Highly stable whippable compositions comprising beta-casein

By preparing an emulsion composition with a high content of β-casein, the problem of unclear emulsification properties and stability of casein in high-fat emulsions was solved, achieving optimized emulsification and stability of the emulsion, reducing the total protein content, and improving properties by utilizing recombinant casein.

CN120936249APending Publication Date: 2025-11-11RICH PRODUCTS CORPORATION
View PDF 0 Cites 0 Cited by

Patent Information

Application Number
CN202480018759.4
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Priority Date
2023-03-15
Filing Date
2024-03-15
Publication Date
2025-11-11

AI Technical Summary

Technical Problem

In the existing technology, it is not clear which casein provides the best emulsifying properties and stability in high-fat emulsions, resulting in a lack of scientific basis for the selection of emulsifiers.

Method used

By preparing an emulsion composition containing more than 45% by weight of β-casein, combined with fats, sweeteners, stabilizers, buffer salts and emulsifiers, a whippable or non-whipable emulsion is formed, optimizing emulsification and stability.

Benefits of technology

It improves the emulsifying properties and stability of the emulsion, reduces the total protein content and lowers the cost, while allowing the use of non-bovine recombinant casein to improve properties.

✦ Generated by Eureka AI based on patent content.

Smart Images

  • Figure BDA0005593423030000171
    Figure BDA0005593423030000171
  • Figure BDA0005593423030000172
    Figure BDA0005593423030000172
  • Figure BDA0005593423030000181
    Figure BDA0005593423030000181
Patent Text Reader

Abstract

Disclosed herein are food formulations comprising beta-casein as the predominant casein. Also disclosed herein are compositions comprising a ss-casein enriched casein. Further disclosed herein are whippable or non-whippable emulsion structures comprising a higher amount of beta-casein than those typically found in milk, and methods of making the compositions.
Need to check novelty before this filing date? Find Prior Art

Description

[0001] Cross-reference to related applications

[0002] This application claims priority to U.S. Provisional Patent Application No. 63 / 490,439, filed March 15, 2023, which is incorporated herein by reference in its entirety. Technical Field

[0003] This disclosure relates to food preparations containing β-casein as the main casein. Compositions containing casein rich in β-casein are described herein. Whipable and non-whipable emulsions and methods for preparing compositions are also described herein, the emulsions containing a higher amount of β-casein than those typically found in milk.

[0004] introduction

[0005] Casein is a protein found in milk and can be separated from milk for use in its natural form. Casein can be further modified by dissociation into casein salts or partial hydrolysis into peptides. All three forms are widely used in food applications due to their various technical functional properties, such as solubility, emulsification, foam-forming properties, stabilization, water-binding, gelation, thermal stability, and acid stability.

[0006] Traditionally, sodium caseinate, as a casein derivative in which individual caseins exist in soluble or monomeric forms, is used as an emulsifier in many whipped cream and topping applications due to its solubility, emulsifying ability, and emulsion stability. Sodium caseinate consists of soluble casein with various proportions of αS1 casein, αS2 casein, β-casein, and κ-casein. Caseins have a flexible structure containing a high proportion of nonpolar groups, making them more effective at reducing interfacial tension than rigid proteins with fewer nonpolar groups. β-casein exhibits the highest surface activity, followed by monodisperse casein micelles. αS-casein and κ-casein have similar surface activities; however, they have lower surface activities compared to β-casein and monodisperse casein micelles. Which of the aforementioned caseins contributes to emulsification and stabilization of the emulsion is unknown.

[0007] Therefore, it is necessary to determine which of the aforementioned caseins provides the desired emulsifying properties and stability for food compositions such as high-fat emulsions. Summary of the Invention

[0008] In one aspect, this disclosure relates to an emulsion composition comprising fat and protein, wherein the protein comprises more than 45% by weight β-casein based on the total amount of casein present in the composition. In one embodiment, the composition comprises: about 5% to about 45% by weight of fat; about 0.001% to about 3% by weight of protein; about 0% to about 55% by weight of sweetener; about 0% to about 3% by weight of one or more stabilizers; about 0.0001% to about 2% by weight of buffer salt; and about 0% to about 3% by weight of one or more emulsifiers. In another embodiment, the composition comprises: about 5% to about 35% by weight of fat; about 1% to about 2.5% by weight of protein; about 5% to about 45% by weight of sweetener; about 0.5% to about 3% by weight of one or more stabilizers; about 0.5% to about 2% by weight of buffer salt; and about 0.5% to about 3% by weight of one or more emulsifiers. In another embodiment, the fat is milk fat; vegetable fat; vegetable oil; algal oil; fermented oil derived from bacteria, yeast, or mold; hydrogenated oil; hydrogenated and transesterified oil; hydrogenated, blended, and transesterified oil; medium-chain triglyceride (MCT) vegetable oil; milk fat; ghee; anhydrous milk fat; butter; or combinations thereof. In another embodiment, the protein is animal protein, recombinant milk protein, plant-based protein, or combinations thereof. In another embodiment, the protein is natural casein, recombinant casein, or combinations thereof. In another embodiment, based on the total composition, the composition contains less than 0.03% by weight of total κ-casein. In another embodiment, the protein is rich in 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 contains about 60% to about 100% of the same amino acid sequence as mammalian milk proteins such as bovine milk protein, sheep milk protein, camel milk protein, yak milk protein, buffalo milk protein, mare milk protein, or goat milk protein. In another embodiment, the proportion of β-casein is from about 45% to about 100% of the total casein in the composition. In another embodiment, the β-casein is in micellar or monomeric form; wherein when the β-casein is in monomeric form, it has a protein particle size of less than 50 nm. In another embodiment, the β-casein is in micellar or monomeric form; wherein when the β-casein is in micellar form, it has a protein particle size of less than 500 nm. In another embodiment, the β-casein has a zeta potential of from 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, tumble drying, or freeze-drying to remove water. In another embodiment, the protein is a single type of natural 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 two or more different types of animal milk proteins, recombinant milk proteins, and plant-based proteins. In another embodiment, the protein may or may not have post-translational modifications. In another embodiment, the post-translational modification is one or more of glycosylation and phosphorylation. In another embodiment, the protein is phosphorylated. In another embodiment, the protein contains non-natural phosphorylation. In another embodiment, the recombinant casein is produced by fungal cells, yeast cells, bacterial cells, algae, or a transgenic method. In another embodiment, the sweetener is a nutritional sweetener, a non-nutritive sweetener, or a combination thereof. In another embodiment, the nutritional 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, syrup; soluble / insoluble fiber derived from corn, wheat, peas, rice, oats, coconut, barley and / or cassava; fructooligosaccharides and galactooligosaccharides; and hydrolyzed cereal powder; or combinations thereof. In another embodiment, the non-nutritive sweetener is sucralose; aspartame; saccharin; stevia; monk fruit extract; neotame; advansatilla; acetylsupanol; sugar alcohols such as maltitol, xylitol, sorbitol, erythritol, mannitol, isomaltitol, lactitol; hydrogenated starch hydrolysate; or combinations thereof. In another embodiment, the sweetener is one or more of brassinolide, curculigo, areca nut, mirabilite, monetin, pentadiene, and sematinine. In another embodiment, the fat comprises one or more lipids derived from plants or animals; one or more lipids derived from milk; or combinations thereof. In another embodiment, the fat comprises one or more monoglycerides, diglycerides, triglycerides, and / or phospholipids, comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid, and decanoic acid. In another embodiment, the one or more monoglycerides, diglycerides, triglycerides, and / or phospholipids are plant-based transesterified monoglycerides, diglycerides, triglycerides, and / or phospholipids, comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid, and decanoic acid. In another embodiment, the fat is a hydrogenated oil; a transesterified oil; a hydrogenated and transesterified oil; a hydrogenated, blended, and transesterified oil; or a combination thereof. In another embodiment, one or more monoglycerides, diglycerides, triglycerides, and / or phospholipids comprise fatty acyl chains in a percentage similar to the percentage of fatty acyl chains found in mammalian-derived milk or dairy products. In another embodiment, the composition is whippable. In another embodiment, the composition is non-whipable. In another embodiment, the composition is cooking cream or coffee creamer. In another embodiment, the fat is fully hydrogenated, partially hydrogenated, transesterified, non-hydrogenated, or hydrogenated and transesterified. In another embodiment, the fat is fully hydrogenated.In another embodiment, the composition further comprises a crystallizing agent, a flavoring agent, a salt, a preservative, or a combination thereof. In another embodiment, the protein is one or more of monomeric casein, sodium caseinate, calcium caseinate, potassium caseinate, acidic casein, rennet casein, micelles, and globular proteins. In another embodiment, the globular protein is one or more of milk proteins, plant proteins, α-lactalbumin, β-lactoglobulin, ovalbumin, ovoglobulin, and recombinant proteins. In another embodiment, the micelle protein is micelle casein, recombinant micelle casein, or a combination thereof. In another embodiment, the plant protein is any cereal, legume, or seed-based protein and is present in an amount from about 0.05% by weight to about 2.5% by weight. In another embodiment, the micelle casein is sodium caseinate or calcium caseinate and is present in an amount from about 0.05% by weight to about 2.5% by weight. In another embodiment, the stabilizer is alginate; carrageenan; guar gum; cellulose such as methylcellulose, microcrystalline cellulose, carboxymethyl cellulose, hydroxypropyl methylcellulose (HPMC); sorbitol; xanthan gum; tara gum; locust bean gum; gellan gum (such as high acyl, low acyl); beet pectin; skim milk powder; whole milk powder; partially skim milk powder; butter milk powder; dairy solids; modified starch; agar; gelatin; gum arabic; konjac; pectin; maltodextrin and astragalus gum, or more thereof. In another embodiment, the emulsifier is one or more of the following: diacetyl tartrate of monoglycerides and / or diglycerides, lactate of monoglycerides and / or diglycerides, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyethylene glycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose ester, sucrose monostearate, monoglycerides, beeswax, carmopa wax, candelilla wax, plant wax, fruit wax, animal wax, polyglycerol fatty acid esters, and polyglycerol ricinoleate (PGPR). In another embodiment, the buffer salt is one or more of the following: any sodium or potassium or calcium salt of citrate, phosphate, carbonate, and halide salts, such as sodium polyphosphate, orthophosphate, pyrophosphate, hexametaphosphate, monophosphate or diphosphate, monocarbonate or dicarbonate.

[0009] In another aspect, this disclosure relates to food products 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 one embodiment, the food product is a coffee creamer, cooking cream, whipped cream, or a similar low- to high-fat emulsion. In another embodiment, the food product contains about 0.001% by weight to about 3% by weight of protein.

[0010] In another aspect, this disclosure relates to a method of manufacturing a composition according to any one of claims 1 to 46, the method comprising: forming an oil phase comprising fats; forming an aqueous phase comprising proteins; 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 to about 50°C to about 145°C; and cooling the emulsion to about 2°C to about 30°C. In one embodiment, the method further comprises packaging the emulsion under aseptic or non-aseptic conditions. In another embodiment, the method further comprises storing the emulsion at about -18°C to about -15°C, about 3°C ​​to about 5°C, or about 18°C ​​to about 25°C. In another embodiment, the aqueous phase further comprises a stabilizer, an emulsifier, and a buffer salt. In another embodiment, the method further comprises aerating the emulsion or storing the emulsion statically. In another embodiment, aeration comprises stirring, mixing using a planetary mixer, or beating using a continuous beater. In another embodiment, the method further comprises heat-treating, pasteurizing, or sterilizing the emulsion. In another embodiment, heat treatment, pasteurization, or sterilization includes boiling, high hydrostatic pressure, ultraviolet radiation, irradiation, or ultra-high temperature treatment. In another embodiment, the emulsion has improved storage stability compared to the corresponding emulsion.

[0011] In another aspect, this disclosure relates to a method for preparing a whipped emulsion, the method comprising whipping any emulsion described herein, wherein whipping may be performed at about 2°C to about 8°C.

[0012] This disclosure provides for other aspects and embodiments that will become apparent from the following detailed description and accompanying drawings. Attached Figure Description

[0013] Figure 1 This is a graph showing the capillary electrophoresis elution curves for the β-casein extract.

[0014] Figure 2 This is an RP-HPLC chromatogram of the neutralized β-casein extract, demonstrating the high purity of β-casein compared to other milk proteins.

[0015] Figure 3 This is a graph showing the particle size density (PSD) data of protein particles in solution measured using the Zetasizer DLS technology.

[0016] Figure 4 This is a graph showing the surface tension measurement of the air-water interface in a rising droplet configuration using an automated droplet tensiometer after a 25-minute equilibration time.

[0017] Figure 5This is a graph showing the decay of foam height in a 0.25% protein solution over time, as measured by a dynamic foam analyzer.

[0018] Figure 6 These are images of a beaten sodium caseinate composition and a beaten β-casein composition.

[0019] Figure 7 This is a graph showing the effect of increasing the proportion of β-casein in a protein blend containing sodium caseinate on particle size in a simple emulsion (20% rapeseed oil).

[0020] Figure 8 This is an image showing the initial (t=0) rosettes from the stirred samples E, F, G, H, I, and J.

[0021] Figure 9 Images show the stability bowls of samples E, F, G, H, I, and J after refrigeration (i.e., from about 2°C to about 4°C) for 24 hours. Detailed Implementation

[0022] Due to its amphiphilic structure, β-casein possesses emulsifying and foam-stabilizing properties. This paper describes protein solutions enriched with β-casein. Experiments in this paper characterize the functionality of β-casein in emulsions used in creamers, toppings, and high-fat toppings. Furthermore, this paper demonstrates that enriching protein solutions with β-casein leads to a reduction in overall protein content and cost savings. Finally, in addition to bovine casein, non-bovine casein from recombinant sources can also be used to improve emulsion properties.

[0023] 1. Definition

[0024] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art. In case of conflict, this document (including the definitions) shall prevail. While preferred methods and materials are described below, similar or equivalent methods and materials may be used in the implementation or testing of the invention. All publications, patent applications, patents, and other references mentioned herein are incorporated herein by reference in their entirety. The materials, methods, and examples disclosed herein are illustrative only and are not intended to be limiting.

[0025] As used herein, the terms “comprising,” “including,” “having,” “having,” “may,” “containing,” and variations thereof are intended as open-ended transitional phrases, terms, or words that do not exclude the possibility of additional actions or structures. The singular forms “a,” “an,” and “the” include plural references unless the context clearly indicates otherwise. This disclosure also contemplates other embodiments that “comprise” the embodiments or elements presented herein, “consist of” the embodiments or elements presented herein, and “consist substantially of” the embodiments or elements presented herein, whether or not explicitly stated.

[0026] For the numerical ranges listed in this article, each intermediate number with the same degree of precision between them is explicitly envisioned. For example, for the range of 6 to 9, the numbers 7 and 8 are considered in addition to 6 and 9; for the range of 6 to 9, the numbers 7 and 8 are considered in addition to 6 and 9; and for the range of 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 envisioned.

[0027] As used herein, when applied to one or more values ​​of interest, the term "about" or "approximately" refers to a value similar to the reference value, or a value within an acceptable error range for a particular value as determined by a person skilled in the art, which will depend in part on how the value was measured or determined, such as limitations of the measurement system. In some respects, the term "about" refers to a range of values ​​that are 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 than the reference value, unless otherwise stated or obvious from the context (unless the number would exceed 100% of a possible value). Alternatively, according to practice in this art, "about" may mean within 3 or greater than 3 standard deviations. Alternatively, such as for biological systems or processes, the term "about" may mean within an order of magnitude, preferably within 5 times the value, and more preferably within 2 times.

[0028] As used herein, the term "casein monomer" refers to a polypeptide comprising a sequence of at least 20 amino acids (e.g., 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 generally not exceeding 250 amino acids), which is at least 80% identical (e.g., at least 85%, at least 90%, at least 95%, at least 99%) to the amino acid sequence in casein and is repeated in the polymers provided herein. For example, a casein monomer may comprise a polypeptide comprising a sequence of the following amino acids: 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, a casein monomer may not exceed 220 amino acids. Non-limiting examples of casein include β-casein, γ-casein, κ-casein, αS1-casein, and αS2-casein.

[0029] As used in this article, “cheese” refers to a group of fermented dairy-based products, representing one of the typical examples of food preservation, such as the gelation of casein through isoelectric (acid) or enzymatic (rennet) coagulation. Some cheeses are produced through a combination of heat and acid, while fewer are produced through thermal evaporation and by removing water and reducing the activity of water with or without the addition of NaCl. Cheese produced by acid or heat / acid coagulation is typically eaten fresh, while rennet cheese is almost always matured through the action of a complex enzymatic cell before consumption.

[0030] As used herein, “cheese product” refers to pasteurized cheese product (PCP), which is a cheese-based food product produced by pulverizing, blending, and melting one or more natural cheeses and optional ingredients into a smooth, homogeneous blend using the aid of heat, mechanical shearing, and (usually) emulsifying salts (ES).

[0031] As used herein, the term "host cell" or "recombinant host cell" refers to a cell containing the introduced recombinant polynucleotide. It should be understood that such terms refer not only to a specific subject cell but also to the progeny of such cells. Because certain modifications may occur in offspring due to mutations or environmental influences, these progeny cells may differ from the parent cells but are still included within the scope of the term "host cell" or "recombinant host cell" as used herein.

[0032] As used herein in the context of polynucleotide or polypeptide sequences, the term "identical" refers to the same residues in two sequences when the alignment yields the maximum correspondence. Many different algorithms are known in the art for measuring the identity of polynucleotide or polypeptide sequences. For example, sequences can be compared using: FASTA (e.g., using default parameters provided in Wisconsin Package Version 10.0, Genetics Computer Group (GCG), Madison, Wis.), Gap (e.g., using default parameters provided in Wisconsin Package Version 10.0, GCG, Madison, Wis.), Bestfit, ClustalW (e.g., using default parameters in version 1.83), or BLAST (e.g., utilizing reciprocal BLAST, PSI-BLAST, BLASTP, BLASTN) (see, for example, Pearson. 1990. Methods Enzymol. 183:63; Altschul et al. 1990. J. Mol. Biol. 215:403).

[0033] As used herein, “native” or “natural” means an ingredient derived from an animal or plant and is not synthesized or recombined from other forms of ingredient. As used herein, “native casein” or “natural casein” means casein derived from bovine or mammalian milk and is not synthesized or recombined from other forms of casein.

[0034] As used herein, the term “post-translational modification” or its acronym “PTM” refers to the covalent attachment of a chemical group to a protein after protein biosynthesis. PTM can occur on the amino acid side chains of a protein or at its C- or N-terminus. Non-limiting examples of PTM include glycosylation (i.e., proteins covalently attached to glycan groups, i.e., 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-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-neuraminic acid, furanylgalactose, phosphodiester, N-acetylglucosamine, N-acetylgalactosamine, sialic acid, and combinations thereof; see, for example, Deshpande et al., 2008. Glycobiology. 18(8):626), via C-bond, N-bond or O-bond, or via glycosylation (i.e., adding glycosyl phosphatidylinositol anchors) or phosphorylated (i.e., linked via phosphate of phosphoserine), phosphorylation (i.e., proteins covalently linked to phosphate groups), alkylation (i.e., proteins covalently linked to chain alkyl groups (e.g., methyl alkyl groups in methylation) and lipidation (i.e., covalently linked to lipid groups (e.g., isoprenyl groups in isoprenylation and isoprenylation (e.g., farnesol groups in farnesylation, geranylation)). Geraniol group in geraniol geraniol group, geraniol group in geraniol geraniol acylation, fatty acid group in fatty acid acylation (e.g., myristic acid in myristoylation, palmitic acid in palmitoylation), glycosyl phosphatidylinositol anchor in glycosyl phosphatidylinositol acylation, hydroxylation (i.e., covalent linkage of hydroxide group), threonization (i.e., protein linked to small ubiquitin-like modified (or SUMO) protein), nitrosylation (i.e., protein linked to NO group), and tyrosine nitration (i.e., tyrosine residue in protein linked to nitrate group).

[0035] As used herein, the terms “recombinant protein” or “recombinant β-casein” refer to proteins produced through recombinant processes (i.e., produced by recombinant host cells) or β-casein, respectively. Protein expression in host cells can be transient or stable.

[0036] As used herein, the term "recombinant polynucleotide" refers to a polynucleotide that has been removed from its natural environment, a polynucleotide that is wholly or partially unrelated to a polynucleotide adjacent to or near it when found in nature, a polynucleotide operatively linked to a polynucleotide not linked in nature, or a polynucleotide not found in nature. This term can be used, for example, to describe cloned DNA isolates or polynucleotides containing chemically synthesized nucleotide analogs. A polynucleotide is also considered "recombinant" if it contains any non-naturally occurring genetic modifications. For example, an endogenous polynucleotide is considered "recombinant" if it contains the insertion, deletion, or substitution of one or more nucleotides artificially introduced (e.g., through human intervention). Such modifications can introduce point mutations, substitution mutations, deletion mutations, insertion mutations, missense mutations, frameshift mutations, replication mutations, amplification mutations, translocation mutations, or inversion mutations into a polynucleotide. The term includes polynucleotides found in the host cell chromosome as well as polynucleotides not found in the host cell chromosome (e.g., polynucleotides contained in free tissue).

[0037] As used herein, "sweetener" refers to an ingredient and / or mixture of ingredients that impart sweetness to a final product.

[0038] As used herein, “yogurt” refers to a food produced by culturing one or more optional dairy ingredients in a culture of characterizing bacteria containing lactic acid-producing bacteria, such as Lactobacillus delbrueckii subsp. bulgaricus and Streptococcus thermophilus, to pH 4.6 or lower.

[0039] As used in this article, "yogurt products" refers to products in which yogurt is used as an ingredient, such as yogurt containing fruit, smoothies, and cultured beverages.

[0040] Unless otherwise defined herein, scientific and technical terms used in conjunction with this disclosure shall have the meanings commonly understood by one of ordinary skill in the art. For example, any nomenclature and techniques used in conjunction with the food science, microbiology, biochemistry, and chemistry described herein are well-known and commonly used in the art. The meaning and scope of terms shall be clear; however, in the event of any potential ambiguity, the definitions provided herein shall prevail over any dictionary or external definition. Furthermore, unless the context requires otherwise, singular terms shall include plural forms and plural terms shall include singular forms.

[0041] 2. Composition

[0042] This document provides compositions for emulsifying and stabilizing both whippable and non-whipable food products. In some embodiments, the composition may comprise proteins, such as β-casein, and fats. The total protein content can be from about 0.05% to about 3% by weight, about 0.10% to about 3% by weight, about 0.15% to about 3% by weight, about 0.25% to about 3% by weight, about 0.50% to about 3% by weight, about 1% to about 3% by weight, about 1.5% to about 3% by weight, about 2% to about 3% by weight, about 2.5% to about 3% by weight, about 0.05% to about 2.5% by weight, about 0.05% to about 2% by weight, about 0.05% to about 1.5% by weight, about 0.05% to about 1% by weight, about 0.05% to about 0.50% by weight, about 0.05% to about 0.25% by weight, about 0.05% to about 0.15% by weight, or about 0.05% to about 0.10% by weight. In some embodiments, the total protein content can be from about 0.05% to about 3% by weight of the composition. Based on the total amount of protein present in the composition, the protein may comprise from about 0.01% by weight to about 100% by weight of casein. Based on the total amount of protein present in the composition, the 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, about 80% by weight to about 100% by weight, about 90% by weight, etc. Casein in the composition, ranging from about 100% by weight, about 0.01% by weight to about 90% by weight, about 0.01% by weight to about 80% by weight, about 0.01% by weight to about 70% by weight, about 0.01% by weight to about 60% by weight, about 0.01% by weight to about 50% by weight, about 0.01% by weight to about 40% by weight, about 0.01% by weight to about 30% by weight, about 0.01% by weight to about 20% by weight, about 0.01% by weight to about 10% by weight, about 0.01% by weight to about 1% by weight, or about 0.5% by weight to about 100% by weight. Based on the total amount of casein present in the composition, the protein may comprise about 45% by weight to about 100% by weight of β-casein.Based on the total amount of casein present in the composition, the protein may comprise about 45% to about 100% by weight, about 50% to about 100% by weight, about 55% to about 100% by weight, about 60% to about 100% by weight, about 65% to about 100% by weight, about 70% to about 100% by weight, about 75% to about 100% by weight, about 80% to about 100% by weight, about 85% to about 100% by weight, about 90% to about 100% by weight, and so on. The composition may contain 0% by weight, about 95% by weight to about 100% by weight, about 45% by weight to about 95% by weight, about 45% by weight to about 90% by weight, about 45% by weight to about 85% by weight, about 45% by weight to about 80% by weight, about 45% by weight to about 75% by weight, about 45% by weight to about 70% by weight, about 45% by weight to about 65% by weight, about 45% by weight to about 60% by weight, about 45% by weight to about 55% by weight, or about 45% by weight to about 50% by weight. Based on the total amount of casein present in the composition, the protein may contain 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. The composition may further contain sweeteners, stabilizers, buffer salts, fillers, and emulsifiers.

[0043] a. protein

[0044] The composition may comprise from about 0.001 wt% to about 3 wt%, about 0.01 wt% to about 3 wt%, about 0.1 wt% to about 3 wt%, about 1 wt% to about 3 wt%, about 2 wt% to about 3 wt%, about 0.001 wt% to about 2 wt%, about 0.001 wt% to about 1 wt%, about 0.001 wt% to about 0.1 wt%, or about 0.001 wt% to about 0.01 wt% of protein. In some embodiments, the composition may comprise from about 0.001 wt% to about 3 wt% of protein. In some embodiments, the composition may comprise from about 1 wt% to about 2 wt% of protein. The protein may be in liquid or powder form. The powder form may be prepared by spray drying, roller drying, tumble drying, or freeze drying of the protein to remove moisture. The protein may lack one or more post-translational modifications. For example, the protein may lack one or more of the following post-translational modifications: glycosylation, phosphorylation, or a combination thereof. The protein may be phosphorylated. The protein may contain non-native phosphorylation. Proteins can be one or more of monomeric casein, sodium caseinate, calcium caseinate, micellar protein, and globular protein. Globular proteins can be one or more of milk proteins, plant proteins, β-lactoglobulin, ovalbumin, α-lactalbumin, ovoglobulin, bacterial proteins, fungal proteins, and recombinant proteins. Micellar proteins 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, skim milk powder, whole milk powder, partially skimmed milk powder, or butter milk powder. Casein may be present in the composition in amounts from about 0.05 wt% to about 2.5 wt%, from about 0.1 wt% to about 2.5 wt%, from about 0.5 wt% to about 2.5 wt%, from about 1.0 wt% to about 2.5 wt%, from about 1.5 wt% to about 2.5 wt%, from about 2.0 wt% to about 2.5 wt%, from about 0.05 wt% to about 2.0 wt%, from about 0.05 wt% to about 1.5 wt%, from about 0.05 wt% to about 1.0 wt%, from about 0.05 wt% to about 0.5 wt%, or from about 0.05 wt% to about 0.1 wt%. In some embodiments, casein may be present in the composition in amounts from about 0.05 wt% to about 2.5 wt%. The amount of casein present in the composition does not exceed 2.6 wt%.The plant protein can be any protein isolate or concentrate based on grains, legumes, or seeds, and can be present in the composition in amounts from about 0.05 wt% to about 2.0 wt%, from about 0.1 wt% to about 2.0 wt%, from about 0.5 wt% to about 2.0 wt%, from about 1.0 wt% to about 2.0 wt%, from about 1.5 wt% to about 2.0 wt%, from about 0.05 wt% to about 1.5 wt%, from about 0.05 wt% to about 1.0 wt%, from about 0.05 wt% to about 0.5 wt%, or from about 0.05 wt% to about 0.1 wt%. In some embodiments, the plant protein can be any protein isolate or concentrate based on grains, legumes, or seeds, and can be present in the composition in amounts from about 0.05 wt% to about 2 wt%. The protein can be two different types of animal and / or recombinant milk proteins. The protein can be a single type of natural milk protein or a single type of recombinant milk protein. The single type of protein can be β-casein.

[0045] The compositions disclosed herein are not intended for use in cheese or yogurt, or cheese or yogurt products. Furthermore, k-casein is typically not used in the whippable products described herein.

[0046] In some embodiments, the disclosed composition may contain a total κ-casein content of less than 0.03% by weight based on the total composition. Amounts of less than 0.03% by weight can help avoid product instability caused by aging and gelation. K-casein can participate in thiol-disulfide exchange reactions with other proteins containing sulfur-containing amino acids, leading to aging, gelation, and subsequent instability. See: Nair and Corredig, Journal of Dairy Science, 2021; 104(1):92-101.

[0047] β-casein can be derived from cow's 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 skim milk (e.g., milk with about 0.8% by weight or less milk fat). β-casein can be separated from other components of milk to produce β-casein purified to 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.

[0048] β-casein may be recombinant and may contain an amino acid sequence that is 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 the amino acid sequence of bovine milk protein, sheep milk protein, mare milk protein, or goat milk protein.

[0049] b. Fat

[0050] One or more fats may be used in the compositions disclosed herein. The fat may be milk fat, vegetable fat, vegetable oil, algae, fungi, recombinant-derived fat, or a combination thereof. The fat may be fully hydrogenated, partially hydrogenated, transesterified, or hydrogenated and transesterified, or a combination thereof, with or without unmodified fat. The composition may contain about 5% to about 45% by weight, about 10% to about 45% by weight, about 15% to about 45% by weight, about 20% to about 45% by weight, about 25% to about 45% by weight, about 30% to about 45% by weight, about 35% to about 45% by weight, about 40% to about 45% by weight, about 5% to about 40% by weight, about 5% to about 35% by weight, about 5% to about 30% by weight, about 5% to about 25% by weight, about 5% to about 20% by weight, about 5% to about 15% by weight, or about 5% to about 10% by weight of fat. In some embodiments, the composition may contain about 25% to about 35% by weight of fat.

[0051] Fats may contain one or more lipids derived from plants; one or more lipids derived from milk; or a combination thereof.

[0052] The fat may contain one or more monoglycerides, diglycerides, triglycerides, and / or phospholipids, comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid, and capric acid. The one or more monoglycerides, diglycerides, triglycerides, and / or phospholipids may be plant-based transesterified monoglycerides, diglycerides, triglycerides, and / or phospholipids. The one or more monoglycerides, diglycerides, triglycerides, and / or phospholipids may contain fatty acyl chains in a percentage similar to the percentage of fatty acyl chains found in mammalian-derived milk or dairy products.

[0053] c. Sweeteners

[0054] The composition may comprise from about 0% to about 45% by weight, about 5% to about 45% by weight, about 10% to about 45% by weight, about 15% to about 45% by weight, about 20% to about 45% by weight, about 25% to about 45% by weight, about 30% to about 45% by weight, about 35% to about 45% by weight, about 40% to about 45% by weight, about 0% to about 40% by weight, about 0% to about 35% by weight, about 0% to about 30% by weight, about 0% to about 25% by weight, about 0% to about 20% by weight, about 0% to about 15% by weight, about 0% to about 10% by weight, or about 0% to about 5% by weight. In some embodiments, the composition may comprise from about 5% to about 25% by weight of a sweetener. The sweetener may be a nutritional sweetener or a non-nutritive sweetener. Nutritional sweeteners 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. Non-nutritive sweeteners may be one or more of sucralose, aspartame, saccharin, stevia, monk fruit extract, neotame, advansame, and acetylsupan potassium. Sweeteners may be one or more of carrageenan, curculigo, areca nut, mirabilite, monetin, pentadiene, and sematinine.

[0055] d. Stabilizer

[0056] The composition may contain one or more stabilizers from about 0% to about 3% by weight, about 0.5% to about 3% by weight, about 1% to about 3% by weight, about 1.5% to about 3% by weight, about 2% to about 3% by weight, about 2.5% to about 3% by weight, about 0% to about 2.5% by weight, about 0% to about 2% by weight, about 0% to about 1.5% by weight, about 0% to about 1% by weight, or about 0% to about 0.5% by weight. In some embodiments, the composition may contain one or more stabilizers from about 0.5% to about 1% by weight. The stabilizer may be one or more of alginate, carrageenan, guar gum, microcrystalline cellulose, carboxymethyl cellulose, sorbitol, hydroxypropyl methylcellulose (HPMC), xanthan gum, tara gum, and locust bean gum. Stabilizers may be one or more of alginate, carrageenan, guar gum, and cellulose; for example, methylcellulose, microcrystalline cellulose, carboxymethylcellulose, sorbitol, hydroxypropyl methylcellulose (HPMC), xanthan gum, tara gum, locust bean gum, gellan gum, beet pectin, plant protein, sodium caseinate, skim milk powder, milk protein isolate / concentrate, micellar casein isolate / concentrate, acidic casein powder, rennet casein powder, whey protein concentrate / isolate powder, dairy solids, whole milk powder, partially skimmed milk powder, butter milk powder, modified starch, agar, gelatin, gellan gum (e.g., high acyl, low acyl), gum arabic, konjac, pectin, maltodextrin, astragalus gum, or combinations thereof.

[0057] Stabilizers can maintain a degree of homogeneity in the composition. In some embodiments, stabilizers can act as emulsifiers to supplement casein. Stabilizers can also act as whitening agents when they help stabilize finely emulsified fat and / or oil globules that scatter light in the emulsion.

[0058] e. Buffer salts

[0059] The composition may comprise from about 0.0001 wt% to about 2 wt%, from about 0.001 wt% to about 2 wt%, from about 0.01 wt% to about 2 wt%, from about 0.1 wt% to about 2 wt%, from about 1 wt% to about 2 wt%, from about 1.5 wt% to about 2 wt%, from about 0.0001 wt% to about 1.5 wt%, from about 0.0001 wt% to about 1 wt%, from about 0.0001 wt% to about 0.1 wt%, from about 0.0001 wt% to about 0.01 wt%, or from about 0.0001 wt% to about 0.001 wt% of a buffer salt. In some embodiments, the composition may comprise from about 0.5 wt% to about 1 wt% of a buffer salt. The buffer salt may be one or more of a phosphate, halide, carbonate, bicarbonate, tartrate, and citrate.

[0060] f. Filler

[0061] The composition may contain about 0% to about 50% by weight, about 10% to about 50% by weight, about 20% to about 50% by weight, about 30% to about 50% by weight, about 40% to about 50% by weight, about 0% to about 40% by weight, about 0% to about 30% by weight, about 0% to about 20% by weight, or about 0% to about 10% by weight of a filler. The filler may be one or more of high fructose corn syrup, starch, modified starch, and maltodextrose.

[0062] g. Emulsifier

[0063] The composition may contain one or more emulsifiers in amounts of about 0% to about 3% by weight, about 0% to about 0.5% by weight, about 0% to about 1% by weight, about 0% to about 1.5% by weight, about 0% to about 2% by weight, about 0% to about 2.5% by weight, about 0.5% to about 3% by weight, about 1% to about 3% by weight, about 1.5% to about 3% by weight, about 2% to about 3% by weight, or about 2.5% to about 3% by weight. In some embodiments, the composition may contain one or more emulsifiers in amounts of about 0.5% to about 1% by weight. The emulsifier may be one or more of the following: diacetyl tartrate of monoglycerides and / or diglycerides, lactate of monoglycerides and / or diglycerides, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyethylene glycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose ester, sucrose monostearate, and monoglycerides. Emulsifiers can be one or more of the following: sugar esters, beeswax, carnauba wax, candelilla wax, plant waxes, fruit waxes, animal waxes, polyglycerol fatty acid esters, polyglycerol ricinoleate (PGPR), polysorbate (polyoxyethylene sorbitan ester), monoglycerides, diglycerides, diacetyl tartrate of monoglycerides and / or diglycerides, lactates of monoglycerides and / or diglycerides, sodium stearoyl lactylate, sorbitan monostearate, polyethylene glycol esters, propylene glycol monostearate, and lecithin. It is noteworthy that waxes, due to their minimal surface activity, can act more as fatty acid modifiers than emulsifiers.

[0064] 3. A method for preparing a composition containing β-casein

[0065] This document provides a method for preparing compositions as described herein. The method may include: forming an oil phase comprising fats; forming an aqueous phase comprising proteins; heating the oil phase and the aqueous phase to about 15°C to about 75°C, about 25°C to about 75°C, about 35°C to about 75°C, about 45°C to about 75°C, about 55°C to about 75°C, about 65°C to about 75°C, about 15°C to about 65°C, about 15°C to about 55°C, about 15°C to about 45°C, about 15°C to about 35°C, or about 15°C to about 25°C; mixing the oil phase and the aqueous phase to form a mixture; homogenizing the mixture to form an emulsion; heating the emulsion to about 60°C to about 150°C, about 60°C to about 140°C, about 60°C to about 130°C, or about 60°C to... About 120°C, about 60°C to about 110°C, about 60°C to about 100°C, about 60°C to about 90°C, about 60°C to about 80°C, about 60°C to about 70°C, about 70°C to about 150°C, about 80°C to about 150°C, about 90°C to about 150°C, about 100°C to about 150°C, 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 cooling the emulsion to about 2°C to about 30°C, about 4°C to about 30°C, about 8°C to about 30°C, about 16°C to about 30°C, about 2°C to about 16°C, about 2°C to about 8°C, or about 2°C to about 4°C. The emulsion can be heated to pasteurization levels (e.g., at least about 72°C for at least about 15 seconds) and UHT pasteurization levels (e.g., about 135°C to about 154°C, such as about 145°C, for about 1 second to about 8 seconds), and then packaged in a non-sterile or sterile environment. Storage temperatures can vary depending on the specific heat treatment and packaging, i.e., freezing (e.g., about -18°C to about -15°C), refrigeration (e.g., about 3°C ​​to about 5°C), or ambient temperature (e.g., about 18°C ​​to about 25°C). The method may further include packaging the emulsion. Packaging may include, but is not limited to, bags, bricks (e.g., 250 mL to half-gallon), jugs (e.g., 250 mL to gallon jugs), bags in boxes (up to 20 lbs), tote bags, cake decorating bags, etc. The aqueous phase may further include stabilizers, emulsifiers, and buffer salts. The method may further include aerating the emulsion. Aeration may include stirring, mixing using a planetary mixer, or beating using a continuous beater. The method may further include heat treatment, pasteurization, or sterilization of the emulsion. Heat treatment, pasteurization, or sterilization may include boiling, high hydrostatic pressure, or ultra-high temperature treatment. The emulsion exhibits improved storage stability compared to the corresponding emulsion. The whipped emulsion can be prepared by whipping the emulsion as described herein at approximately 2°C to approximately 8°C, approximately 3°C to approximately 8°C, approximately 4°C to approximately 8°C, approximately 5°C to approximately 8°C, approximately 6°C to approximately 8°C, approximately 7°C to approximately 8°C, approximately 2°C to approximately 7°C, approximately 2°C to approximately 6°C, approximately 2°C to approximately 5°C, approximately 2°C to approximately 4°C, or approximately 2°C to approximately 3°C.

[0066] 4. Food products

[0067] This document describes food products comprising compositions as described herein. Food products may be dairy or non-dairy products, such as coffee creamer, cooking cream, whipped cream, or similar low- to high-fat emulsions. Food products may contain about 0.001% to about 3% by weight, about 0.01% to about 3% by weight, about 0.1% to about 3% by weight, about 1% to about 3% by weight, about 2% to about 3% by weight, about 0.001% to about 2% by weight, about 0.001% to about 1% by weight, about 0.001% to about 0.1% by weight, or about 0.001% to about 0.01% by weight of protein. Food products may contain about 0.1% to about 2.5% by weight, about 0.5% to about 2.5% by weight, about 1% to about 2.5% by weight, about 1.5% to about 2.5% by weight, about 2.0% to about 2.5% by weight, about 0.1% to about 2.0% by weight, about 0.1% to about 1.5% by weight, about 0.1% to about 1% by weight, or about 0.1% to about 0.5% by weight of total casein.

[0068] 5. Examples

[0069] The foregoing can be better understood by referring to the following examples, which are presented for illustrative purposes and are not intended to limit the scope of the invention. This disclosure has multiple aspects and embodiments, illustrated by the appended non-limiting examples.

[0070] Example 1

[0071] Isolation of β-casein from milk

[0072] It is hypothesized that β-casein may be the primary cause of the high functionality of sodium caseinate. To develop protein solutions rich in β-casein, starting materials could be reconstituted micellar casein powder or skim milk. Unlike the other two major fractions of casein, αS-casein and k-casein, the dissociation of β-casein from the micelles is temperature-dependent. When the milk is cooled to below 5°C, β-casein dissociates from the casein micelles into the serum phase; this is a reversible process. β-casein can be separated from skim milk at low temperatures using microfiltration (MF). The current method is a slight modification of the method described by Hoffmann et al., (2006) KielerMilchwirtschaftliche Forschungsberichte, 58(1), 41-51, and Schafer et al., (2019) International Dairy Journal, 97, 222-229. This involves MF at low temperatures and subsequent concentration of the MF permeate using an ultrafiltration (UF) process.

[0073] Microfilter skim milk or micellar casein or whey protein solution (adjusted to 3.5% protein content using deionized water) at 55°C to separate soluble whey protein from casein. Obtain a permeate rich in casein micelles and a permeate rich in whey protein. Discard the latter portion and adjust the former portion again to 3.5% protein content using deionized water. Microfilter it further to remove the permeate rich in whey protein fraction. This dialysis step can be repeated to reduce the whey protein content. Dilute the permeate back with deionized water to obtain the original protein content as skim milk. Keep the solution at low temperature (<4°C) for 48 to 72 hours, as β-casein dissociates from casein micelles at low temperature due to weakened hydrophobic interactions. Then microfilter the solution at 4°C using a 100 kDa membrane to obtain a permeate rich in both β-casein and whey protein. Discard the obtained permeate. The solution was then concentrated using ultrafiltration (10 kDa membrane) to produce a β-casein-rich osmotic residue. The osmotic residue solution was titrated with 1 N HCl to precipitate β-casein at approximately pH 4.6. The slurry was centrifuged at 4000 g for 35 min to separate the β-casein-rich precipitate from whey protein present in serum. The precipitate was further washed with deionized water to remove residual whey protein. The precipitated β-casein was mixed with water to obtain a slurry containing 20% ​​to 30% TS, and titrated back to pH 6.7 using 0.01 N NaOH. The solution was slowly heated to 65 °C to completely dissolve the β-casein. The protein composition of the starting material and the resulting UF osmotic residue was analyzed using capillary electrophoresis. Figure 1 ) and HPLC Figure 2 The compositions are shown in Table 1. This β-casein-rich solution is used to develop liquid emulsion compositions and high-fat emulsions that can be aerated with greater stability than sodium caseinate alone.

[0074] Table 1. Percentage of casein in three independent experimental compositions

[0075] Casein type % β-casein 89.8±2.4 α-S1 8.5±1.5 α-S2 1.4±0.6 κ-casein Not detected

[0076] This indicates that β-casein can be concentrated from other caseins and whey proteins, increasing the ratio of αS1-casein, αS2-casein, β-casein, and κ-casein to 1:0:12:0. Figure 3 In this study, the average protein particle size density (PSD) was measured using dynamic light scattering of β-casein, revealing a PSD of approximately 6 nm. This confirms that β-casein is in monomeric form, while sodium caseinate exhibits some aggregates, and the micellar casein concentrate remains in its intact micellar form.

[0077] Example 2

[0078] Surface tension of β-casein-containing solutions

[0079] The decrease in surface tension of the solution was measured. The solution was diluted 10-fold to assess its ability to reduce the interfacial tension between air and water, and between oil and water. Figure 4 It is clear that the higher purity β-casein sample reduced surface tension to a greater extent than sodium caseinate and casein in micelle form.

[0080] Example 3

[0081] Emulsion containing solution prepared with β-casein

[0082] A three-component oil-in-water emulsion (oil, water, and protein) was prepared using 20% ​​rapeseed oil and 1% protein (w / w) processed at room temperature and homogenized at 2500 psi (stage 1) and 500 psi (stage 2). Sodium caseinate (NaCas) was used instead of β-casein as a control. The particle size of the finished product was measured using a mastersizer, and foaming properties were studied using a planetary mixer.

[0083] Table 2. Average PSD of simple emulsions measured by Mastersizer

[0084] sample Dx(10)(μm) Dx(50)(μm) Dx(90)(μm) D[4,3](μm) Span (90, 10) Comparison - NaCas 0.0445 0.414 2.56 1.0715 6.0725 BCN 100% Replacement 0.0836 0.484 2.29 0.91 4.558

[0085] The foaming properties of the samples were analyzed, and the results are shown in... Figure 6 The samples were aerated using a kitchen-assisted mixing device. The sample containing β-casein exhibited better foaming and foam stability compared to the sample containing sodium caseinate.

[0086] Example 4

[0087] Foaming ability of β-casein-containing solutions

[0088] To understand the functionality of β-casein-rich solutions compared to control sodium caseinate solutions, the foaming ability of 0.25% protein solutions was tested. Both proteins foamed rapidly, but the foam stability of the β-casein solution was significantly higher than that of sodium caseinate. Figure 5 This is reflected in the fact that the foam height decays much longer than that of sodium caseinate, which collapsed within 10 minutes of the start of the test.

[0089] Example 5

[0090] Whipped topping emulsion containing β-casein

[0091] A composite emulsion containing multiple components was prepared to simulate commercially available aerated / stirred toppings.

[0092] Table 3. Formulations with 100% replacement of stirred toppings

[0093]

[0094] Table 4. Average PSD of Gold Medal Liquid Toppings Containing Sodium Caseinate and β-Casein

[0095] sample Dx(10)(μm) Dx(50)(μm) Dx(90)(μm) D[4,3](μm) Span (90, 10) Comparison with NaCas 0.0449 0.220 0.877 2.14 3.784 BCN 100% Replacement 0.0943 0.289 0.691 0.350 2.066

[0096] Table 5. Whipping results using a KitchenAid mixer

[0097]

[0098]

[0099] Example 6

[0100] Whipped topping emulsion containing reduced β-casein

[0101] Given the excellent results of replacing sodium caseinate with β-casein 1:1 in the application of the whipped topping, protein reduction was also evaluated.

[0102] Table 6. Formulations for whipped toppings with reduced protein content

[0103]

[0104] These results demonstrate that adding less β-casein can achieve product characteristics and performance similar to the control. Similar PSD results shown in Table 7 confirm this. Whipping properties were also improved, with lower product viscosity, slightly higher whipping time, but longer rosette formation time and stability on cakes (Table 8).

[0105] Table 7. PSD of Gold Medal Liquid Topping Products Made with Reduced β-Casein Content.

[0106]

[0107] Table 8. The results of beating with a 660g liquid topping on a Hobart mixer at speed 2.

[0108]

[0109] Example 7

[0110] Sodium caseinate emulsion containing β-casein

[0111] β-casein was added to sodium caseinate to vary the ratio of β-casein to total casein. Typically, β-casein comprises 33% to 37% of total casein. Various ratios of β-casein formulations were examined. In the following examples, the β-casein content was increased from 37% to 50%, 65%, 75%, and 90% by mixing different levels of β-casein solution with sodium caseinate or β-casein solution alone, while keeping the total protein content of all formulations the same. Emulsions were prepared using 20% ​​rapeseed oil and 1% protein in a two-stage homogenizer at 2500 / 500 psi pressure. Table 9 shows that increasing the β-casein content of sodium caseinate can result in excellent emulsion performance.

[0112] Table 9. Average PSD of simple emulsions of sodium caseinate and β-casein mixture.

[0113] sample Dx(10)(μm) Dx(50)(μm) Dx(90)(μm) D[4,3](μm) 100% NaCas 0.0476 0.456 2.86 1.04 75% NaCas 25% BCN 0.0495 0.392 1.93 0.747 50% NaCas / 50% BCN 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

[0114] Example 8

[0115] Sodium caseinate emulsion with whipped topping containing β-casein

[0116] In another embodiment, β-casein is added to sodium caseinate to alter the ratio of β-casein to total casein content, and this is applied to a whipped topping product. In the following embodiment, the β-casein content is increased to 50% and 55% by mixing β-casein extract and sodium caseinate.

[0117] Table 10. Formulation of sodium caseinate product with added β-casein as a whipped topping.

[0118]

[0119] Table 11. Average PSD values ​​of the stirred topping samples prepared with spiked sodium caseinate / β-casein.

[0120]

[0121] Example 9

[0122] Non-whipped coffee creamer containing β-casein

[0123] In another embodiment, β-casein was incorporated into non-whipped low-fat and high-fat coffee creamer formulations using non-hydrogenated vegetable fats and milk fats, respectively. Different sugar contents and different supporting emulsifiers were also used, including polysorbate-60 and monoglycerides and diglycerides of fatty acids. Salts such as sodium chloride and dipotassium phosphate were included for flavoring and to prevent feathering. Table 12 shows the formulations subjected to downstream heat treatment and homogenization at 2500 / 500 psi pressure in a two-stage homogenizer. Table 13 shows the properties of the resulting emulsions, indicating low viscosity and small particle size obtained after processing and refrigeration. The resulting products (i.e., samples C and D) exhibited good stability in coffee with no visible feathering.

[0124] Table 12: Formulas for non-whipped coffee creamer products containing β-casein.

[0125]

[0126]

[0127] Table 13. Average particle size, liquid separation and viscosity of coffee creamer.

[0128]

[0129] Example 10

[0130] Sodium caseinate emulsion with whipped topping containing β-casein

[0131] In another embodiment, β-casein is incorporated into various whippable low-fat, medium-fat, and high-fat toppings, frostings, and soft foam formulations. In these formulations, various oils are used in concentration ranges, not limited to hydrogenated vegetable fats from palm kernels and coconut oil. Sweeteners, such as corn syrup (HFCS 42, 43 / 43, 36DE), glucose, granulated sugar, and lactose, are included to achieve a total sweetener content of 16% to 60%. Many different emulsifiers have shown compatibility with β-casein, such as soy lecithin, distilled monoacylglycerol, polysorbate-60, soy protein concentrate, sodium stearoyl lactylate, polyglycerol esters of fatty acids, and dehydrated sorbitan monostearate. Various stabilizers are used to improve product stability, including sodium alginate, hydroxypropyl methylcellulose, xanthan gum, guar gum, locust bean gum, corn starch, and carrageenan. Other dairy ingredients, such as cream powder and buttermilk powder, may also be used to improve the dairy flavor characteristics 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 beaten products is shown in... Figure 8 . Figure 8The initial rosettes dispensed from a standard pastry bag with star-shaped tips after whipping are shown. Stability bowls containing samples chilled for 24 hours (i.e., from about 2°C to about 4°C) are shown. Figure 9 . Figure 9 The product appearance is shown after 150g of the product was placed in a deli container and stored in the refrigerator. A small amount was scooped from the cup with a spoon to show the internal foam structure and stability of the whipped cream.

[0132] Table 14. Recipes for whippable toppings, frostings, and foams containing β-casein.

[0133]

[0134] Table 15. Emulsion properties and whipping performance of toppings, frostings and foams after these emulsions have undergone freezing and thawing at refrigeration temperatures.

[0135]

[0136] ***

[0137] The foregoing description of the specific aspects so fully reveals the general nature of the invention that others, by applying knowledge within the art, can easily modify and / or adapt various applications of such specific aspects without excessive experimentation or departing from the general conception of this disclosure. Therefore, based on the teachings and guidance given herein, such adaptations and modifications are intended to fall within the meaning and scope of equivalents of the disclosed aspects. It should be understood that the wording or terminology used herein is for descriptive rather than restrictive purposes, and that the terminology or terminology of this specification will be interpreted by those skilled in the art in light of the teachings and guidance.

[0138] The breadth and scope of this disclosure should not be limited by any of the exemplary aspects described above, but should be defined solely by the following claims and their equivalents.

[0139] All publications, patents, patent applications and / or other documents cited in this application are incorporated by reference in their entirety for all purposes as if each individual publication, patent, patent application and / or other document were individually incorporated by reference for all purposes.

[0140] For the sake of completeness, various aspects of the present invention are set forth in the following numbered clauses:

[0141] Clause 1. An emulsion composition comprising fat and protein, wherein, based on the total amount of casein present in the composition, the protein comprises more than 45% by weight β-casein.

[0142] Clause 2. The composition according to Clause 1, wherein the composition comprises: about 5% to about 45% by weight of the fat; about 0.001% to about 3% by weight of the protein; about 0% to about 55% by weight of a sweetener; about 0% to about 3% by weight of one or more stabilizers; about 0.0001% to about 2% by weight of a buffer salt; and about 0% to about 3% by weight of one or more emulsifiers.

[0143] Clause 3. The composition according to Clause 1 or Clause 2, wherein the composition comprises: about 5% to about 35% by weight of the fat; about 1% to about 2.5% by weight of the protein; about 5% to about 45% by weight of a sweetener; about 0.5% to about 3% by weight of one or more stabilizers; about 0.5% to about 2% by weight of a buffer salt; and about 0.5% to about 3% by weight of one or more emulsifiers.

[0144] Clause 4. The composition according to any one of Clauses 1 to 3, wherein the fat is milk fat; vegetable fat; vegetable oil; algal oil; fermented oil derived from bacteria, yeast or mold; hydrogenated oil; hydrogenated and transesterified oil; hydrogenated, blended and transesterified oil; medium-chain triglyceride (MCT) vegetable oil; milk fat; ghee; anhydrous milk fat; butter; or combinations thereof.

[0145] Clause 5. The composition according to any one of Clauses 1 to 4, wherein the protein is an animal protein, a recombinant milk protein, a plant-based protein, or a combination thereof.

[0146] Clause 6. The composition according to any one of Clauses 1 to 5, wherein the protein is natural casein, recombinant casein, or a combination thereof.

[0147] Clause 7. The composition according to any one of Clauses 1 to 6, wherein, based on the total composition, the composition contains less than 0.03% by weight of total κ-casein.

[0148] Clause 8. The composition according to any one of Clauses 1 to 7, wherein the protein is enriched with animal and / or recombinant β-casein.

[0149] Clause 9. The composition according to any one of Clauses 1 to 8, wherein the β-casein is natural or recombinant.

[0150] Clause 10. The composition according to Clause 9, wherein the β-casein is recombinant and comprises about 60% to about 100% of the same amino acid sequence as that of a mammalian milk protein such as bovine milk protein, sheep milk protein, camel milk protein, yak milk protein, buffalo milk protein, mare milk protein or goat milk protein.

[0151] Clause 11. The composition according to any one of Clauses 1 to 10, wherein the proportion of β-casein is about 45% to about 100% of the total amount of casein in the composition.

[0152] Clause 12. The composition according to any one of Clauses 1 to 11, wherein the β-casein is in micelle or monomeric form; wherein when the β-casein is in monomeric form, the β-casein has a protein particle size of less than 50 nm.

[0153] Clause 13. The composition according to any one of Clauses 1 to 11, wherein the β-casein is in micelle or monomeric form; wherein when the β-casein is in micelle form, the β-casein has a protein particle size of less than 500 nm.

[0154] Clause 14. The composition according to any one of Clauses 1 to 13, wherein the β-casein has a zeta potential of about -50 mV to about -15 mV in a pH 7.0 buffer.

[0155] Clause 15. The composition according to any one of Clauses 1 to 14, wherein the protein is in liquid or powder form, wherein the powder form is produced by spray drying, roller drying, tumble drying or freeze drying of the protein to remove water.

[0156] Clause 16. The composition according to any one of Clauses 1 to 15, wherein the protein is a single type of natural milk protein, a single type of recombinant milk protein, or a combination thereof.

[0157] Clause 17. The composition according to Clause 16, wherein the single type of protein is β-casein.

[0158] Clause 18. The composition according to any one of Clauses 1 to 17, wherein the protein is two or more different types of animal milk protein, recombinant milk protein and plant-based protein.

[0159] Clause 19. The composition according to any one of Clauses 1 to 18, wherein the protein has or does not have post-translational modifications.

[0160] Clause 20. The composition according to Clause 19, wherein the post-translational modification is one or more of glycosylation and phosphorylation.

[0161] Clause 21. The composition according to any one of Clauses 1 to 18, wherein the protein is phosphorylated.

[0162] Clause 22. The composition according to any one of Clauses 1 to 18, wherein the protein comprises non-natural phosphorylation.

[0163] Clause 23. The composition according to any one of Clauses 6 to 22, wherein the recombinant casein is produced by fungal cells, yeast cells, bacterial cells, algae or by a transgenic method.

[0164] Clause 24. The composition according to any one of Clauses 2 to 23, wherein the sweetener is a nutritional sweetener, a non-nutritive sweetener, or a combination thereof.

[0165] Clause 25. The composition according to Clause 24, wherein the nutritional 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, syrup; soluble / insoluble fiber derived from corn, wheat, peas, rice, oats, coconut, barley and / or cassava; fructooligosaccharides and galactooligosaccharides; and hydrolyzed cereal powder; or combinations thereof.

[0166] Clause 26. The composition according to Clause 24, wherein the non-nutritive sweetener is sucralose; aspartame; saccharin; stevia; monk fruit extract; neotame; advansame; acetylsupan potassium; sugar alcohols such as maltitol, xylitol, sorbitol, erythritol, mannitol, isomaltitol, lactitol; hydrogenated starch hydrolysate; or one or more combinations thereof.

[0167] Clause 27. The composition according to Clause 24, wherein the sweetener is one or more of brassinolide, curculigolide, areca nut, mirabilite, monetin, pentadiene, and somatin.

[0168] Clause 28. The composition according to any one of Clauses 1 to 27, wherein the fat comprises one or more lipids derived from plants, animals; one or more lipids derived from milk; or a combination thereof.

[0169] Clause 29. The composition according to any one of Clauses 1 to 28, wherein the fat comprises one or more monoglycerides, diglycerides, triglycerides and / or phospholipids, comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid and capric acid.

[0170] Clause 30. The composition according to Clause 29, wherein said one or more monoglycerides, diglycerides, triglycerides and / or phospholipids are plant-based transesterified monoglycerides, diglycerides, triglycerides and / or phospholipids comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid and decanoic acid.

[0171] Clause 31. The composition according to any one of Clauses 1 to 30, wherein the fat is a hydrogenated oil; an exchanged oil; a hydrogenated and exchanged oil; a hydrogenated, blended and exchanged oil; or a combination thereof.

[0172] Clause 32. The composition according to Clause 29, wherein the one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprise fatty acyl chains in a percentage similar to the percentage of fatty acyl chains found in mammalian-derived milk or dairy products.

[0173] Clause 33. The composition according to any one of Clauses 1 to 32, wherein the composition is whippable.

[0174] Clause 34. The composition according to any one of Clauses 1 to 32, wherein the composition is non-whisking.

[0175] Clause 35. The composition described in Clause 34, wherein the composition is cooking cream or coffee creamer.

[0176] Clause 36. The composition according to any one of Clauses 1 to 35, wherein the fat is fully hydrogenated, partially hydrogenated, transesterified, non-hydrogenated, or hydrogenated and transesterified.

[0177] Clause 37. The composition according to any one of Clauses 1 to 36, wherein the fat is fully hydrogenated.

[0178] Clause 38. The composition according to any one of Clauses 1 to 37, wherein the composition further comprises a crystallizing agent, a flavoring agent, a salt, a preservative, or a combination thereof.

[0179] Clause 39. The composition according to any one of Clauses 1 to 38, wherein the protein is one or more of monomeric casein, sodium caseinate, calcium caseinate, potassium caseinate, acidic casein, rennet casein, micelles, and globular proteins.

[0180] Clause 40. The composition according to Clause 39, wherein the globular protein is one or more of milk protein, plant protein, α-lactalbumin, β-lactoglobulin, ovalbumin, ovoglobulin and recombinant protein.

[0181] Clause 41. The composition according to Clause 39, wherein the micelle protein is micelle casein, recombinant micelle casein, or a combination thereof.

[0182] Clause 42. The composition according to Clause 40, wherein the plant protein is any grain, legume, or seed-based protein and is present in an amount of about 0.05% by weight to about 2.5% by weight.

[0183] Clause 43. The composition according to Clause 41, wherein the micelle 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.

[0184] Clause 44. The composition according to any one of Clauses 2 to 43, wherein the stabilizer is an alginate; carrageenan; guar gum; cellulose such as methylcellulose, microcrystalline cellulose, carboxymethyl cellulose, hydroxypropyl methylcellulose (HPMC); sorbitol; xanthan gum; tara gum; locust bean gum; gellan gum (such as high acyl, low acyl); beet pectin; skim milk powder; whole milk powder; partially skim milk powder; butter milk powder; dairy solids; modified starch; agar; gelatin; gum arabic; konjac; pectin; maltodextrin and astragalus gum, or more thereof.

[0185] Clause 45. The composition according to any one of Clauses 2-43, wherein the emulsifier is one or more of the following: diacetyl tartrate of monoglyceride and / or diglyceride, lactate of monoglyceride and / or diglyceride, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyethylene glycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose ester, sucrose monostearate, monoglyceride, beeswax, carmobar wax, candelilla wax, plant wax, fruit wax, animal wax, polyglycerol fatty acid ester, and polyglycerol ricinoleate (PGPR).

[0186] Clause 46. The composition according to any one of Clauses 2 to 43, wherein the buffer salt is one or more of any sodium or potassium or calcium salt of citrate, phosphate, carbonate and halide, such as sodium polyphosphate, orthophosphate, pyrophosphate, hexametaphosphate, monophosphate or diphosphate, monocarbonate or dicarbonate.

[0187] Clause 47. A food product comprising any one of the compositions pursuant to Clauses 1 to 46.

[0188] Clause 48. Food products as described in Clause 47, wherein the food product is a dairy product, a product of non-animal origin, a beverage product, or a combination thereof.

[0189] Clause 49. Food products as described in Clause 47 or Clause 48, wherein said food products are coffee creamer, cooking cream, whipped cream or similar low- to high-fat emulsions.

[0190] Clause 50. A food product pursuant to any one of Clauses 47 to 49, wherein the food product comprises about 0.001% by weight to about 3% by weight of the protein.

[0191] Clause 51. A method of manufacturing a composition according to any one of Clauses 1 to 46, the method comprising: forming an oil phase comprising fats; forming an aqueous phase comprising proteins; 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 to about 50°C to about 145°C; and cooling the emulsion to about 2°C to about 30°C.

[0192] Clause 52. The method according to Clause 51, wherein the method further comprises packaging the emulsion under aseptic or non-aseptic conditions.

[0193] Clause 53. The method according to Clause 51 or Clause 52, wherein the method further comprises storing the emulsion at about -18°C to about -15°C, about 3°C ​​to about 5°C, or about 18°C ​​to about 25°C.

[0194] Clause 54. The method according to any one of Clauses 51 to 53, wherein the aqueous phase further comprises a stabilizer, an emulsifier, and a buffer salt.

[0195] Clause 55. The method according to any one of Clauses 51 to 54, wherein the method further comprises aerating the emulsion or storing the emulsion statically.

[0196] Clause 56. The method described in Clause 55, wherein aeration includes stirring, mixing using a planetary mixer or beating using a continuous beater.

[0197] Clause 57. The method according to any one of Clauses 51 to 56, wherein the method further comprises heat-treating, pasteurizing or sterilizing the emulsion.

[0198] Clause 58. The method according to Clause 57, wherein the heat treatment, pasteurization or sterilization includes boiling, high hydrostatic pressure, ultraviolet radiation, irradiation or ultra-high temperature treatment.

[0199] Clause 59. The method according to any one of Clauses 51 to 58, wherein the emulsion has improved storage stability compared to the corresponding emulsion.

[0200] Clause 60. A method for preparing a whipped emulsion, the method comprising whipping an emulsion according to any one of Clauses 51 to 59, wherein the whipping is performed at about 2°C to about 8°C.

Claims

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

2. The composition according to claim 1, wherein the composition comprises: The fat comprises about 5% by weight to about 45% by weight; The protein, in amounts from about 0.001% by weight to about 3% by weight; From about 0% by weight to about 55% by weight of sweetener; One or more stabilizers, from about 0% by weight to about 3% by weight; Buffer salts of about 0.0001% by weight to about 2% by weight; and One or more emulsifiers, from about 0% to about 3% by weight.

3. The composition according to claim 1 or claim 2, wherein the composition comprises: The fat comprises about 5% by weight to about 35% by weight; The protein, approximately 1% by weight to approximately 2.5% by weight; From about 5% by weight to about 45% by weight of sweetener; One or more stabilizers, ranging from about 0.5% by weight to about 3% by weight; Buffer salts of about 0.5% by weight to about 2% by weight; and One or more emulsifiers, ranging from about 0.5% by weight to about 3% by weight.

4. The composition according to any one of claims 1 to 3, wherein the fat is milk fat; vegetable fat; vegetable oil; algal oil; fermented oil derived from bacteria, yeast or mold; hydrogenated oil; hydrogenated and transesterified oil; hydrogenated, blended and transesterified oil; medium-chain triglyceride (MCT) vegetable oil; milk fat; ghee; anhydrous milk fat; butter; or combinations thereof.

5. The composition according to any one of claims 1 to 4, wherein the protein is an animal protein, a recombinant milk protein, a plant-based protein, or a combination thereof.

6. The composition according to any one of claims 1 to 5, wherein the protein is natural casein, recombinant casein, or a combination thereof.

7. The composition according to any one of claims 1 to 6, wherein, based on the total composition, the composition contains less than 0.03% by weight of total κ-casein.

8. The composition according to any one of claims 1 to 7, wherein the protein is enriched with animal and / or recombinant β-casein.

9. The composition according to any one of claims 1 to 8, wherein the β-casein is natural or recombinant.

10. The composition of claim 9, wherein the β-casein is recombinant and comprises about 60% to about 100% of the same amino acid sequence as that of mammalian milk proteins such as bovine milk protein, sheep milk protein, camel milk protein, yak milk protein, buffalo milk protein, horse milk protein, or goat milk protein.

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

12. The composition according to any one of claims 1 to 11, wherein the β-casein is in micelle or monomeric form; When the β-casein is in monomeric form, the β-casein has a protein particle size of less than 50 nm.

13. The composition according to any one of claims 1 to 11, wherein the β-casein is in micelle or monomeric form; When the β-casein is in micelle form, the β-casein has a protein particle size of less than 500 nm.

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

15. The composition according to any one of claims 1 to 14, wherein the protein is in liquid or powder form, wherein the powder form is produced by spray drying, roller drying, tumble drying or freeze drying of the protein to remove water.

16. The composition according to any one of claims 1 to 15, wherein the protein is a single type of natural milk protein, a single type of recombinant milk protein, or a combination thereof.

17. The composition of claim 16, wherein the single type of protein is β-casein.

18. The composition according to any one of claims 1 to 17, wherein the protein is two or more different types of animal milk protein, recombinant milk protein and plant-based protein.

19. The composition according to any one of claims 1 to 18, wherein the protein has or does not have post-translational modifications.

20. The composition of claim 19, wherein the post-translational modification is one or more of glycosylation and phosphorylation.

21. The composition according to any one of claims 1 to 18, wherein the protein is phosphorylated.

22. The composition according to any one of claims 1 to 18, wherein the protein comprises non-natural phosphorylation.

23. The composition according to any one of claims 6 to 22, wherein the recombinant casein is produced by fungal cells, yeast cells, bacterial cells, algae or transgenic methods.

24. The composition according to any one of claims 2 to 23, wherein the sweetener is a nutritional sweetener, a non-nutritive sweetener, or a combination thereof.

25. The composition of claim 24, wherein the nutritional 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, syrup; soluble / insoluble fiber derived from corn, wheat, peas, rice, oats, coconut, barley and / or cassava; fructooligosaccharides and galactooligosaccharides; and hydrolyzed cereal powder; or combinations thereof.

26. The composition of claim 24, wherein the non-nutritive sweetener is sucralose; aspartame; saccharin; stevia; monk fruit extract; neotame; advansame; acetylsupan potassium; sugar alcohols such as maltitol, xylitol, sorbitol, erythritol, mannitol, isomaltitol, lactitol; hydrogenated starch hydrolysate; or one or more combinations thereof.

27. The composition according to claim 24, wherein the sweetener is one or more of brassinolide, curculigolide, areca nut, mirabilite, monetin, pentadiene, and sematinine.

28. The composition according to any one of claims 1 to 27, wherein the fat comprises one or more lipids derived from plants, animals; one or more lipids derived from milk; or a combination thereof.

29. The composition according to any one of claims 1 to 28, wherein the fat comprises one or more monoglycerides, diglycerides, triglycerides and / or phospholipids, comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid and capric acid.

30. The composition of claim 29, wherein the one or more monoglycerides, diglycerides, triglycerides and / or phospholipids are plant-based transesterified monoglycerides, diglycerides, triglycerides and / or phospholipids comprising short-chain fatty acids selected from the group consisting of butyric acid, hexanoic acid, caprylic acid and decanoic acid.

31. The composition according to any one of claims 1 to 30, wherein the fat is a hydrogenated oil; an exchanged oil; a hydrogenated and exchanged oil; a hydrogenated, blended and exchanged oil; or a combination thereof.

32. The composition of claim 29, wherein the one or more monoglycerides, diglycerides, triglycerides and / or phospholipids comprise fatty acyl chains in a percentage similar to the percentage of fatty acyl chains found in mammalian-derived milk or dairy products.

33. The composition according to any one of claims 1 to 32, wherein the composition is whippable.

34. The composition according to any one of claims 1 to 32, wherein the composition is non-whisking.

35. The composition of claim 34, wherein the composition is cooking cream or coffee creamer.

36. The composition according to any one of claims 1 to 35, wherein the fat is fully hydrogenated, partially hydrogenated, transesterified, non-hydrogenated, or hydrogenated and transesterified.

37. The composition according to any one of claims 1 to 36, wherein the fat is fully hydrogenated.

38. The composition according to any one of claims 1 to 37, wherein the composition further comprises a crystallizing agent, a flavoring agent, a salt, a preservative, or a combination thereof.

39. The composition according to any one of claims 1 to 38, wherein the protein is one or more of monomeric casein, sodium caseinate, calcium caseinate, potassium caseinate, acidic casein, rennet casein, micelles, and globular proteins.

40. The composition of claim 39, wherein the globular protein is one or more of milk-derived proteins, plant proteins, α-lactalbumin, β-lactoglobulin, ovalbumin, ovoglobulin, and recombinant proteins.

41. The composition of claim 39, wherein the micelle protein is micelle casein, recombinant micelle casein, or a combination thereof.

42. The composition of claim 40, wherein the plant protein is any cereal, legume, or seed-based protein and is present in an amount of about 0.05% by weight to about 2.5% by weight.

43. The composition of claim 41, wherein the micelle 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. The composition according to any one of claims 2 to 43, wherein the stabilizer is one or more of alginate; carrageenan; guar gum; cellulose such as methylcellulose, microcrystalline cellulose, carboxymethyl cellulose, hydroxypropyl methylcellulose (HPMC); sorbitol; xanthan gum; tara gum; locust bean gum; gellan gum (such as high acyl, low acyl); beet pectin; skim milk powder; whole milk powder; partially skim milk powder; butter milk powder; dairy solids; modified starch; agar; gelatin; gum arabic; konjac; pectin; maltodextrin and astragalus gum.

45. The composition according to any one of claims 2 to 43, wherein the emulsifier is one or more of the following: diacetyl tartrate of monoglyceride and / or diglyceride, lactate of monoglyceride and / or diglyceride, sodium stearoyl lactylate, lecithin, sorbitan monostearate, polyethylene glycol ester, propylene glycol monostearate, polysorbate, polysorbate 60, polysorbate 80, sucrose ester, sucrose monostearate, monoglyceride, beeswax, carmobar wax, candelilla wax, plant wax, fruit wax, animal wax, polyglycerol fatty acid ester, and polyglycerol ricinoleate (PGPR).

46. ​​The composition according to any one of claims 2 to 43, wherein the buffer salt is one or more of any sodium, potassium, or calcium salt of citrate, phosphate, carbonate, and halide, such as sodium polyphosphate, orthophosphate, pyrophosphate, hexametaphosphate, monophosphate, or diphosphate, monocarbonate, or dicarbonate.

47. A food product comprising the composition according to any one of claims 1 to 46.

48. The food product of claim 47, wherein the food product is a dairy product, a non-animal product, a beverage product, or a combination thereof.

49. The food product according to claim 47 or claim 48, wherein the food product is coffee creamer, cooking cream, whipped cream or similar low- to high-fat emulsions.

50. The food product according to any one of claims 47 to 49, wherein the food product comprises about 0.001% by weight to about 3% by weight of the protein.

51. A method for manufacturing a composition according to any one of claims 1 to 46, the method comprising: It forms an oil phase containing fats; Formation of an aqueous phase containing proteins; The oil phase and the aqueous phase are adjusted from about 15°C to about 75°C; The oil phase and the aqueous phase are mixed to form a mixture; The mixture is homogenized to form an emulsion; The emulsion is heated to approximately 50°C to approximately 145°C; and The emulsion is cooled to about 2°C to about 30°C.

52. The method of claim 51, wherein the method further comprises packaging the emulsion under aseptic or non-aseptic conditions.

53. The method of claim 51 or claim 52, wherein the method further comprises storing the emulsion at about -18°C to about -15°C, about 3°C ​​to about 5°C, or about 18°C ​​to about 25°C.

54. The method according to any one of claims 51 to 53, wherein the aqueous phase further comprises a stabilizer, an emulsifier, and a buffer salt.

55. The method according to any one of claims 51 to 54, wherein the method further comprises aerating the emulsion or storing the emulsion statically.

56. The method of claim 55, wherein aeration comprises stirring, mixing using a planetary mixer, or beating using a continuous mixer.

57. The method according to any one of claims 51 to 56, wherein the method further comprises heat-treating, pasteurizing or sterilizing the emulsion.

58. The method of claim 57, wherein the heat treatment, pasteurization or sterilization includes boiling, high hydrostatic pressure, ultraviolet radiation, irradiation or ultra-high temperature treatment.

59. The method according to any one of claims 51 to 58, wherein the emulsion has improved storage stability compared to the corresponding emulsion.

60. A method for preparing a whipped emulsion, the method comprising whipping the emulsion according to any one of claims 51 to 59, wherein the whipping is performed at about 2°C to about 8°C.