Highly stable, beatable compositions comprising beta-casein.

Abstract

Disclosed herein are food formulations comprising β-casein as the primary casein protein. Also disclosed herein are compositions comprising casein protein enriched in β-casein. Further disclosed herein are whippable or non-whippable emulsion structures comprising β- casein in amounts higher than those typically found in milk and methods of making the compositions.

Description

Highly stable, beatable compositions comprising beta-casein. CROSS-REFERENCE TO RELATED REQUESTS

[0001] This application claims priority to Provisional Patent Application No. US 63 / 490,439, filed March 15, 2023, which is incorporated herein by reference in its entirety. FIELD

[0002] The present invention relates to food formulations that include β-casein as the principal casein protein. Compositions comprising casein protein enriched with β-casein are described herein. Also described herein are churning and non-churning emulsions containing β-casein in amounts greater than those normally found in milk, and methods for manufacturing the compositions. INTRODUCTION

[0003] Caseins are proteins found in milk and can be separated from milk for use in their natural form. Caseins can be further modified by being dissociated into caseinates or partially hydrolyzed into peptides. All three forms are widely used in food applications due to their diverse technofunctional properties, such as solubility, emulsification, foaming, stabilization, water binding, gelation, thermal stability, and acid stability.

[0004] Traditionally, sodium caseinate, a casein derivative in which the individual caseins exist in soluble or monomeric form, was used as an emulsifying agent for many frosting and whipped cream applications due to its solubility, emulsifying ability, and emulsion stability. Sodium caseinate Petition 870250080886, dated 09 / 09 / 2025, page 9 / 88 2 / 51 consists of soluble caseins with varying proportions of αS1 casein, αS2 casein, β-casein, and κ-casein. Caseins have flexible structures with a high proportion of nonpolar groups that are more effective at reducing interfacial tension than rigid proteins with fewer nonpolar groups. β-casein has the highest surface activity, followed by monodisperse casein micelles. αS-casein and κ-casein have similar surface activities; however, they have lower surface activity compared to β-casein and monodisperse casein micelles. It is not known which of the above caseins contribute to the emulsification and stabilization of emulsions.

[0005] Thus, there is a need to determine which of the aforementioned caseins offers desirable emulsifying properties and stability for food compositions, such as high-fat emulsions. SUMMARY

[0006] In one aspect, this disclosure relates to an emulsion composition comprising a fat and a protein, wherein the protein comprises more than 45% by weight of β-casein based on the total amount of casein present in the composition. In one embodiment, the composition comprises: from about 5% by weight to about 45% by weight of fat; from about 0.001% by weight to about 3% by weight of protein; from about 0% by weight to about 55% by weight of a sweetener; from about 0% by weight to about 3% by weight of one or more stabilizers; from about 0.0001% by weight to about 2% by weight of buffer salts; and from about 0% by weight to about 3% by weight of one or more emulsifiers. In another embodiment, the composition comprises: from about 5% by weight to about 35% by weight of fat; from about 1% by weight to about 2.5% by weight of protein Petition 870250080886, dated 09 / 09 / 2025, page 10 / 88 3 / 51 protein; from about 5% by weight to about 45% by weight of a sweetener; from about 0.5% by weight to about 3% by weight of one or more stabilizers; from about 0.5% by weight to about 2% by weight of buffer salts; and from about 0.5% by weight to about 3% by weight of one or more emulsifiers. In another embodiment, the fat is a milk fat, a vegetable fat, vegetable oil, algae oil, fermented oil of bacteria, yeasts or fungi, hydrogenated oil, hydrogenated and interesterified oil, hydrogenated, mixed and interesterified oil, medium-chain triglyceride (MCT) vegetable oil, milk fat, ghee, anhydrous milk fat, butter oil, or a combination thereof. In another embodiment, the protein is an animal protein, a recombinant milk protein, a protein of vegetable origin, or a combination thereof. In another form, the protein is natural casein, recombinant casein, or a combination thereof.In another embodiment, the composition comprises a total κ-casein content of less than 0.03% by weight based on the total composition. In another embodiment, the protein is enriched with animal and / or recombinant β-casein. In another embodiment, the β-casein is natural or recombinant. In another embodiment, the β-casein is recombinant and comprises an amino acid sequence that is about 60% to about 100% identical to an amino acid sequence of a mammalian milk protein, such as a cow's milk protein, a sheep's milk protein, a camel's milk protein, a yak's milk protein, a buffalo milk protein, a horse's milk protein, or a goat's milk protein. In another embodiment, the proportion of β-casein is about 45% to about 100% of the total amount of casein in the composition.In another embodiment, β-casein is in micellar form or monomeric form; when β-casein is in monomeric form, the protein particle size is less than 50 nm. In another embodiment, β-casein is in... Petition 870250080886, dated 09 / 09 / 2025, page 11 / 88 4 / 51 micellar form or monomeric form; when β-casein is in micellar form, the β-casein has a protein particle size of less than 500 nm. In another embodiment, β-casein has a zeta potential of about -50 mV to about -15 mV in a pH 7.0 buffer. In another embodiment, the protein is in liquid or powder form, wherein the powder form is produced by spray drying, roller drying, drum drying, or freeze-drying of the protein to remove water. In another embodiment, the protein is a single type of native milk protein, a single type of recombinant milk protein, or a combination thereof. In another embodiment, the single type of protein is β-casein. In another embodiment, the protein is composed of two or more different types of animal milk proteins, recombinant milk proteins, and plant-derived proteins. In another embodiment, the protein is with or without post-translational modifications.In another embodiment, post-translational modifications are one or more of the glycosylation and phosphorylation modifications. In another embodiment, the protein is phosphorylated. In another embodiment, the protein includes non-native phosphorylation. In another embodiment, recombinant caseins are produced by a fungal cell, a yeast cell, a bacterial cell, algae, or a transgenic method. In another embodiment, the sweetener is a nutritive sweetener, a non-nutritive sweetener, or a combination thereof. In another embodiment, the nutritive sweetener is one or more of the following: sucrose, lactose, glucose, fructose, corn syrup solids, high-fructose corn syrup, dextrose, maltodextrin, brown sugar, honey and maple syrup, syrups; soluble / insoluble fibers derived from corn, wheat, peas, rice, oats, coconut, barley and / or tapioca; fructo- and galacto-oligosaccharides; and hydrolyzed cereal flour; or a combination thereof.In another category, the non-nutritive sweetener is one or more of the following: sucralose, aspartame, saccharin, stevia, monk fruit extract, neotame, advantame, acesulfame. Petition 870250080886, dated 09 / 09 / 2025, page 12 / 88 5 / 51 potassium, sugar alcohols, such as maltitol, xylitol, sorbitol, erythritol, mannitol, isomalt, lactitol, hydrogenated starch hydrolysates or a combination thereof. In another embodiment, the sweetener is one or more of brazzein, curculin, mabinlin, miraculin, monellin, pentadin and thaumatin. In another embodiment, the fat comprises one or more lipids derived from a plant, an animal, one or more lipids derived from milk or a combination thereof. In another embodiment, the fat comprises one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid.In another embodiment, the one or more monoglycerides, diglycerides, triglycerides and / or phospholipids are transesterified monoglycerides, diglycerides, triglycerides and / or phospholipids of vegetable origin comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid. In another embodiment, the fat is hydrogenated oil, interesterified oil, hydrogenated and interesterified oil, hydrogenated, blended and interesterified oil or a combination thereof. In another embodiment, the one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprise fatty acyl chains in a percentage that resembles a percentage of the fatty acyl chains found in milk or a dairy product derived from mammals. In another embodiment, the composition may be whipped. In another embodiment, the composition may not be whipped.In another embodiment, the composition is a cooking cream or a coffee creamer. In another embodiment, the fat is fully hydrogenated, partially hydrogenated, interesterified, non-hydrogenated, or hydrogenated and interesterified. In another embodiment, the fat is fully hydrogenated. In another embodiment, the composition is... Petition 870250080886, dated 09 / 09 / 2025, page 13 / 88 6 / 51 also includes a crystallizer, a flavoring agent, a salt, a preservative, or a combination thereof. In another embodiment, the protein is one or more of the following: monomeric caseins, sodium caseinate, calcium caseinate, potassium caseinate, acid casein, rennet casein, micellar protein, and globular protein. In another embodiment, the globular protein is one or more of the following: milk-derived proteins, vegetable protein, alpha-lactalbumin, beta-lactoglobulin, ovalbumin, ovoglobulin, and recombinant protein. In another embodiment, the micellar protein is micellar casein, a recombinant micellar casein, or a combination thereof. In another embodiment, the vegetable protein is any protein based on cereals, legumes, or seeds and is present in an amount of about 0.05% by weight to about 2.5% by weight. In another embodiment, micellar casein is sodium caseinate or calcium caseinate and is present in an amount of about 0.05% by weight to about 2.5% by weight.In another embodiment, the stabilizer is one or more of the following: alginate, carrageenan, guar gum, cellulose, such as methylcellulose, microcrystalline cellulose, carboxymethylcellulose, hydroxypropylmethylcellulose (HPMC), sorbitol, xanthan gum, tara gum, locust bean gum, gellan gum (such as high acyl content, low acyl content), beet pectin, skimmed milk powder, whole milk powder, partially skimmed milk powder, butter powder, dairy solids, modified starch, agar-agar, gelatin, gum arabic, konjac, pectin, maltodextrin, and tragacanth.In another embodiment, the emulsifier is one or more of the following: diacetyltartaric acid esters of mono- and / or diglycerides, lactic acid esters of mono- and / or diglycerides, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyglycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose esters, sucrose monostearate, monoglyceride, beeswax, camauba wax, candelilla wax, vegetable waxes, fruit waxes, animal waxes, acid esters. Petition 870250080886, dated 09 / 09 / 2025, page 14 / 88 7 / 51 polyglycerol fatty acids and polyglycerol polyricinoleate (PGPR). In another embodiment, the buffer salt is one or more of any sodium, potassium or calcium citrate, phosphate, carbonate salts, such as sodium polyphosphates, orthophosphate, pyrophosphate, hexametaphosphate, mono- or di-phosphate salts, mono- or di-carbonates and halide salts.

[0007] In another aspect, this disclosure refers to a food product comprising any of the compositions disclosed herein. In one embodiment, the food product is a dairy product, a non-animal-derived product, a beverage product, or a combination thereof. In another embodiment, the food product is a coffee creamer, a cooking creamer, a whipped cream, or a similar emulsion with a low or high fat content. In another embodiment, the food product contains from 0.001% by weight to about 3% by weight of protein.

[0008] In another aspect, this disclosure relates to a method of manufacturing the composition of any of clauses 1 to 46, wherein the method comprises: forming an oil phase comprising fat; forming an aqueous phase comprising protein; adjusting the oil phase and the aqueous phase from about 15 °C to about 75 °C; mixing the oil phase and the aqueous phase to form a mixture; homogenizing the mixture to form an emulsion; heating the emulsion from about 50 °C to about 145 °C; and cooling the emulsion from about 2 °C to about 30 °C. In one embodiment, the method further comprises packaging the emulsion under sterile or non-sterile conditions. In another embodiment, the method further comprises storing the emulsion at approximately -18 °C to approximately -15 °C, approximately 3 °C to approximately 5 °C, or approximately 18 °C to approximately 25 °C. In yet another embodiment, the aqueous phase further comprises stabilizers, emulsifiers, and buffering salts.In another embodiment, the method also includes aeration of the emulsion or quiescent storage of the emulsion. Petition 870250080886, dated 09 / 09 / 2025, page 15 / 88 8 / 51 In another embodiment, aeration comprises beating, mixing using a planetary mixer, or beating using a continuous beating machine. In another embodiment, the method further comprises heat treatment, pasteurization, or sterilization of the emulsion. In another embodiment, the heat treatment, pasteurization, or sterilization includes retort treatment, high hydrostatic pressure, ultraviolet radiation, irradiation, or ultra-high temperature processing. In another embodiment, the emulsion has improved storage stability compared to a corresponding emulsion.

[0009] In another aspect, this disclosure refers to a method of preparing a whipped emulsion, wherein the method may comprise whipping any of the emulsions described in this document, wherein the whipping may be carried out between 2 °C and 8 °C.

[0010] This disclosure provides other aspects and modalities that will become apparent in light of the detailed description and accompanying figures. BRIEF DESCRIPTION OF THE DRAWINGS

[0011] Figure 1 is a graph showing a capillary electrophoresis elution profile for a beta-casein extract.

[0012] Figure 2 is an RP-HPLC chromatogram of the neutralized beta-casein extract, showing the high purity of beta-casein compared to other milk proteins.

[0013] Figure 3 is a graph showing particle size density (PSD) data for protein particles in solution measured by the Zetasizer DLS technique.

[0014] Figure 4 is a graph showing air-water interface surface tension measurements made with an Automatic Drop Tensiometer in the rising drop setting after 25 minutes of equilibration time.

[0015] Figure 5 is a graph showing the decay of height. Petition 870250080886, dated 09 / 09 / 2025, page 16 / 88 9 / 51 of the foam over time of 0.25% protein solutions, as measured by the Dynamic Foam Analyzer.

[0016] Figure 6 shows images of a whipped sodium caseinate composition and a whipped beta-casein composition.

[0017] Figure 7 is a graph showing the effect of increasing the proportion of beta-casein in protein mixtures with sodium caseinate on particle size in simple emulsions (20% canola oil).

[0018] Figure 8 shows images of the initial rosettes (t=0) of the tapped samples E, F, G, H, I and J.

[0019] Figure 9 shows images of the stability bowls of the beaten samples E, F, G, H, I and J after 24 hours of refrigeration (i.e., from about 2 °C to about 4 °C). DETAILED DESCRIPTION

[0020] Due to its amphiphilic structure, β-casein has emulsifying and foam-stabilizing properties. This document describes a protein solution enriched with β-casein. The experiments described in this document characterize the functionality of β-casein in emulsions for creams, coatings, and high-fat coatings. Furthermore, it has been demonstrated in this document that enriching protein solutions with β-casein leads to an overall reduction in protein content and cost savings. Finally, in addition to bovine-derived casein proteins, non-bovine-derived casein proteins from recombinant sources can also be used to improve emulsion properties. 1. DEFINITIONS

[0021] Unless otherwise defined, all technical and scientific terms used in this document have the same meaning as commonly understood by one skilled in the art. In case of conflict, this document, including definitions, shall prevail. Petition 870250080886, dated 09 / 09 / 2025, page 17 / 88 10 / 51 Preferred methods and materials are described below, although methods and materials similar or equivalent to those described herein may be used in practice or in testing the present invention. All publications, patent applications, patents and other references mentioned in this document are incorporated by reference in their entirety. The materials, methods and examples described in this document are illustrative only and are not intended to be a limiting factor.

[0022] The terms “comprises”, “includes”, “that has”, “has”, “may”, “contains”, and variants thereof, as used in this document, are intended to be open transitional phrases, terms, or words that do not preclude the possibility of additional acts or structures. The singular forms “a”, “and”, and “the” include plural references unless the context clearly indicates otherwise. This disclosure also includes other modalities “that comprises”, “that consists of”, and “that essentially consists of” the modalities or elements presented in this document, whether explicitly stated or not.

[0023] For the recitation of numerical intervals described in this document, each intermediate number with the same degree of precision is explicitly contemplated. For example, for the interval 6-9, the numbers 7 and 8 are contemplated in addition to 6 and 9; for the range 6 to 9, the numbers 7 and 8 are contemplated in addition to 6 and 9; and for the range 6.0 to 7.0, the numbers 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9 and 7.0 are explicitly contemplated.

[0024] The term “about” or “approximately,” as used in this document and applied to one or more values ​​of interest, refers to a value that is similar to a stated reference value or within an acceptable error range for the specific value, as determined by one skilled in the art, which will depend in part on Petition 870250080886, dated 09 / 09 / 2025, p. 18 / 88 11 / 51 how the value is measured or determined, such as the limitations of the measurement system. In certain respects, the term “about” refers to a range of values ​​that fall within 20%, 19%, 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1% or less in any direction (greater or less than) the stated reference value, unless otherwise indicated or evident from the context (except when such a number exceeds 100% of a possible value). Alternatively, “about” may mean within 3 or more standard deviations, as is the practice in the field. Alternatively, as in the case of biological systems or processes, the term "about" can mean within an order of magnitude, preferably within 5 times, and more preferably within 2 times, of a value.

[0025] The term “casein monomer”, as used in this document, refers to a polypeptide comprising a sequence of at least 20 amino acids (for example, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90, at least 100 or at least 150 and, normally, not more than 250 amino acids) that is at least 80% identical (for example, at least 85%, at least 90% identical, at least 99% identical) to an amino acid sequence in a casein and that is repeated in a polymer provided in this document. For example, the casein monomer may comprise a polypeptide with a sequence of about 20 amino acids to about 220 amino acids; about 40 amino acids to about 200 amino acids; about 60 amino acids to about 180 amino acids; about 80 amino acids to about 160 amino acids; or about 100 amino acids to about 140 amino acids.For example, the casein monomer cannot exceed 220 amino acids. Non-limiting examples of caseins include β-casein, γ-casein, κ-casein, aS1-casein and aS2-casein. Petition 870250080886, dated 09 / 09 / 2025, p. 19 / 88. 12 / 51 casein.

[0026] “Cheese”, as used in this document, refers to a group of fermented milk-based products that involve one of the typical examples of food preservation, such as the gelation of casein by means of isoelectric (acid) or enzymatic (rennet) coagulation. Some cheeses are produced by a combination of heat and acid, and an even smaller number by thermal evaporation and reduction of water activity by removing water, with or without the addition of NaCl. Cheeses produced by acid coagulation or by heat / acid are generally consumed fresh, while rennet cheeses are almost always matured before consumption through the action of a complex array of enzymes.

[0027] “Cheese products”, as used in this document, refers to pasteurized processed cheese products (PCPs) that are cheese-based foods produced by grinding, mixing and melting one or more natural cheeses and optional ingredients into a smooth homogeneous mixture with the aid of heat, mechanical shearing and (usually) emulsifying salts (ES).

[0028] The term “host cell” or “recombinant host cell,” as used in this document, refers to a cell comprising a recombinant polynucleotide that has been introduced. It should be understood that these terms refer not only to the specific cell in question but also to the progeny of that cell. Because certain modifications may occur in subsequent generations due to mutations or environmental influences, this progeny may not be identical to the parent cell but is still included within the scope of the term “host cell” or “recombinant host cell,” as used in this document.

[0029] The term “identical”, as used in this document in the context of polynucleotide or polypeptide sequences, refers Petition 870250080886, dated 09 / 09 / 2025, page 20 / 88 13 / 51 refers to residues in the two sequences that are the same when aligned for maximum match. There are several different algorithms known on the market that can be used to measure the identity of polynucleotide or polypeptide sequences. For example, sequences can be compared using FASTA (e.g., using the standard parameters provided in the Wisconsin Package Version 10.0, Genetics Computer Group (GCG), Madison, Wis.), Gap (e.g., using the standard parameters provided in the Wisconsin Package Version 10.0, Genetics Computer Group (GCG), Madison, Wis.), Bestfit, ClustalW (e.g., using the standard parameters of version 1.83) or BLAST (e.g., using reciprocal BLAST, PSI-BLAST, BLASTP, BLASTN) (see, for example, Pearson. 1990. Methods Enzymol. 183:63; Altschul et al. 1990. J. Mol. Biol. 215:403).

[0030] “Native” or “natural,” as used in this document, refers to an ingredient derived from an animal or plant that is not synthesized from other forms of the ingredient or is not recombinant. “Native casein” or “natural casein,” as used in this document, refers to a casein derived from bovine or mammalian milk that is not synthesized from other forms of casein or is not recombinant.

[0031] The term “post-translational modification,” or its acronym “PTM,” as used in this document, refers to the covalent attachment of a chemical group to a protein after the protein’s biosynthesis. PTMs can occur in the amino acid side chain of the protein or at its C or N termini. Non-limiting examples of PTMs include glycosylation (i.e., covalent attachment to proteins of glycan groups (i.e., monosaccharides, disaccharides, polysaccharides, glycans)). Petition 870250080886, dated 09 / 09 / 2025, page 21 / 88 14 / 51 Modified, glycans with galf, sulfate and / or phosphate residues), monosaccharides, disaccharides, polysaccharides, linear glycans, branched glycans, glycans with galf residues, glycans with sulfate and / or phosphate residues, D-glucose, D-galactose, D-mannose, L-fucose, N-acetyl-D-galactose amine, N-acetyl-D-glucose amine, N-acetyl-D-neuraminic acid, galactofuranose, phosphodiesters, N-acetylglucosamine, N-acetylgalactosamine, sialic acid and combinations thereof; see, for example, Deshpande et al. 2008. Glycobiology 18(8):626) via C-linkage, N-linkage or O-linkage, or via glypiation (i.e., addition of a glycosylphosphatidylinositol anchor) or phosphoglycosylation (i.e., linked through the phosphate of a phosphoserine), phosphorylation (i.e., covalent linkage to proteins of phosphate groups), alkylation (i.e., covalent linkage to proteins of alkane groups (e.g., methane group in methylation) and lipidation (i.e.,covalent bonding of a lipid group (e.g., isoprenoid group in prenylation and isoprenylation (e.g., farnesol group in farnesylation, geraniol group in geranylation, geranylgeraniol group in geranylgeranilation), fatty acid group in fatty acylation (e.g., myristic acid in myristoylation, palmitic acid in palmitoylation), glycosylphosphatidylinositol anchor in glypiation), hydroxylation (i.e., covalent bonding of a hydroxide group), sumoylation (i.e., binding to proteins of the Ubiquitin-like Small Modifier (or SUMO) protein), nitrosylation (i.e., binding to proteins of an NO group), and tyrosine nitration (i.e., binding to tyrosine residues of proteins of nitrate groups).

[0032] The term “recombinant protein” or “recombinant β-casein”, as used in this document, refers to a protein or β-casein, respectively, that is produced recombinantly (i.e., produced by a recombinant host cell). The expression of the protein in the host cell may be transient or stable. Petition 870250080886, dated 09 / 09 / 2025, page 22 / 88 15 / 51

[0033] The term “recombinant polynucleotide,” as used in this document, refers to a polynucleotide that has been removed from its natural environment, a polynucleotide that is not associated with all or part of an adjacent or nearby polynucleotide when found in nature, a polynucleotide that is operationally linked to a polynucleotide to which it is not linked in nature, or a polynucleotide that does not occur in nature. The term may be used, for example, to describe cloned DNA isolates or a polynucleotide comprising a chemically synthesized nucleotide analog. A polynucleotide is also considered “recombinant” if it contains any genetic modification that does not occur naturally. For example, an endogenous polynucleotide is considered a “recombinant polynucleotide” if it contains an insertion, deletion, or substitution of one or more nucleotides artificially introduced, for example, by human intervention.This modification can introduce into the polynucleotide a point mutation, a substitution mutation, a deletion mutation, an insertion mutation, a missense mutation, a frameshift mutation, a duplication mutation, an amplification mutation, a translocation mutation, or an inversion mutation. The term includes a polynucleotide on the chromosome of a host cell, as well as a polynucleotide that is not on the chromosome of a host cell (for example, a polynucleotide that is included in an episome).

[0034] As used in this document, “sweetener” refers to an ingredient and / or a mixture of ingredients that imparts sweetness to a final product.

[0035] “Yogurt”, as used in this document, refers to the food produced by culturing one or more optional dairy ingredients with a characterizing bacterial culture containing lactic acid-producing bacteria, such as Lactobacillus delbrueckii subsp. Petition 870250080886, dated 09 / 09 / 2025, p. 23 / 88 16 / 51 bulgaricus and Streptococcus thermophilus, at pH 4.6 or less.

[0036] “Yogurt products”, as used in this document, refers to products in which yogurt is used as an ingredient, such as yogurt with fruit inclusions, smoothies, cultured drinks and the like.

[0037] Unless otherwise defined in this document, the scientific and technical terms used in connection with this disclosure shall have the meanings that are commonly understood by those skilled in the art. For example, all nomenclatures used in connection with food science, microbiology, biochemistry, and chemistry described in this document, as well as their techniques, are well known and commonly used in the art. The meaning and scope of terms should be clear; however, in the case of any latent ambiguity, the definitions given in this document shall take precedence over any dictionary or extrinsic definition. Furthermore, unless otherwise required by the context, singular terms shall include plurals and plural terms shall include the singular. 2. COMPOSITION

[0038] Compositions are provided for emulsifying and stabilizing food products that can be whipped and those that cannot be whipped. In some embodiments, the composition may include a protein, such as β-casein, and a fat. The total protein content can vary from approximately 0.05% to approximately 3%, approximately 0.10% to approximately 3%, approximately 0.15% to approximately 3%, approximately 0.25% to approximately 3%, approximately 0.50% to approximately 3% by weight, approximately 0.50% to approximately 3% by weight, approximately 1% to approximately 3% by weight, approximately 1.5% to approximately 3% by weight, approximately 2% to approximately 3% by weight, approximately 2.5% to approximately 3% by weight, approximately 0.05% to approximately 2.5% by weight, approximately 0.05% to approximately 2% by weight, approximately 0.05% to approximately 1.5% by weight. Petition 870250080886, dated 09 / 09 / 2025, p. 24 / 88 17 / 51 weight, approximately 0.05% by weight to approximately 1% by weight, approximately 0.05% to approximately 0.50% by weight, approximately 0.05% to approximately 0.25% by weight, approximately 0.05% to approximately 0.15% by weight, or approximately 0.05% to approximately 0.10% by weight of the composition. In some embodiments, the total protein content may vary from approximately 0.05% by weight to approximately 3% by weight of the composition. The protein may contain from 0.01% by weight to approximately 100% by weight of casein based on the total amount of protein present in the composition. Protein may comprise from about 0.01% by weight to about 100% by weight, about 0.5% by weight to about 100% by weight, about 1% by weight to about 100% by weight, about 10% by weight to about 100% by weight, about 20% by weight to about 100% by weight, about 30% by weight to about 100% by weight, about 40% by weight to about 100% by weight, about 50% by weight to about 100% by weight, about 60% by weight to about 100% by weight, about 70% by weight to about 100% by weight.approximately 80% by weight to approximately 100% by weight, approximately 90% by weight to approximately 100% by weight, approximately 0.01% by weight to approximately 90% by weight, approximately 0.01% by weight to approximately 80% by weight, approximately 0.01% by weight to approximately 70% by weight, approximately 0.01% by weight to approximately 60% by weight, approximately 0.01% by weight to approximately 50% by weight, approximately 0.01% by weight to approximately 40% by weight, approximately 0.01% by weight to approximately 30% by weight, approximately 0.01% by weight to approximately 20% by weight, approximately 0.01% by weight to approximately 10% by weight, approximately 0.01% by weight to approximately 1% by weight or approximately 0.5% by weight The protein may contain from 45% to approximately 100% by weight of β-casein based on the total amount of casein present in the composition. The protein may comprise from approximately 45% to approximately 100% by weight, or from approximately 50% to approximately 100% by weight. Petition 870250080886, dated 09 / 09 / 2025, p. 25 / 88 18 / 51 approximately 55% by weight to approximately 100% by weight, approximately 60% by weight to approximately 100% by weight, approximately 65% ​​by weight to approximately 100% by weight, approximately 70% by weight to approximately 100% by weight, approximately 75% by weight to approximately 100% by weight, approximately 80% by weight to approximately 100% by weight, approximately 85% by weight to approximately 100% by weight, approximately 90% by weight to approximately 100% by weight, approximately 95% by weight to approximately 100% by weight, approximately 45% by weight to approximately 95% by weight, approximately 45% by weight to approximately 90% by weight, approximately 45% by weight to approximately 85% by weight, approximately 45% by weight to approximately 80% by weight, approximately 45% to approximately 75%, approximately 45% to approximately 70%, approximately 45% to approximately 65%, approximately 45% to approximately 60%, approximately 45% to approximately 55%, or approximately 45% to approximately 50% of β-casein based on the total amount of casein present in the composition.The protein content may be equal to or greater than 45% by weight, greater than 50% by weight, greater than 55% by weight, greater than 60% by weight, greater than 65% by weight, greater than 70% by weight, greater than 75% by weight, or greater than 80% by weight of β-casein based on the total amount of casein present in the composition. The composition may also include sweeteners, stabilizers, buffering salts, bulking agents, and emulsifiers. A. PROTEIN.

[0039] The composition may comprise from about 0.001% by weight to about 3% by weight, about 0.01% by weight to about 3% by weight, about 0.1% by weight to about 3% by weight, about 1% by weight to about 3% by weight, about 2% by weight to about 3% by weight, about 0.001% by weight to about 2% by weight, about 0.001% by weight to about 1% by weight, about 0.001% by weight to about 0.1% by weight or about 0.001% by weight to about 0.01% by weight of a protein. In some embodiments, the composition Petition 870250080886, dated 09 / 09 / 2025, p. 26 / 88 19 / 51 may comprise from about 0.001% by weight to about 3% by weight of a protein. In some embodiments, the composition may contain from about 1% by weight to about 2% by weight of the protein. The protein may be in a liquid or powder form. The powder form may be produced by spray drying, roller drying, drum drying, or freeze-drying of the protein to remove water. The protein may be devoid of one or more post-translational modifications. For example, the protein may be devoid of one or more of the following post-translational modifications: glycosylation, phosphorylation, or a combination thereof. The protein may be phosphorylated. The protein may include non-native phosphorylation. The protein may be one or more of the monomeric caseins, sodium caseinate, calcium caseinate, micellar protein, and globular protein.Globular protein can be one or more of the following: milk-derived protein, vegetable protein, beta-lactoglobulin, ovalbumin, alpha-lactalbumin, ovoglobulin, bacterial protein, fungal protein, and recombinant protein. Micellar protein can be micellar casein or recombinant micellar casein. Casein can exist in micellar, aggregated, or monomeric form. Monomeric casein can be sodium caseinate or potassium caseinate. Aggregated casein can be calcium caseinate. Micellar casein can be micellar casein concentrate / isolate, milk protein concentrate / isolate, skimmed milk powder, whole milk powder, partially skimmed milk powder, or buttermilk powder.Caseins may be present in the composition in an amount of approximately 0.05% by weight to approximately 2.5% by weight, approximately 0.1% by weight to approximately 2.5% by weight, approximately 0.5% by weight to approximately 2.5% by weight, approximately 1.0% by weight to approximately 2.5% by weight, approximately 1.5% by weight to approximately 2.5% by weight, approximately 2.0% by weight to approximately 2.5% by weight, approximately 0.05% by weight to approximately 2.0% by weight, approximately 0.05% by weight to approximately 1.5% by weight, approximately 0.05% by weight to approximately 1.0% by weight. Petition 870250080886, dated 09 / 09 / 2025, page 27 / 88 20 / 51 approximately 0.05% by weight to approximately 0.5% by weight or approximately 0.05% by weight to approximately 0.1% by weight. In some embodiments, caseins may be present in the composition in an amount of approximately 0.05% by weight to approximately 2.5% by weight. The caseins present in the composition do not exceed 2.6% by weight. Vegetable protein can be any protein isolate or concentrate based on cereals, legumes, or seeds and may be present in the composition in an amount of approximately 0.05% to approximately 2.0%, approximately 0.1% to approximately 2.0%, approximately 0.5% to approximately 2.0%, approximately 1.0% by weight to approximately 2.0% by weight, approximately 1.5% by weight to approximately 2.0% by weight, approximately 0.05% by weight to approximately 1.5% by weight, approximately 0.05% by weight to approximately 1.0% by weight, approximately 0.05% by weight to approximately 0.5% by weight, or approximately 0.05% by weight to approximately 0.1% by weight.In some embodiments, the vegetable protein may be any isolate or concentrate of cereal, legume, or seed-based protein and may be present in the composition in an amount of about 0.05% by weight to about 2% by weight. The protein may be of two different types: animal and / or recombinant milk proteins. The protein may be a single type of native milk protein or a single type of recombinant milk protein. The single type of protein may be β-casein.

[0040] The compositions disclosed in this document are not used for cheese or yogurt, or cheese products or yogurt products. Furthermore, k-casein is not normally used in the whipped products described in this document.

[0041] In some embodiments, the disclosed compositions may include a total κ-casein content of less than 0.03% by weight based on the total composition. Amounts less than Petition 870250080886, dated 09 / 09 / 2025, page 28 / 88 21 / 51 at 0.03% by weight can help prevent product instability caused by age gelation. K-casein can participate in sulfhydryl-disulfide exchange reactions with other proteins containing sulfur-containing amino acids, leading to age gelation and subsequent instability. See: Nair and Corredig, Journal of Dairy Science, 2021; 104(1): 92-101.

[0042] β-casein can be derived from bovine milk, such as whole milk (e.g., milk with about 3.5% milk fat), reduced-fat milk (e.g., milk with about 2% milk fat), low-fat milk (e.g., milk with about 1% milk fat), and fat-free milk (e.g., milk with about 0.8% or less by weight of milk fat). β-casein can be separated from the other milk components to produce a β-casein that is purified from about 45% by weight to about 99% by weight on a dry basis. For example, β-casein can be purified to about 45% by weight, about 50% by weight, about 55% by weight, about 60% by weight, about 65% by weight, about 70% by weight, about 75% by weight, about 80% by weight, about 83% by weight, about 86% by weight, about 89% by weight, about 91% by weight, about 92% by weight, about 93% by weight, or about 99% by weight on a dry basis.

[0043] β-casein may be recombinant and comprises an amino acid sequence that may be about 60% to about 100%, about 70% to about 100%, about 80% to about 100%, about 90% to about 100%, about 60% to about 90%, about 60% to about 80%, or about 60% to about 70% identical to an amino acid sequence of a cow's milk protein, sheep's milk protein, horse's milk protein, or goat's milk protein. B. FAT Petition 870250080886, dated 09 / 09 / 2025, p. 29 / 88 22 / 51

[0044] One or more fats are useful in the compositions disclosed in this document. The fat may be a milk fat, a vegetable fat, a vegetable oil, an algae, a fungus, a recombinant product or a combination thereof. The fat may be fully hydrogenated, partially hydrogenated, interesterified or hydrogenated and interesterified or a combination of these options with or without unmodified fat.The composition may comprise from about 5% by weight to about 45% by weight, about 10% by weight to about 45% by weight, about 15% by weight to about 45% by weight, about 20% by weight to about 45% by weight, about 25% by weight to about 45% by weight, about 30% by weight to about 45% by weight, about 35% by weight to about 45% by weight, about 40% by weight to about 45% by weight, about 5% by weight to about 40% by weight, about 5% by weight to about 35% by weight, about 5% by weight to about 30% by weight, about 5% by weight to about 25% by weight, about 5% by weight to about 20% by weight, about 5% by weight to about 15% by weight, or about 5% by weight to about 10% by weight of fat. In some forms, the composition may comprise about 25% by weight to about 35% by weight of fat.

[0045] Fat may include one or more lipids derived from a plant, one or more lipids derived from milk, or a combination thereof.

[0046] Fat may comprise one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid. The one or more monoglycerides, diglycerides, triglycerides and / or phospholipids may be a trans monoglyceride, diglyceride, triglyceride and / or phospholipid Petition 870250080886, dated 09 / 09 / 2025, page 30 / 88 23 / 51 esterified of vegetable origin. One or more monoglycerides, diglycerides, triglycerides and / or phospholipids may comprise fatty acyl chains in a percentage that resembles a percentage of fatty acyl chains found in milk or dairy products derived from mammals. C. SWEETENER

[0047] The composition may comprise from about 0% by weight to about 45% by weight, about 5% by weight to about 45% by weight, about 10% by weight to about 45% by weight, about 15% by weight to about 45% by weight, about 20% by weight to about 45% by weight, about 25% by weight to about 45% by weight, about 30% by weight to about 45% by weight, about 35% by weight to about 45% by weight, about 40% by weight to about 45% by weight, about 0% by weight to about 40% by weight, about 0% by weight to about 35% by weight, about 0% by weight to about 30% by weight, about 0% by weight to about 25% by weight, about 0% by weight The composition may comprise approximately 20% by weight, approximately 0% by weight to approximately 15% by weight, approximately 0% by weight to approximately 10% by weight, or approximately 0% by weight to approximately 5% by weight of a sweetener. In some embodiments, the composition may comprise from approximately 5% by weight to approximately 25% by weight of a sweetener. The sweetener may be a nutritive sweetener or a non-nutritive sweetener.The nutritive sweetener may be one or more of the following: sucrose, lactose, glucose, fructose, corn syrup solids, high-fructose corn syrup, dextrose, maltodextrin, brown sugar, honey, and maple syrup. The non-nutritive sweetener may be one or more of the following: sucralose, aspartame, saccharin, stevia, monk fruit extract, neotame, advantame, and acesulfame potassium. The sweetener may be one or more of the following: brazzein, curculin, mabinin, miraculin, monellin, pentadin, and thaumatin. D. STABILIZER Petition 870250080886, dated 09 / 09 / 2025, page 31 / 88 24 / 51

[0048] The composition may comprise from about 0% by weight to about 3% by weight, from about 0.5% by weight to about 3% by weight, from about 1% by weight to about 3% by weight, from about 1.5% by weight to about 3% by weight, from about 2% by weight to about 3% by weight, from about 2.5% by weight to about 3% by weight, from about 0% by weight to about 2.5% by weight, from about 0% by weight to about 2% by weight, from about 0% by weight to about 1.5% by weight, from about 0% by weight to about 1% by weight or from about 0% by weight to about 0.5% by weight of one or more stabilizers. In some embodiments, the composition may include from about 0.5% by weight to about 1% by weight of one or more stabilizers. The stabilizer may be one or more of the following: alginate, carrageenan, guar gum, microcrystalline cellulose, carboxymethylcellulose, sorbitol, hydroxypropyl methylcellulose (HPMC), xanthan gum, tara gum, and locust bean gum.Stabilizers may be one or more of the following: alginate, carrageenan, guar gum, cellulose; for example, methylcellulose, microcrystalline cellulose, carboxymethylcellulose, sorbitol, hydroxypropylmethylcellulose (HPMC), xanthan gum, tara gum, locust bean gum, gellan gum, beet pectin, vegetable proteins, sodium caseinate, skimmed milk powder, milk protein isolate / concentrate, micellar casein isolate / concentrate, acid casein powder, rennet casein powder, whey protein concentrate / isolate powder, dairy product solids, whole milk powder, partially skimmed milk powder, buttermilk powder, modified starch, agar-agar, gelatin, gellan (e.g., high acyl, low acyl), gum arabic, konjac, pectin, maltodextrin, tragacanth, or a combination thereof.

[0049] A stabilizer can maintain a degree of homogeneity in the compositions. In some embodiments, the stabilizer can act as an emulsifier that complements the casein protein. When Petition 870250080886, dated 09 / 09 / 2025, p. 32 / 88 25 / 51 help stabilize finely emulsified fat and / or oil globules that scatter light in emulsions; stabilizers can also act as a bleaching agent. E. SALTS BUFFERING

[0050] The composition may comprise from about 0.0001% by weight to about 2% by weight, about 0.001% by weight to about 2% by weight, about 0.01% by weight to about 2% by weight, about 0.1% by weight to about 2% by weight, about 1% by weight to about 2% by weight, about 1.5% by weight to about 2% by weight, about 0.0001% by weight to about 1.5% by weight, about 0.0001% by weight to about 1% by weight, about 0.0001% by weight to about 0.1% by weight, about 0.0001% by weight to about 0.01% by weight or about 0.0001% by weight to about 0.001% by weight of buffer salts. In some embodiments, the composition may comprise from about 0.5% by weight to about 1% by weight of buffer salts. The buffer salt may be one or more of the following: phosphate salt, halide salt, carbonates, bicarbonates, tartrates, and citrate salt. F. VOLUME AGENTS

[0051] The composition may comprise from about 0% by weight to about 50% by weight, about 10% by weight to about 50% by weight, about 20% by weight to about 50% by weight, about 30% by weight to about 50% by weight, about 40% by weight to about 50% by weight, about 0% by weight to about 40% by weight, about 0% by weight to about 30% by weight, about 0% by weight to about 20% by weight or about 0% by weight to about 10% by weight of bulking agents. The bulking agents may be one or more of high fructose corn syrup, starches, modified starches and maltodextrose. G. EMULSIFIERS

[0052] The composition may comprise approximately 0% by weight Petition 870250080886, dated 09 / 09 / 2025, page 33 / 88 26 / 51 to about 3% by weight, about 0% by weight to about 0.5% by weight, about 0% by weight to about 1% by weight, about 0% by weight to about 1.5% by weight, about 0% by weight to about 2% by weight, about 0% by weight to about 2.5% by weight, about 0.5% by weight to about 3% by weight, about 1% by weight to about 3% by weight, about 1.5% by weight to about 3% by weight, about 2% by weight to about 3% by weight or about 2.5% by weight to about 3% by weight of one or more emulsifiers. In some embodiments, the composition may include from about 0.5% by weight to about 1% by weight of one or more emulsifiers.The emulsifier may be one or more of the following: diacetyltartaric acid esters of mono- and / or diglycerides, lactic acid esters of mono- and / or diglycerides, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyglycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose esters, sucrose monostearate, and monoglyceride. Emulsifiers may be one or more of the following: sugar esters, beeswax, carnauba wax, candelilla wax, vegetable waxes, fruit waxes, animal waxes, polyglycerol fatty acid esters, polyglycerol polyricinoleate (PGPR), polysorbates (polyoxyethylene sorbitan esters), monoglycerides, diglycerides, diacetyl tartaric acid esters of mono- and / or diglycerides, lactic acid esters of mono- and / or diglycerides, sodium stearoyl lactylate, sorbitan monostearate, polyglycol ester, propylene glycol monostearate, and lecithin.Notably, waxes can act as fat modifiers more effectively than emulsifiers due to their minimal surface-active properties. 3. METHODS FOR MANUFACTURING A COMPOSITION COMPRISING β-CASEIN

[0053] Manufacturing methods for a composition are provided. Petition 870250080886, dated 09 / 09 / 2025, page 34 / 88 27 / 51 as described in this document. The methods may include forming an oil phase comprising fat; forming an aqueous phase comprising protein; heating the oil phase and the aqueous phase from about 15 °C to about 75 °C, from about 25 °C to about 75 °C, from about 35 °C to about 75 °C, from about 45 °C to about 75 °C, from about 55 °C to about 75 °C, from about 65 °C to about 75 °C, from about 15 °C to about 65 °C, from about 15 °C to about 55 °C, from about 15 °C to about 45 °C, from about 15 °C to about 35 °C or from about 15 °C to about 25 °C; Mix the oil phase and the aqueous phase to form a mixture; homogenize the mixture to form an emulsion;Heat the emulsion from about 60°C to about 150°C, from about 60°C to about 140°C, from about 60°C to about 130°C, from about 60°C to about 120°C, from about 60°C to about 110°C, from about 60°C to about 100°C, from about 60°C to about 90°C, from about 60°C to about 80°C, from about 60°C to about 70°C, from about 70°C to about 150°C, from about 80°C to about 150°C, from about 90°C to about 150°C, from about 100°C to about 150°C, from about 110°C to about 150°C, about 120°C to about 150°C, about 130°C to about 150°C, or about 140°C to about 150°C;and cool the emulsion from about 2 °C to about 30 °C, from about 4 °C to about 30 °C, from about 8 °C to about 30 °C, from about 16 °C to about 30 °C, from about 2 °C to about 16 °C, from about 2 °C to about 8 °C, or from about 2 °C to about 4 °C. The emulsion may be heated to pasteurization levels (e.g., at least about 72 °C for at least about 15 seconds) and UHT pasteurization (e.g., from about 135 °C to about 154 °C, such as about 145 °C, for about 1 second to about 8 seconds), followed by packaging in non-sterile or sterile environments. Storage temperatures can vary - frozen (e.g., from about -18°C to about -15°C), refrigerated (e.g., from about 3°C ​​to about; Petition 870250080886, dated 09 / 09 / 2025, p. 35 / 88 The method may include: 28 / 51 °C) or ambient temperature (e.g., from about 18 °C to about 25 °C) based on specific heat treatment and packaging. The method may also include packaging of the emulsion. Packaging may include, without limitation, in bags, in brick-shaped containers (e.g., 250 ml to half a gallon), in jars (e.g., 250 ml jar to gallon), in a bag in a box (up to 20 pounds), in shopping bags, in cake decorating bags and the like. The aqueous phase may also include stabilizers, emulsifiers and buffering salts. The method may also include aeration of the emulsion. Aeration may include beating, mixing using a planetary mixer or beating using a continuous mixer. The method may also include heat treatment, pasteurization or sterilization of the emulsion. Heat treatment, pasteurization, or sterilization may involve retort treatment, high hydrostatic pressure, or ultra-high temperature processing.The emulsion may have improved stability in storage compared to a corresponding emulsion. A whipped emulsion can be prepared by whipping the emulsion as described in this document at a temperature of about 2 °C to about 8 °C, about 3 °C to about 8 °C, about 4 °C to about 8 °C, about 5 °C to about 8 °C, about 6 °C to about 8 °C, about 7 °C to about 8 °C, about 2 °C to about 7 °C, about 2 °C to about 6 °C, about 2 °C to about 5 °C, about 2 °C to about 4 °C or about 2 °C to about 3 °C. 4. FOOD PRODUCT

[0054] This document describes a food product comprising a composition as described herein. The food product may be a dairy or non-dairy product, such as coffee creamer, cooking creamer, whipped cream or a similar emulsion with low or high fat content. The food product may comprise from about 0.001% by weight to about 3% by weight. Petition 870250080886, dated 09 / 09 / 2025, page 36 / 88 29 / 51 weight, approximately 0.01% by weight to approximately 3% by weight, approximately 0.1% by weight to approximately 3% by weight, approximately 1% by weight to approximately 3% by weight, approximately 2% by weight to approximately 3% by weight, approximately 0.001% by weight to approximately 2% by weight, approximately 0.001% by weight to approximately 1% by weight, approximately 0.001% by weight to approximately 0.1% by weight or approximately 0.001% by weight to approximately 0.01% by weight of the protein. The food product may comprise from about 0.1% by weight to about 2.5% by weight, from about 0.5% by weight to about 2.5% by weight, from about 1% by weight to about 2.5% by weight, from about 1.5% by weight to about 2.5% by weight, from about 2.0% by weight to about 2.5% by weight, from about 0.1% by weight to about 2.0% by weight, from about 0.1% by weight to about 1.5% by weight, from about 0.1% by weight to about 1% by weight, or from about 0.1% by weight to about 0.5% by weight of total casein. 5. EXAMPLES

[0055] The above can be better understood based on the following examples, which are presented for illustrative purposes and are not intended to limit the scope of the invention. The present disclosure has several aspects and embodiments, illustrated by the non-limiting examples attached. EXAMPLE 1 Separation of β-casein from milk

[0056] It has been hypothesized that β-caseins may be primarily responsible for the high functionality of sodium caseinates. To develop protein solutions enriched with β-casein, the starting material can be reconstituted micellar casein powder or skim milk. Unlike the other two main casein fractions, αS- and κ-casein, the dissociation of β-casein from the micelle is temperature-dependent. β-casein dissociates from the casein micelle to the whey phase after cooling the milk to temperatures below 5 Petition 870250080886, dated 09 / 09 / 2025, p. 37 / 88 30 / 51 °C, which is a reversible process. Using microfiltration (MF), β-casein can be separated from skim milk at cold temperatures. For the current process, a slight modification of the method described by Hoffmann et al., (2006) Kieler Milchwirtschaftliche Forschungsberichte, 58(1), 41-51 and Schafer et al., (2019) International Dairy Journal, 97, 222-229 was used. This includes MF at low temperatures and subsequent concentration of the MF permeate using an ultrafiltration (UF) process.

[0057] Skim milk, micellar casein, or milk protein solution (protein content adjusted to 3.5% using deionized water) were microfiltered at 55 °C to separate soluble whey proteins from caseins. A retentate rich in casein micelles and a permeate rich in whey protein were obtained. The latter was discarded, and the former was again adjusted to a protein content of 3.5% using deionized water. This product was subsequently microfiltered to remove the permeate rich in whey protein fractions. This diafiltration step can be repeated to reduce the whey protein content. The retentate was diluted again to obtain the original protein content as skim milk using deionized water.This solution was kept at cold temperatures (<4 °C) for 48 to 72 hours, as β-casein dissociates from casein micelles at low temperatures due to the weakening of hydrophobic interactions. This solution was then microfiltered at 4 °C using a 100 kDa membrane to obtain a permeate enriched with β-casein and whey proteins. The retentate obtained was discarded. Subsequently, this solution was concentrated by ultrafiltration (10 kDa membrane) to produce a retentate enriched with β-casein. This retentate solution was titrated with 1 N HCl to precipitate β-casein at a pH of approximately... [Petition 870250080886, dated 09 / 09 / 2025, page 38 / 88.] 31 / 51 precisely 4.6. This fluid paste was centrifuged at 4000 g for 35 minutes to separate the β-casein-enriched precipitate from the whey proteins present in the whey. The precipitate was washed with deionized water to remove residual whey proteins. The precipitated β-casein was mixed with water to obtain a fluid paste containing 20-30% TS and was titrated back to pH 6.7 using 0.01 N NaOH. This solution was slowly heated to 65 °C to fully solubilize the β-casein solution. The protein composition of the initial material and the resulting UF retentate was analyzed by capillary electrophoresis (Figure 1) and HPLC (Figure 2). The composition is shown in Table 1. This β-casein protein-enriched solution was used to develop liquid emulsion compositions and high-fat emulsions that can be aerated with greater stability than sodium caseinate alone. TABLE 1. PERCENTAGE OF CASEINS IN THE COMPOSITION OF THREE SEPARATE EXPERIMENTS Casein type % β-Casein 89.8 ± 2.4 α-31 8.5 ± 1.5 α-32 1.4 ± 0.6 κ-Casein Not detected

[0058] This shows that β-casein could be concentrated from other caseins and whey proteins by increasing the ratio of αS1-, αS2-, β- and κ-caseins to 1:0:12:0. In Figure 3, the average protein particle size density (PSD) was measured using dynamic light scattering of β-casein and found to be approximately 6 nm. This confirmed that the β-casein was in monomeric form, while the sodium caseinate had some aggregates and the micellar casein concentrate was still in intact micellar form. Petition 870250080886, dated 09 / 09 / 2025, p. 39 / 88 32 / 51 EXAMPLE 2 SURFACE TENSION OF β-CASEIN COMPOUND SOLUTIONS

[0059] The reduction of surface tension in the solutions was measured. The solutions were diluted 10 times to evaluate their ability to reduce air-water and oil-water interfacial tension. It was clear in Figure 4 that the highest purity β-casein sample reduced surface tension to a greater extent than sodium caseinate and casein in its micellar form. EXAMPLE 3 Emulsions made with solutions comprising β-casein

[0060] Three-ingredient oil-in-water emulsions (oil, water, and protein) were prepared using 20% ​​canola oil and 1% protein (by weight) processed at room temperature and homogenized at 2500 psi (1st stage) and 500 psi (2nd stage). Sodium caseinate (NaCas) was used as a control instead of β-casein. The finished product was subjected to particle size measurement using a Mastersizer and foamability analysis using a planetary mixer. TABLE 2. MEASURED MEDIA FOR PSD OF SIMPLE EMULSIONS BY MASTERSIZER Sample Dx (10) fom) Dx (50) fom) Dx (90) fom) D [4,3] fom) Extension (90,10) Control NaCas 0.0445 0.414 2.56 1.0715 6.0725 BCN 100% replacement 0.0836 0.484 2.29 0.91 4.558

[0061] The foaming properties of the samples were analyzed, and the results are shown in Figure 6. The samples were subjected to aeration using a beater apparatus. Petition 870250080886, dated 09 / 09 / 2025, page 40 / 88 33 / 51 kitchen. Samples with β-casein showed better foam formation and foam stability compared to samples with sodium caseinate. EXAMPLE 4 Foaming capacity of solutions comprising β-casein

[0062] The foaming ability of 0.25% protein solutions was tested to understand the functionality of the β-casein enriched solution compared to the sodium caseinate control. Both proteins foamed rapidly, but the β-casein solution exhibited much greater foam stability than the sodium caseinate solution (Figure 5). This is evidenced by the much longer decay of foam height compared to sodium caseinate, which collapsed within the first 10 minutes of the test. EXAMPLE 5 WHIPPED TOPPING EMULSIONS COMPRISING β-CASEIN

[0063] Complex emulsions containing various ingredients have been prepared, simulating commercial whipped / aerated toppings. TABLE 3. RECIPE FOR APPLYING A 100% REPLACEMENT MIXTURE Ingredient Control (%) Sample of β-casein (%) Vegetable oil (palm kernel oil) 20 20 Sugar 30 30 Sodium caseinate 1 0 β-casein solution (dry basis) 0 1 Emulsifiers (polysorbate 60 / sodium stearoyl lactylate / mono & diglycerides) 0.5 0.5 Stabilizers 0.5 0.5 Water up to 100 Petition 870250080886, dated 09 / 09 / 2025, page 41 / 88 34 / 51 TABLE 4. MEANS FOR PSD OF THE GOLD LABEL LIQUID TOP COATING PRODUCT WITH SODIUM CASEINATE AND BETA-CASEIN Sample Dx (10) (pm) Dx (50) (pm) Dx (90) (pm) D [4,3] (pm) Extension (90,10) Control NaCas 0.0449 0.220 0.877 2.14 3.784 BCN 100% replacement 0.0943 0.289 0.691 0.350 2.066 TABLE 5. RESULTS OF BEATING IN A KITCHENAID MIXER Beta-casein Control Caseinate Manufacturing Date 09 / 09 / 22 09 / 09 / 22 Test Date 16 / 09 / 22 16 / 09 / 22 Beating Time (min) 4 4 Excess (%) 296 323 Penetrometer (t=0 min) 40.7 41.6 Viscosity S3 (cPs / torque) 100 rpm 627 / 62.7 185 / 18.5 Rosette Time (min) 120 120 Bowl and Cake Application Roughness Classification Fine Grain Smooth Gloss Classification Semi-gloss / reflects little Soft gloss Firmness Classification Soft-firm Soft-firm EXAMPLE 6 Emulsions for whipped toppings comprising reduced β-casein

[0064] Due to the excellent results with the 1:1 substitution of sodium caseinate for beta-casein in the whipped topping application, protein reductions were also evaluated. Petition 870250080886, dated 09 / 09 / 2025, page 42 / 88 35 / 51 TABLE 6. RECIPE FOR APPLYING WHIPPED TOPPING WITH REDUCED PROTEIN CONTENT Ingredient Control Sample of β-casein (25% reduction) Sample of β-casein (50% reduction) Vegetable oil (palm kernel oil) 20% 20% 20% Sugar 30% 30% 30% Sodium caseinate 1% 0% 0% β-casein solution (dry basis) 0% 0.75% 0.5% Emulsifiers (polysorbate 60 / sodium stearoyl lactylate / mono & diglycerides) 0.5% 0.5% 0.5% Stabilizers 0.5% 0.5% 0.5% Water up to 100%

[0065] These results indicate that it is possible to add less beta-casein to obtain product characteristics and performance similar to those of the control. This is evidenced by the similar PSD results shown in Table 7. Beating characteristics were also improved with lower product viscosity, slightly longer beating time, but longer rosette time and cake stability (Table 8). TABLE 7. PSD FOR GOLD LABEL LIQUID COATING PRODUCT MANUFACTURED WITH REDUCED BETACASEIN PROTEIN CONTENT. Sample Dx (10) (Mm) Dx (50) (pm) Dx (90) (pm) D [4,3] (pm) Extension (90,10) Control GL 0.0575 0.246 0.722 0.346 2.701 GL BCN 25% reduced 0.0581 0.264 0.793 0.358 2.787 GL BCN 50% reduced 0.062 0.283 0.839 0.382 2.743 Petition 870250080886, dated 09 / 09 / 2025, page 43 / 88 36 / 51 TABLE 8. RESULTS OF BEATING IN A HOBART MIXER AT SPEED 2 WITH 660 G OF LIQUID FROSTING. 10-4 GL-A Control caseinate 10-4 GL-B (25% reduction in βCN) 10-4 GL-C (50% reduction in βCN) Beating Time (min) 8:30 12:30 11:00 Excess (%) 366% 336% 376% Rosette Time (min) 35 50 45 Bench Time (min) 40 55 50 Penetrometer (mm) 38.5 38 37.5 Bowl and Cake Application Roughness Smooth with fine granulation Smooth Smooth Gloss Semi-gloss Soft gloss Semi-gloss Firmness Soft Soft-firm Firm EXAMPLE 7 Sodium caseinate emulsions comprising β-casein

[0066] β-casein was added to sodium caseinate to alter the ratio of β-casein relative to the total casein content. In general, β-casein constitutes 33-37% of the total casein. Various β-casein formulation ratios were examined. In the following example, the β-casein content was increased from 37% to 50%, 65%, 75%, and 90% by mixing various levels of β-casein solutions with sodium caseinate or β-casein solutions alone, while maintaining the total protein content equal in all formulations. Emulsions were made with 20% canola oil and 1% protein processed at 2500 / 500 psi pressure in a two-stage homogenizer. Table 9 shows that increasing the β-casein content of sodium caseinate can lead to superior emulsion properties. Petition 870250080886, dated 09 / 09 / 2025, p. 44 / 88 37 / 51 TABLE 9. MEDIA FOR PSD OF SIMPLE EMULSIONS WITH MIXTURES OF SODIUM CASEINATE AND BETA-CASEIN. Sample: 0.057 0.434 2.26 0.874 25% NaCas 75% BCN 0.0607 0.285 1.44 0.569 100% BCN 0.0767 0.522 2.5 1.01 EXAMPLE 8 Whipped Sodium Caseinate Emulsions Comprising β-Casein

[0067] In another embodiment, β-casein was added to sodium caseinate to alter the ratio of β-casein to the total casein content and applied to a whipped coating product. In the following example, the β-casein content was increased to 50 and 55% by mixing β-casein extract and sodium caseinate. TABLE 10. RECIPE FOR A WHIPPED TOPPING PRODUCT WITH SODIUM CASEINATE ENRICHED WITH BETA CASEIN. Ingredient Control (%) 50% NaCas Enriched with BCN (%) 75% NaCas Enriched with BCN (%) Vegetable oil (palm kernel oil) 20 20 20 Sugar 30 30 30 Sodium caseinate 1 0.5 0.25 Beta-casein solution (dry basis) 0 0.5 0.75 Emulsifiers (polysorbate 60 / sodium stearoyl lactylate / mono & diglycerides) 0.5 0.5 0.5 Stabilizers 0.5 0.5 0.5 Water up to 100 Petition 870250080886, dated 09 / 09 / 2025, p. 45 / 88 38 / 51 TABLE 11. MEDIA FOR PSD OF BEAT SAMPLES MADE WITH ENRICHED SODIUM CASEINATE / BETA-CASEIN. Sample Dx (10) (Mm) Dx (50) (Mm) Dx (90) (Mm) D [4,3] (Mm) D [3,2] (M™) Control 100% caseinate 0.0551 0.227 0.69 0.685 0.127 50% enriched beta casein 0.0468 0.207 0.671 0.501 0.111 75% enriched beta casein 0.0449 0.189 0.546 0.25 0.105 EXAMPLE 9 COFFEE CREAM THAT CANNOT BE WHIPPED THAT CONTAINS β-CASEIN

[0068] In another embodiment, β-casein was incorporated into low-fat and high-fat non-whipped coffee creamer formulations using non-hydrogenated vegetable fats and milk fat, respectively. Variable sugar contents were also used, as well as different supporting emulsifiers, including polysorbate-60 and monoglycerides and diglycerides of fatty acids. Salts such as sodium chloride and dipotassium phosphates were included to provide flavor and prevent feather coagulation. Table 12 shows the formulations that were heat-treated and homogenized downstream at a pressure of 2500 / 500 psi in a two-stage homogenizer. Table 13 shows the properties of the resulting emulsion, indicating the low viscosity and small particle sizes obtained after processing and refrigerated storage. The resulting products (i.e., samples C and D) showed good stability in coffee, with no visible feather coagulation. Petition 870250080886, dated 09 / 09 / 2025, page 46 / 88 39 / 51 TABLE 12: COFFEE CREAM PRODUCT RECIPES THAT CANNOT BE WHIPPED WITH BETA CASEIN. Ingredients Sample CD Non-hydrogenated palm kernel and coconut mixture 5 Anhydrous milk fat 30 Granulated sugar 10 4.5 Polysorbate-60 0.3 Mono & Diglycerides 0.3 Salt (sodium chloride) 0.3 0.3 Dipotassium phosphate 0.2 0.5 Beta-casein solution (dry basis) 1.0 1.5 Water up to 100% TABLE 13. AVERAGE PARTICLE SIZE, LIQUID SEPARATION AND VISCOSITY OF COFFEE CREAMS. Sample Parameters CD Particle size - Dx (10) (μπ) 0.16 0.19 Particle size - Dx (50) ^m) 0.46 0.54 Particle size - Dx (90) ^m) 1.36 1.62 Particle size - D [4,3] ^m) 0.70 0.77 Particle size - D [3,2] ^m) 0.34 0.39 Liquid separation - 3 weeks (mm) 10 1 Brookfield viscosity of DVT at 100 rpm (cP / %torque / Spindle) <100 / 2 / S1 <100 / 5 / S1 EXAMPLE 10 Whipped Sodium Caseinate Emulsions They include β-casein

[0069] In another embodiment, β-casein was incorporated into several Petition 870250080886, dated 09 / 09 / 2025, p. 47 / 88 40 / 51 toppings, glazes, and soft foam formulations that can be whipped with low, medium, and high fat content. In these formulations, various oils, not limited to hydrogenated vegetable oils from palm kernel oil and coconut oil, were used in a range of concentrations. Sweeteners such as corn syrups (HFCS 42, 43 / 43, 36DE), dextrose, granulated sugar, and lactose were included to achieve a total sweetener content of 16 to 60%. Many different emulsifiers showed compatibility with β-casein, such as soy lecithin, distilled monoacylglycerol, polysorbate-60, soy protein concentrate, sodium stearoyl lactylate, polyglycerol esters of fatty acids, and sorbitan monostearate. Several stabilizers were used to improve product stability and included sodium alginate, hydroxypropyl methylcellulose, xanthan gum, guar gum, locust bean gum, corn starch, and carrageenan.Other dairy ingredients, such as powdered cream and powdered buttermilk, can also be used to enhance the dairy flavor profile in imitation creams. The various compositions (i.e., samples E, F, G, H, I, and J) are shown in Table 14. Table 15 shows the resulting properties of the compositions. The initial appearance of the whipped product is shown in Figure 8. Figure 8 shows the initial rosette as dispensed from a standard piping bag with a star nozzle immediately after whipping. The stability bowls comprising the samples after 24 hours of refrigeration (i.e., from about 2°C to about 4°C) are shown in Figure 9. Figure 9 shows the appearance of the product after 150 g of the product was placed in a cold container and stored under refrigeration. A spoon was used to remove a small amount from the cup to show the internal structure of the foam and the stability of the whipped cream. Petition 870250080886, dated 09 / 09 / 2025, page 48 / 88 41 / 51 TABLE 14. RECIPES FOR WHIPPABLE FROSTINGS, GLAZES AND FOAMS CONTAINING BETA-CASEIN. Ingredient Samples EFGHIJ High Fructose Corn Syrup 42 30 52 10.5 Fully Hydrogenated Palm Kernel Oil 14 22 12.0 28 18 27.0 Hydrogenated Coconut Oil 6.0 Corn Syrup 43 / 43 7.0 9 Corn Syrup 36DE 18 7 Dextrose 0.45 8.0 Granulated Sugar 11 6.8 16 23.0 Cream Powder 3.3 Buttermilk Powder 3 Lactose 2.5 Soy Lecithin 0.1 Distilled Monoglyceride 0.07 Polysorbate-60 0.45 0.3 0.1 0.3 0.3 0.3 Soy Protein Concentrate 0.1 0.1 Sodium Stearoyl Lactate 0.3 Polyglycerol esters of fatty acids 0.1 0.1 Mono & Diglycerides 0.1 0.15 0.3 Sorbitan monostearate 0.2 Salt (sodium chloride) 0.1 0.15 0.1 Potassium carbonate 0.1 0.1 Sodium alginate 0.05 0.05 Disodium phosphate 0.1 Hydroxypropyl methylcellulose mixture 0.2 Hydroxypropyl methylcellulose F50 0.2 0.36 0.25 0.3 Xanthan gum 0.05 0.1 0.05 0.04 Guar gum 0.1 0.10 0.1 Locust bean gum 0.10 Modified corn starch 0.30 Carrageenan 0.05 Beta-casein solution (dry basis) 0.1 0.8 0.3 1.2 1.2 2.0 Water up to 100%, Petition 870250080886, dated 09 / 09 / 2025, page 49 / 88 42 / 51 TABLE 15. EMULSION PROPERTIES AND WHIPPING PERFORMANCE OF FLAVORS, GLAZES AND FOAMS AFTER THESE EMULSIONS WERE SUBJECTED TO FREEZING AND THAWING AT REFRIGERATED TEMPERATURE. Sample EFGHIJ Storage / Treatment Freezing / Thawing Freezing / Thawing Freezing / Thawing Freezing / Thawing Freezing / Thawing Refrigerated Particle Size Dx [CI] (µm) 0.05 0.14 0.27 0.12 0.22 0.10 Particle Size Dx

[50] (µm) 0.19 0.43 0.82 0.35 0.47 0.26 Particle Size Dx

[90] (µm) 0.50 1.98 2.76 1.08 1.06 0.58 Particle Size D[4,3] (µm) 0.25 0.76 1.62 0.56 0.84 0.37 Particle Size D [3,2] (µm) 0.12 0.30 0.58 0.26 0.40 0.20 Liquid separation 3 weeks (mm) 0 25 0 0 5 Brookfield DVT viscosity 100 rpm (cP / %torque / Spindle) 761 / 76.1 / 33 240 / 24 / 33 1840 / 46 / Ξ5 477 / 47.7 / S3 429 / 42.9 / 33 860 / 43.0 / 34 Net weight in standard cup (g) 340 330 333 332 336 340.00 Beaten weight.In Standard Cup (g) 74.3 84 120.6 120.1 104.2 102.10 Beating Time (min) 16.0 13.5 9.0 16.0 11.0 8:00 Excess [%] 358 293 176 176 221 233 Rosette Time [min) 60 30 30 60 75 Penetrometer (mm) 36 36.4 >50 35 36.3 31.5 Roughness - beaten smooth sandy / small marks smooth grain Fine grain very smooth Gloss - beaten semi-gloss semi-gloss gloss soft semi-gloss semi-gloss semi-gloss Firmness - beaten firm stiff soft firm / rigid firm very firm Stability - beaten 1 day excellent good unsatisfactory good good excellent Stability - beaten 2 days good unsatisfactory unsatisfactory good good excellent Stability - shaken - syneresis (ml) 0 0 0 0 0 0.

[0070] The preceding description of the specific aspects will reveal the general nature of the invention in such a way that others will be able, applying knowledge of the art, to readily modify and / or adapt such specific aspects for various applications without undue experimentation and without departing from the general concept of the present disclosure. Therefore, such adaptations and modifications must be within the meaning and range of equivalents of the disclosed aspects, based on the teaching and guidance presented in this document. It should be understood that the phraseology or terminology contained in this document is for descriptive purposes and not for limitation, so that the terminology or Petition 870250080886, dated 09 / 09 / 2025, page 50 / 88 43 / 51 The phraseology in this descriptive report should be interpreted by those skilled in the art in light of the teachings and guidance provided.

[0071] The scope and extent of this disclosure shall not be limited by any of the exemplary aspects described above, but shall be defined only in accordance with the following claims and their equivalents.

[0072] All publications, patents, patent applications and / or other documents cited in this application are incorporated by reference in their entirety for all purposes, in the same manner as if each individual publication, patent, patent application and / or other document were individually indicated for incorporation by reference for all purposes.

[0073] For reasons of completeness, various aspects of the invention are presented in the following numbered clauses:

[0074] Clause 1. An emulsion composition comprising a fat and a protein, wherein the protein comprises more than 45% by weight of β-casein based on the total amount of casein present in the composition.

[0075] Clause 2. The composition of clause 1, wherein the composition comprises: from about 5% by weight to about 45% by weight of fat; from about 0.001% by weight to about 3% by weight of protein; from about 0% by weight to about 55% by weight of a sweetener; from about 0% by weight to about 3% by weight of one or more stabilizers; from about 0.0001% by weight to about 2% by weight of buffer salts; and from about 0% by weight to about 3% by weight of one or more emulsifiers.

[0076] Clause 3. The composition of clause 1 or clause 2, wherein the composition comprises: from about 5% by weight to about 35% by weight of fat; from about 1% by weight to about 2.5% by weight of protein; from about 5% by weight to about 45% by weight of Petition 870250080886, dated 09 / 09 / 2025, page 51 / 88 44 / 51 a sweetener; from about 0.5% by weight to about 3% by weight of one or more stabilizers; from about 0.5% by weight to about 2% by weight of buffer salts; and from about 0.5% by weight to about 3% by weight of one or more emulsifiers.

[0077] Clause 4. The composition of any of clauses 1 to 3, wherein the fat is a milk fat, a vegetable fat, vegetable oil, algae oil, fermented oil of bacteria, yeast or mold, hydrogenated oil, hydrogenated and interesterified oil, hydrogenated, blended and interesterified oil, medium chain triglyceride (MCT) vegetable oil, milk fat, ghee, anhydrous milk fat, butter oil or a combination thereof.

[0078] Clause 5. The composition of any of clauses 1 to 4, wherein the protein is an animal protein, a recombinant milk protein, a vegetable protein or a combination thereof.

[0079] Clause 6. The composition of any of clauses 1 to 5, wherein the protein is natural casein, recombinant casein or a combination thereof.

[0080] Clause 7. The composition of any of clauses 1 to 6, wherein the composition comprises a total κ-casein content of less than 0.03% by weight based on the total composition.

[0081] Clause 8. The composition of any of clauses 1 to 7, wherein the protein is enriched with animal and / or recombinant β-casein.

[0082] Clause 9. The composition of any of clauses 1 to 8, wherein β-casein is natural or recombinant.

[0083] Clause 10. The composition of clause 9, wherein the β-casein is recombinant and comprises an amino acid sequence that is about 60% to about 100% identical to an amino acid sequence of a mammalian milk protein, such as a protein of Petition 870250080886, dated 09 / 09 / 2025, p. 52 / 88 45 / 51 cow's milk, a sheep's milk protein, a camel's milk protein, a yak milk protein, a buffalo milk protein, a horse milk protein or a goat's milk protein.

[0084] Clause 11. The composition of any of the clauses to 10, where the proportion of β-casein is from about 45% to about 100% of the total amount of casein in the composition.

[0085] Clause 12. The composition of any of the clauses to 11, wherein the β-casein is in micellar form or in monomeric form; wherein, when the β-casein is in monomeric form, the β-casein has a protein particle size of less than 50 nm.

[0086] Clause 13. The composition of any of the clauses to 11, wherein the β-casein is in micellar form or in monomeric form; wherein, when the β-casein is in micellar form, the β-casein has a protein particle size of less than 500 nm.

[0087] Clause 14. The composition of any of the clauses to 13, wherein β-casein has a zeta potential of about -50 mV to about -15 mV in a pH 7.0 buffer.

[0088] Clause 15. The composition of any of the clauses to 14, wherein the protein is in liquid or powder form, wherein the powder form is produced by spray drying, roller drying, drum drying or freeze-drying of the protein to remove water.

[0089] Clause 16. The composition of any of the clauses to 15, wherein the protein is a single type of native milk protein, a single type of recombinant milk protein or a combination thereof.

[0090] Clause 17. The composition of clause 16, where the only type of protein is β-casein.

[0091] Clause 18. The composition of any of the clauses to 17, in which the protein is composed of two or more different types Petition 870250080886, dated 09 / 09 / 2025, p. 53 / 88 46 / 51 of animal milk proteins, recombinant milk proteins and plant-based proteins.

[0092] Clause 19. The composition of any of the clauses to 18, wherein the protein is with or without post-translational modifications.

[0093] Clause 20. The composition of clause 19, wherein the post-translational modifications are one or more of the glycosylation and phosphorylation modifications.

[0094] Clause 21. The composition of any of the clauses to 18, in which the protein is phosphorylated.

[0095] Clause 22. The composition of any of the clauses to 18, wherein the protein comprises non-native phosphorylation.

[0096] Clause 23. The composition of any of the clauses to 22, wherein the recombinant caseins are produced by a fungal cell, a yeast cell, a bacterial cell, algae or a transgenic method.

[0097] Clause 24. The composition of any of the clauses to 23, wherein the sweetener is a nutritive sweetener, a non-nutritive sweetener or a combination thereof.

[0098] Clause 25. The composition of clause 24, wherein the nutritive sweetener is one or more of the following: sucrose, lactose, glucose, fructose, corn syrup solids, high fructose corn syrup, dextrose, maltodextrin, brown sugar, honey and maple syrup, syrups; soluble / insoluble fibers derived from corn, wheat, peas, rice, oats, coconut, barley and / or tapioca; fructo- and galacto-oligosaccharides; and hydrolyzed cereal flour; or a combination thereof.

[0099] Clause 26. The composition of clause 24, wherein the non-nutritive sweetener is one or more of sucralose, aspartame, saccharin, stevia, monk fruit extract, neotame, advantame, acesulfame potassium, sugar alcohols such as maltitol, xylitol, sorbitol, erythritol, mannitol, isomalt, lactitol, hydrogenated starch hydrolysates or a Petition 870250080886, dated 09 / 09 / 2025, page 54 / 88 47 / 51 combination of these.

[0100] Clause 27. The composition of clause 24, wherein the sweetener is one or more of brazzein, curculin, mabinlin, miraculin, monellin, pentadin and thaumatin.

[0101] Clause 28. The composition of any of the clauses to 27, wherein the fat comprises one or more lipids derived from a plant, an animal, one or more lipids derived from milk or a combination thereof.

[0102] Clause 29. The composition of any of the clauses to 28, wherein the fat comprises one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid.

[0103] Clause 30. The composition of clause 29, in which one or more monoglycerides, diglycerides, triglycerides and / or phospholipids is a transesterified monoglyceride, diglyceride, triglyceride and / or phospholipid of vegetable origin comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid.

[0104] Clause 31. The composition of any of the clauses to 30, wherein the fat is hydrogenated oil, interesterified oil, hydrogenated and interesterified oil, hydrogenated, mixed and interesterified oil or a combination thereof.

[0105] Clause 32. The composition of clause 29, wherein the one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprise fatty acyl chains in a percentage that resembles a percentage of the fatty acyl chains found in milk or dairy products derived from mammals.

[0106] Clause 33. The composition of any of the clauses to 32, in which the composition may be beaten. Petition 870250080886, dated 09 / 09 / 2025, p. 55 / 88 48 / 51

[0107] Clause 34. The composition of any of the clauses to 32, in which the composition cannot be beaten.

[0108] Clause 35. The composition of clause 34, wherein the composition is a cooking cream or a coffee creamer.

[0109] Clause 36. The composition of any of the clauses to 35, wherein the fat is fully hydrogenated, partially hydrogenated, interesterified, non-hydrogenated or hydrogenated and interesterified.

[0110] Clause 37. The composition of any of the clauses to 36, in which the fat is fully hydrogenated.

[0111] Clause 38. The composition of any of the clauses to 37, wherein the composition further includes a crystallizer, a flavoring agent, a salt, a preservative or a combination thereof.

[0112] Clause 39. The composition of any of the clauses to 38, wherein the protein is one or more of the following: monomeric caseins, sodium caseinate, calcium caseinate, potassium caseinate, acid casein, rennet casein, micellar protein and globular protein.

[0113] Clause 40. The composition of clause 39, wherein the globular protein is one or more milk-derived proteins, vegetable protein, alpha-lactalbumin, beta-lactoglobulin, ovalbumin, ovoglobulin and recombinant protein.

[0114] Clause 41. The composition of clause 39, wherein the micellar protein is micellar casein, a recombinant micellar casein or a combination thereof.

[0115] Clause 42. The composition of clause 40, wherein vegetable protein is any protein based on cereals, legumes or seeds and is present in an amount of about 0.05% by weight to about 2.5% by weight.

[0116] Clause 43. The composition of clause 41, in which casein Petition 870250080886, dated 09 / 09 / 2025, p. 56 / 88 49 / 51 micellar is sodium caseinate or calcium caseinate and is present in an amount of about 0.05% by weight to about 2.5% by weight.

[0117] Clause 44. The composition of any of the clauses to 43, wherein the stabilizer is one or more of the following: alginate, carrageenan, guar gum, cellulose, such as methylcellulose, microcrystalline cellulose, carboxymethylcellulose, hydroxypropylmethylcellulose (HPMC), sorbitol, xanthan gum, tara gum, locust bean gum, gellan gum (such as high acyl, low acyl), beet pectin, skimmed milk powder, whole milk powder, partially skimmed milk powder, milk powder with butter, dairy solids, modified starch, agar-agar, gelatin, gum arabic, konjac, pectin, maltodextrin and tragacanth.

[0118] Clause 45. The composition of any of the clauses to 43, wherein the emulsifier is one or more of the following: diacetyltartaric acid esters of mono- and / or diglycerides, lactic acid esters of mono- and / or diglycerides, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyglycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose esters, sucrose monostearate, monoglyceride, beeswax, camauba wax, candelilla wax, vegetable waxes, fruit waxes, animal waxes, polyglycerol fatty acid esters and polyglycerol polyricinoleate (PGPR).

[0119] Clause 46. The composition of any of the clauses to 43, wherein the buffer salt is one or more of any sodium, potassium or calcium citrate, phosphate, carbonate salts, such as sodium polyphosphates, orthophosphate, pyrophosphate, hexametaphosphate, mono- or diphosphate salts, mono- or dicarbonates and halide salts.

[0120] Clause 47. A food product comprising the composition of any of clauses 1 to 46.

[0121] Clause 48. The food product of clause 47, wherein the food product is a dairy product, a product not derived from Petition 870250080886, dated 09 / 09 / 2025, page 57 / 88 50 / 51 animals, a beverage product, or a combination thereof.

[0122] Clause 49. The food product of clause 47 or clause 48, wherein the food product is a coffee creamer, a cooking cream, a whipped cream or a similar emulsion with a low or high fat content.

[0123] Clause 50. The food product of any of clauses 47 to 49, wherein the food product comprises from about 0.001% by weight to about 3% by weight of protein.

[0124] Clause 51. A method for manufacturing the composition of any of clauses 1 to 46, wherein the method comprises: forming an oil phase comprising fat; forming an aqueous phase comprising protein; adjusting the oil phase and the aqueous phase from about 15 °C to about 75 °C; mixing the oil phase and the aqueous phase to form a mixture; homogenizing the mixture to form an emulsion; heating the emulsion from about 50 °C to about 145 °C; and cooling the emulsion from about 2 °C to about 30 °C.

[0125] Clause 52. The method of clause 51, wherein the method further comprises packaging the emulsion under sterile or non-sterile conditions.

[0126] Clause 53. The method of clause 51 or clause 52, wherein the method further comprises storing the emulsion between about -18 °C and about -15 °C, between about 3 °C and about 5 °C or between about 18 °C and about 25 °C.

[0127] Clause 54. The method of any of clauses 51 to 53, in which the aqueous phase also includes stabilizers, emulsifiers and buffering salts.

[0128] Clause 55. The method of any of clauses 51 to 54, in which the method also includes aeration of the emulsion or quiescent storage of the emulsion.

[0129] Clause 56. The method of clause 55, in which aeration Petition 870250080886, dated 09 / 09 / 2025, p. 58 / 88 51 / 51 includes beating, mixing with a planetary mixer, or beating with a continuous mixer.

[0130] Clause 57. The method of any of clauses 51 to 56, in which the method also includes heat treatment, pasteurization or sterilization of the emulsion.

[0131] Clause 58. The method of clause 57, in which the heat treatment, pasteurization or sterilization includes retort, high hydrostatic pressure, ultraviolet radiation, irradiation or ultra-high temperature processing.

[0132] Clause 59. The method of any of clauses 51 to 58, in which the emulsion has improved stability during storage compared to a corresponding emulsion.

[0133] Clause 60. A method of preparing a whipped emulsion, wherein the method comprises whipping the emulsion of any of clauses 51 to 59, wherein the whipping is carried out at a temperature of about 2 °C to about 8 °C.

Claims

CLAIMS 1. Emulsion composition, characterized in that it comprises a fat and a protein, wherein the protein comprises more than 45% by weight of β-casein based on the total amount of casein present in the composition.

2. Composition, according to claim 1, characterized in that it comprises: from about 5% by weight to about 45% by weight of fat; from about 0.001% by weight to about 3% by weight of protein; from about 0% by weight to about 55% of a sweetener; from about 0% by weight to about 3% by weight of one or more stabilizers; from about 0.0001% by weight to about 2% by weight of buffer salts; and from about 0% by weight to about 3% by weight of one or more emulsifiers.

3. Composition, according to claim 1 or 2, characterized in that it comprises: from about 5% by weight to about 35% by weight of fat; from about 1% by weight to about 2.5% by weight of protein; from about 5% by weight to about 45% by weight of a sweetener; from about 0.5% by weight to about 3% by weight of one or more stabilizers; from about 0.5% by weight to about 2% by weight of buffer salts; and Petition 870250080886, dated 09 / 09 / 2025, page 60 / 88 2 / 10 from about 0.5% by weight to about 3% by weight of one or more emulsifiers.

4. Composition, according to any one of claims 1 to 3, characterized in that the fat is a milk fat, a vegetable fat, vegetable oil, algae oil, fermented oil of bacteria, yeasts or fungi, hydrogenated oil, hydrogenated and interesterified oil, hydrogenated, mixed and interesterified oil, medium chain triglyceride (MCT) vegetable oil, milk fat, ghee, anhydrous milk fat, butter oil or a combination thereof.

5. Composition, according to any one of claims 1 to 4, characterized in that the protein is an animal protein, a recombinant milk protein, a protein of vegetable origin or a combination thereof.

6. Composition, according to any one of claims 1 to 5, characterized in that the protein is natural casein, recombinant casein or a combination thereof.

7. Composition, according to any one of claims 1 to 6, characterized in that the composition comprises a total κ-casein content of less than 0.03% by weight based on the total composition.

8. Composition, according to any one of claims 1 to 7, characterized in that the protein is enriched in animal and / or recombinant β-casein.

9. Composition, according to any one of claims 1 to 8, characterized in that the β-casein is natural or recombinant.

10. Composition according to claim 9, characterized in that the β-casein is recombinant and comprises an amino acid sequence that is about 60% to about 100% identical to an amino acid sequence of a mammalian milk protein, such as a cow's milk protein, a sheep's milk protein, a camel's milk protein, a yak's milk protein, a buffalo's milk protein, a horse's milk protein or a goat's milk protein.

11. Composition, according to any one of claims 1 to 10, characterized in that the proportion of β-casein is from about 45% to about 100% of the total amount of casein in the composition.

12. Composition, according to any one of claims 1 to 11, characterized in that the β-casein is in micellar form or in monomeric form; wherein, when the β-casein is in a monomeric form, the β-casein has a protein particle size of less than 50 nm.

13. Composition, according to any one of claims 1 to 11, characterized in that the β-casein is in micellar form or in monomeric form; wherein, when the β-casein is in micellar form, the β-casein has a protein particle size of less than 500 nm.

14. Composition, according to any one of claims 1 to 13, characterized in that the β-casein has a zeta potential of about -50 mV to about -15 mV in a pH 7.0 buffer.

15. Composition, according to any one of claims 1 to 14, characterized in that the protein is in liquid or powder form, wherein the powder form is produced by spray drying, roller drying, drum drying or freeze-drying of the protein to remove water. Petition 870250080886, dated 09 / 09 / 2025, p. 62 / 88 4 / 10 16. Composition, according to any one of claims 1 to 15, characterized in that the protein is a single type of native milk protein, a single type of recombinant milk protein, or a combination thereof.

17. Composition according to claim 16, characterized in that the only type of protein is β-casein.

18. Composition, according to any one of claims 1 to 17, characterized in that the protein is composed of two or more different types of animal milk proteins, recombinant milk proteins and plant-derived proteins.

19. Composition, according to any one of claims 1 to 18, characterized in that the protein is with or without post-translational modifications.

20. Composition according to claim 19, characterized in that the post-translational modifications are one or more of glycosylation and phosphorylation.

21. Composition according to any one of claims 1 to 18, characterized in that the protein is phosphorylated.

22. Composition, according to any one of claims 1 to 18, characterized in that the protein comprises non-native phosphorylation.

23. Composition, according to any one of claims 6 to 22, characterized in that the recombinant caseins are produced by a fungal cell, a yeast cell, a bacterial cell, algae or a transgenic method.

24. Composition, according to any one of claims 2 to 23, characterized in that the sweetener is a nutritive sweetener, a non-nutritive sweetener, or a combination thereof.

25. Composition, according to claim 24, characterized by the fact that the nutritive sweetener is one or more of the following: sucrose, lactose, glucose, fructose, corn syrup solids, high fructose corn syrup, dextrose, maltodextrin, brown sugar, honey and maple syrup, syrups; soluble / insoluble fibers derived from corn, wheat, peas, rice, oats, coconut, barley and / or tapioca; fructo- and galacto-oligosaccharides; and hydrolyzed cereal flour; or a combination thereof.

26. Composition according to claim 24, characterized in that the non-nutritive sweetener is one or more of sucralose, aspartame, saccharin, stevia, monk fruit extract, neotame, advantame, acesulfame potassium, sugar alcohols such as maltitol, xylitol, sorbitol, erythritol, mannitol, isomalt, lactitol, hydrogenated starch hydrolysates or a combination thereof.

27. Composition according to claim 24, characterized in that the sweetener is one or more of brazzein, curculin, mabinlin, miraculin, monellin, pentadin and thaumatin.

28. Composition, according to any one of claims 1 to 27, characterized in that the fat comprises one or more lipids derived from a plant, an animal, one or more lipids derived from milk, or a combination thereof.

29. Composition, according to any one of claims 1 to 28, characterized in that the fat comprises one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid.

30. Composition, according to claim 29, characterized in that one or more monoglycerides, diglycerides, triglycerides and / or phospholipids is a monoglyceride, diglyceride, triglyceride and / or transesterified phospholipid of vegetable origin comprising a short-chain fatty acid selected from the group consisting of butyric acid, caproic acid, caprylic acid and capric acid.

31. Composition, according to any one of claims 1 to 30, characterized in that the fat is hydrogenated oil, interesterified oil, hydrogenated and interesterified oil, hydrogenated oil, mixed and interesterified oil, or a combination thereof.

32. Composition according to claim 29, characterized in that one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprise fatty acyl chains in a percentage that resembles a percentage of the fatty acyl chains found in milk or a mammalian dairy product.

33. A composition according to any one of claims 1 to 32, characterized in that it can be beaten.

34. A composition, according to any one of claims 1 to 32, characterized in that it cannot be beaten.

35. Composition according to claim 34, characterized in that it is a cooking cream or a coffee creamer.

36. Composition, according to any one of claims 1 to 35, characterized in that the fat is fully hydrogenated, partially hydrogenated, interesterified, non-hydrogenated, or hydrogenated and interesterified.

37. Composition, according to any one of claims 1 to 36, characterized in that the fat is fully hydrogenated.

38. Composition, according to any one of claims 1 to 37, characterized in that it further comprises a crystallizer, a flavoring agent, a salt, a preservative or a combination thereof. Petition 870250080886, dated 09 / 09 / 2025, page 65 / 88 7 / 10 39. Composition, according to any one of claims 1 to 38, characterized in that the protein is one or more of the monomeric caseins, sodium caseinate, calcium caseinate, potassium caseinate, acid casein, rennet casein, micellar protein and globular protein.

40. Composition according to claim 39, characterized in that the globular protein is one or more proteins derived from milk, vegetable protein, alpha-lactalbumin, beta-lactoglobulin, ovalbumin, ovoglobulin and recombinant protein.

41. Composition according to claim 39, characterized in that the micellar protein is micellar casein, a recombinant micellar casein, or a combination thereof.

42. Composition, according to claim 40, characterized in that the vegetable protein is any protein based on cereals, legumes or seeds and is present in an amount of about 0.05% by weight to about 2.5% by weight.

43. Composition according to claim 41, characterized in that the micellar casein is sodium caseinate or calcium caseinate and is present in an amount of about 0.05% by weight to about 2.5% by weight.

44. Composition, according to any one of claims 2 to 43, characterized in that the stabilizer is one or more of the following: alginate, carrageenan, guar gum, cellulose, such as methylcellulose, microcrystalline cellulose, carboxymethylcellulose, hydroxypropylmethylcellulose (HPMC), sorbitol, xanthan gum, tara gum, locust bean gum, gellan gum (such as high acyl content, low acyl content), beet pectin, skimmed milk powder, whole milk powder, partially skimmed milk powder, milk powder with butter, dairy solids, modified starch, agar-agar, gelatin, gum arabic, konjac, pectin, maltodextrin and tragacanth.

45. Composition, according to any one of claims 2 to 43, characterized in that the emulsifier is one or more of the following: diacetyltartaric acid esters of mono- and / or diglycerides, lactic acid esters of mono- and / or diglycerides, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyglycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose esters, sucrose monostearate, monoglyceride, beeswax, camauba wax, candelilla wax, vegetable waxes, fruit waxes, animal waxes, polyglycerol fatty acid esters and polyglycerol polyricinoleate (PGPR).

46. ​​Composition, according to any one of claims 2 to 43, characterized in that the buffer salt is one or more of any sodium, potassium or calcium citrate, phosphate, carbonate salts, such as sodium polyphosphates, orthophosphate, pyrophosphate, hexametaphosphate, mono- or di-phosphate salts, mono- or di-carbonates and halide salts.

47. Food product, characterized in that it comprises the composition as defined in any one of claims 1 to 46.

48. Food product according to claim 47, characterized in that it is a dairy product, a product not derived from animals, a beverage product or a combination thereof.

49. Food product, according to claim 47 or 48, characterized in that it is a coffee creamer, a cooking creamer, a whipped cream or a similar emulsion with a low or high fat content.

50. Food product, according to any of claims 47 to 49, characterized in that it comprises from Petition 870250080886, dated 09 / 09 / 2025, page 67 / 88 9 / 10 about 0.001% by weight to about 3% by weight of protein.

51. Method for manufacturing the composition, as defined in any one of claims 1 to 46, characterized in that it comprises: forming an oil phase comprising fat; forming an aqueous phase comprising protein; adjusting the oil phase and the aqueous phase from about 15 °C to about 75 °C; mixing the oil phase and the aqueous phase to form a mixture; homogenizing the mixture to form an emulsion; heating the emulsion from about 50 °C to about 145 °C; and cooling the emulsion from about 2 °C to about 30 °C.

52. Method according to claim 51, characterized in that it further comprises packaging the emulsion under sterile or non-sterile conditions.

53. Method according to claim 51 or 52, characterized in that it further comprises storing the emulsion at about -18 °C to about -15 °C, at about 3 °C to about 5 °C or at about 18 °C to about 25 °C.

54. Method according to any one of claims 51 to 53, characterized in that the aqueous phase further comprises stabilizers, emulsifiers and buffering salts.

55. A method according to any one of claims 51 to 54, characterized in that it further comprises aerating the emulsion or storing the emulsion in a quiescent state.

56. Method according to claim 55, characterized in that the aeration comprises beating, mixing using a planetary mixer or beating using a continuous beating machine. Petition 870250080886, dated 09 / 09 / 2025, pp. 68 / 88 10 / 10 57. A method according to any one of claims 51 to 56, characterized in that it further comprises heat treatment, pasteurization or sterilization of the emulsion.

58. Method according to claim 57, characterized in that the heat treatment, pasteurization or sterilization comprises retort, high hydrostatic pressure, ultraviolet radiation, irradiation or ultra-high temperature processing.

59. A method according to any one of claims 51 to 58, characterized in that the emulsion has improved storage stability compared with a corresponding emulsion.

60. Method for preparing a whipped emulsion, characterized in that it comprises whipping the emulsion, as defined in any one of claims 51 to 59, wherein the whipping is carried out at a temperature of about 2 °C to about 8 °C.

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