce a product characterized by the presence of at least 1 × 10 ⁸ particles / cm ^{3 of} denatured protein having a diameter in the range of 0.5 to 2; 5 цт is characterized. 2. The method according to claim 1 a, characterized in that the macrocolloid replaced dairy fat. 3. The method according to claim 1 a, characterized in that this macrocolloid replaced more than 50% of the fat and / or oil. 4. The method according to claim 1 a, characterized in that this macrocolloid completely replaced fat and / or oil. 5. The method according to claim 1 a, characterized in that the ice cream dessert thus obtained is an analogue product to ice cream, which receives less than 1% fat. A method according to claim 1, characterized in that the macrocolloid consists of denatured protein selected from the group consisting of dairy whey protein, egg albumen, soybean and bovine serum albumin. 7. The method according to claim 1 a, characterized in that at least 1 x 10 ⁸ particles per cubic centimeter denatured protein having a diameter in the range of 0.5 цт to 2.5 цт are present. 8. The method according to claim 7, characterized in that between 1 x 10 ⁹ and 1 χ 10 ^{12 of} these particles / cm ³ are present. 9. The method according to claim 7, characterized in that less than 1% fat is present.