Emulsions and methods for their preparation

Abstract

The present invention relates to a method for producing an emulsion using a plant-derived protein hydrogel slurry. The present invention also relates to the emulsion itself and to compositions comprising the emulsion. The present invention also relates to the use of the plant-derived protein hydrogel slurry as an emulsifier.

Description

[Technical field]

[0001] The present invention relates to a method for producing an emulsion using a plant-derived protein hydrogel slurry. The present invention also relates to the emulsion itself and to compositions comprising the emulsion. The present invention also relates to the use of the plant-derived protein hydrogel slurry as an emulsifier. [Background technology]

[0002] In many consumer product applications, for example in cosmetic formulations such as skin creams, poorly water-soluble active ingredients need to be solubilized in water. Amphiphilic molecules can be used as emulsifiers to create oil-in-water emulsions that solubilize the actives and provide some stability to the formulation (i.e., to prevent the consumer product from separating / decomposing as soon as it is produced). Traditional amphiphilic emulsifiers are essentially thermodynamically unstable and do not provide sufficient emulsion stability over very long periods of time. Materials derived from fossil fuels are also commonly used as emulsifiers, but there is an increasing desire to use more sustainable materials. Unfortunately, many materials of natural origin that can be used for this purpose are highly processed, which creates a new set of problems. For example, many such emulsifiers have foaming properties that are not suitable for non-cleansing products, or are unpleasant to use in the sense that they are sticky when applied topically.

[0003] More recently, plant proteins have been studied for their emulsifying properties.However, traditional plant protein emulsifiers are relatively poor emulsifiers, which require high levels in the formulation to successfully solubilize poorly water-soluble materials.Traditional plant protein emulsifiers also tend to have high levels of soluble protein, which is likely to lead to allergic reactions.Therefore, the high levels of potentially allergenic soluble plant protein in such formulations limit the use of these materials.For example, such materials cannot be used in formulations intended for topical application or edible formulations, because the risk of allergic reactions is too high.

[0004] Therefore, there is a need to formulate new emulsifiers that are sustainable and capable of forming emulsions with low or negligible allergenicity risk and long-term stability. Summary of the Invention

[0005] Viewed from a first aspect, the present invention provides a method for the preparation of an emulsion, the method comprising the steps of: (a) forming a solution comprising one or more plant-derived proteins in a solvent system, the solvent system comprising miscible co-solvents, a first co-solvent increasing the solubility of the plant-derived proteins and a second co-solvent decreasing the solubility of the plant-derived proteins; (b) inducing the protein in the solution to undergo a sol-gel transition to form a plant-derived protein hydrogel; (c) subjecting the plant-derived protein hydrogel to a first shear step to form a first plant-derived protein hydrogel slurry; (d) subjecting the first plant-derived protein hydrogel slurry to a solvent reduction step to form a washed plant-derived protein hydrogel slurry; (e) subjecting the washed plant-derived protein hydrogel slurry to a second shear step to form a second plant-derived protein hydrogel slurry; (f) dispersing a lipophilic phase in the second plant-derived protein hydrogel slurry to form an emulsion; forming an emulsion having less than 1% protein solids by weight, based on the total weight of the emulsion.

[0006] Viewed from a further aspect, the present invention provides an emulsion obtained or obtainable by the process described above.

[0007] Viewed from a further aspect, the present invention provides an emulsion comprising a lipophilic phase dispersed in a plant-derived protein hydrogel slurry comprising a plant-derived protein, the emulsion having less than 1 wt. % protein solids based on the total weight of the emulsion.

[0008] Viewed from a further aspect, the present invention provides a composition comprising an emulsion prepared according to the above method.

[0009] Viewed from a further aspect, the present invention provides the use of a plant-derived protein hydrogel slurry as an emulsifier in a composition.

[0010] definition As used herein, the term "lower shear process" may refer to a process step in which low levels of mechanical energy are applied to a material, preferably by a cutting action, to break or fragment it primarily into large separate fragments. "Low shear" typically refers to high velocity impacts, e.g., less than 2 ms -1 The low shear process does not include any comminution process that crushes or fragments a material by impact with a velocity difference exceeding 1 mm. It also typically does not include cavitation-based milling processes. In certain embodiments, during the low shear process, the hydrogel is fragmented to obtain fragments such that at least 80% by weight of the hydrogel fragments have a maximum dimension of between 1 mm and 100 mm as measured by optical microscopy.

[0011] As used herein, the term "higher shear step" may refer to a process step in which energy is applied to reduce a hydrogel into small fragments, such as to form a colloidal dispersion. In certain embodiments, during the higher shear step, the hydrogel is fragmented to a size of less than 100 microns d as measured by laser diffraction. 50 It may give fragments having a particle size.

[0012] For the avoidance of doubt, the high shear step subjects the hydrogel to a higher level of shear than the low shear step. If the process involves both a low shear step and a high shear step, the high shear step must occur after the low shear step (i.e., they are separate steps occurring in this particular order).

[0013] As used herein, the term "sol-gel transition temperature" refers to the temperature at which the plant-derived protein transforms from a liquid state to a hydrogel state. Thus, at temperatures above the sol-gel transition temperature, the plant-derived protein is in a liquid state, and at temperatures below the sol-gel transition temperature, the plant-derived protein is in a hydrogel state.

[0014] As used herein, "fragrance" (used interchangeably with the term "perfume") refers to an ingredient of a formulation that can impart or modify the odor of a product, such as a body lotion or hair conditioner, or the odor of a substrate, such as skin or hair. Fragrances are typically used to impart an overall pleasant odor or odor profile to a product to provide a pleasant experience, e.g., fine fragrances, or to provide sensory cues regarding the benefits and functionality of the product, e.g., the calming effect of a lavender sleep aid, the idea of ​​cleanliness in laundry products, or to mask unpleasant odors, as in insect repellent products. A "fragrance" can be composed of one or more ingredients, which can be a single chemical, referred to herein as a "fragrance material" (used interchangeably with the term "perfume material"), or a mixture of different "fragrance materials". Fragrance materials can be created by synthetic processes or extracted from nature, especially plants, to obtain naturally occurring plant essential oils and plant extracts, e.g., orange oil. Fragrance materials created by synthetic processes can be either entirely new chemicals or nature-identical fragrance materials. The synthetic and naturally derived fragrance materials can then be blended into fragrances by skilled perfumers (also called noses) for use in consumer products. Fragrance materials can be obtained from specialized fragrance suppliers known as fragrance houses as individual chemicals, natural blends, or as proprietary specialty blends whose complete composition is not disclosed.Individual fragrance materials, including known natural blends, can be found by consulting journals commonly used by those skilled in the art, such as "Perfume and Flavourist" or "Journal of Essential Oil Research", or journals listed in reference books such as S. Arctander Perfume and Flavor Chemicals, 1969, Montclair, New Jersey, USA, and more recently republished by Allured Publishing Corporation Illinois (1994) and "Perfume and Flavour Materials of Natural Origin", S. Arctander, Ed., Elizabeth, NJ, 1960. For the purposes of the present invention, "fragrance material" will be understood to include profragrances, such as acetal profragrances, ketal profragrances, ester profragrances, hydrolyzable inorganic-organic profragrances, and combinations thereof. The fragrance material may be released from the profragrances in any number of ways, for example, by hydrolysis, or by a shift in an equilibrium reaction, or by a pH change, or by enzyme release, or by UV radiation.

[0015] Fragrance materials can be described in terms of their odor intensity, detection threshold, odor saturation, and their characteristics. In fragrance encapsulations, it is preferable to use fragrance materials with low odor detection thresholds and high intensity so as to maximize detectability even with small levels of encapsulated and released fragrance.

[0016] To impart an odor, fragrance materials must be volatile, even if only to a small extent, because they must be airborne and enter the nose where they attach to specific neuroreceptors and trigger signals within the olfactory system. Fragrance materials can be classified according to their volatility. Preferably, fragrance materials are liquid at 20° C. and atmospheric pressure, but in some cases they may be solid and can be blended with other liquid fragrance materials or solvents. Typically, the fragrance industry refers to volatility and persistence by broadly classifying materials into one of three categories: base notes, which are the least volatile and most persistent; heart notes, which are medium volatile and persistent; and top notes, which are the most volatile and least persistent. This is based on the perception of the odor of the material and is entirely subjective. One way to objectively classify the volatility of fragrance materials is by their vapor pressure.

[0017] As used herein, the term "vapor pressure" refers to the partial pressure in air at a specified temperature (e.g., 25°C) and standard atmospheric pressure (760mmHg) for a given chemical species. It defines the affinity of a chemical species for the gas phase rather than the liquid or solid state. The higher the vapor pressure, the greater the proportion of the material present in a closed headspace at equilibrium. It is also related to the evaporation rate of the fragrance material, defined in an open environment where the material leaves the system. Vapor pressure can be readily determined according to the reference program ACD / Percepta Desktop Software, Version 14.0 (Build: Aug / 26 / 2021), Advanced Chemistry Development, Inc (ACD / Labs), Toronto, Canada, www.acdlabs.com.

[0018] A physical parameter relevant to the encapsulation of a fragrance material is its hydrophobicity, which can be defined in terms of its partition coefficient P. As used herein, the term "partition coefficient" refers to the ratio between the equilibrium concentration of the substance in n-octanol and in water, and is a measure of the differential solubility of the substance between these two solvents. As used herein, the term "logP" refers to the base 10 logarithm of the partition coefficient P. logP can be easily determined according to the reference program ACD / Percepta Desktop Software, Version 14.0 (Build: Aug / 26 / 2021), Advanced Chemistry Development, Inc (ACD / Labs), Toronto, Canada, www.acdlabs.com. The logP value is predicted from the SMILE string of the fragrance material molecule. Three different types of logP values ​​can be selected from the software. logP Classic is based on an algorithm that takes into account a database of experimental logP values ​​while using the principle of isolating carbon. logP GALAS is based on an algorithm that takes into account a database of training sets of compounds and adjusts the values ​​with data from structurally similar compounds. Consensus logP is a model based on the previous two algorithms and can be expressed as Consensus logP = a x logP Classic + b x logP GALAS, where a and b are the coefficients of the model. The latter value, Consensus logP, is the logP value shown in this specification.

[0019] Another aspect related to the encapsulation of a fragrance material is its Hansen Solubility Parameter (HSP). The term HSP refers to the solubility parameter approach proposed by Charles Hansen, which was first used to predict polymer solubility in a given solvent, as described in The Three Dimensional Solubility Parameter and Solvent Diffusion Coefficient, by Charles Hansen, Danish Technical Press (Copenhagen, 1967). This approach has since been reapplied to many other molecules. A fragrance material (or flavor material or solvent) and its interaction with its environment are defined by three forces: atomic dispersion forces, molecular permanent dipole forces, and molecular hydrogen bond forces. Materials with similar HSP parameters are more likely to be miscible. These forces can be quantified by three values: δD, the Hansen dispersion value related to van der Waals interactions (intermolecular forces); δP, the Hansen polarity value related to dipole moments (charges); and δH, the Hansen hydrogen bond ("h-bond") value. Solubility parameter δ(MPa 1 / 2 ) is δ 2 = δ D 2 +δ P 2 +δ H 2=E / V, where E is the cohesive energy of the solvent and V is the molar volume. HSP values ​​for a given material can be obtained in two main different ways from the Hansen Solubility Parameters in Practice (HSPiP) software available at www.hansen-solubility.com. These values ​​can be retrieved from the Master Dataset, which contains over 20,000 materials, by searching by name or CAS number, or they are predicted by entering the SMILE string of a given molecule in the DIY section of the software using the Yamamoto-Molecular Breaking (Y-MB) method. Furthermore, the determination of the HSP sphere for a given fragrance material is a good way to predict the solubility preference within a blend of fragrance materials. The radius of the HSP sphere, Ro, is defined as Ro=Ra / RED, where Ra is the cohesive energy of the solvent and V is the molar volume. 2 = 4(δ D1 -δ D2 ) 2 +(δ P1 -δ P2 ) 2 +(δ H1 -δ H2 ) 2 where RED is the relative energy difference between two molecules (1 and 2) and RED is the HSP distance between the two molecules (1 and 2). This RED value can also be extracted or predicted from the HSPiP software, and a good solvent for a given material should exhibit a RED value of 1 or less, while a solvent exhibiting a RED value greater than 1 should be considered a poor solvent for the given material.

[0020] The fragrance materials may be selected from alcohols, aldehydes, ketones, esters, ethers, acetates, alkenes, nitriles, nitrogen heterocycles, sulfur heterocycles, and Schiff bases.

[0021] Preferred aldehyde fragrance materials include alpha-amylcinnamaldehyde, anisaldehyde, decyl aldehyde, lauric aldehyde, methyl n-nonylacetaldehyde, methyl octylacetaldehyde, nonyl aldehyde, benzenecarboxaldehyde, neral, geranial, 1,1-diethoxy-3,7-dimethylocta-2,6-diene, 4-isopropylbenzaldehyde, 2,4-dimethyl-3-cyclohexene-1-carboxylate, 1,2-dimethyl-2,3-dimethyl-1,4-dimethyl-1,5-dimethyl-1,6-dimethyl-1,7-dimethyl-1,8-dimethyl-1,9-dimethyl-1,8-dimethyl-1,9-dimethyl-1,9-dimethyl-1,5-dimethyl-1,8-dimethyl-1,9 ... cinnamaldehyde, alpha-methyl-p-isopropyldihydrocinnamaldehyde, 3-(3-isopropylphenyl)butanal, alpha-hexylcinnamaldehyde, 7-hydroxy-3,7-dimethyloctan-1-al, 2,4-dimethyl-3-cyclohexene-1-carboxaldehyde, octylaldehyde, phenylacetaldehyde, 2,4-dimethyl-3-cyclohexene-1-carboxaldehyde, hexanal, 3,7-dimethyloctanal, 6,6-dimethylbicyclo[3. 1.1]hept-2-ene-2-butanal, nonanal, octanal, 2-nonenal, undecenal, 2-methyl-4-(2,6,6-trimethyl-1-cyclohexenyl-1)-2-butenal, 2,6-dimethyloctanal, 3-(p-isopropylphenyl)propionaldehyde, 3-phenyl-4-pentenal, citronellal, o / p-ethyl-alpha, alpha, 9-decenal, dimethyldihydrocinnamaldehyde, p-isobutyl-alpha, methylhydrocinnamaldehyde , cis-4-decen-1-al, 2,5-dimethyl-2-ethenyl-4-hexenal, trans-2-methyl-2-butenal, 3-methylnonanal, alpha-sinensal, 3-phenylbutanal, 2,2-dimethyl-3-phenylpropionaldehyde, m-tertbutyl-alpha-methyldihydrocinnamic aldehyde, geranyloxyacetaldehyde, trans-4-decen-1-al, methoxycitronellal, and mixtures thereof.

[0022] Preferred ester fragrance materials include allyl cyclohexane propionate, allyl heptanoate, allyl amyl glycolate, allyl caproate, amyl acetate (n-pentyl acetate), amyl propionate, benzyl acetate, benzyl propionate, benzyl salicylate, cis-3-hexenyl acetate, citronellyl acetate, citronellyl propionate, cyclohexyl salicylate, dihydroisojasmonate, Dimethylbenzylcarbinyl acetate, ethyl acetate, ethyl acetoacetate, ethyl butyrate, ethyl 2-methylbutyrate, ethyl 2-methylpentanoate, fenchyl acetate (1,3,3-trimethyl-2-norbornanyl acetate), tricyclodecenyl acetate, tricyclodecenyl propionate, geranyl acetate, cis-3-hexenyl isobutyrate, hexyl acetate, cis-3-hexenyl salicylate, n- Hexyl salicylate, isobornyl acetate, linalyl acetate, para-tert-butylcyclohexyl acetate, (-)-L-menthyl acetate, ortho-tert-butylcyclohexyl acetate, methyl benzoate, methyl dihydroisojasmonate, alpha-methylbenzyl acetate, methyl salicylate, 2-phenylethyl acetate, prenyl acetate, cedryl acetate, cyclabute, phenethyl phenyl acetate , terpinyl formate, citronellyl anthranilate, ethyl tricyclo[5.2.1.0-2,6]decane-2-carboxylate, n-hexyl ethyl acetoacetate, 2-tert-butyl-4-methylcyclohexyl acetate, formic acid, 3,5,5-trimethylhexyl ester, phenethyl crotonate, cyclogeranyl acetate, geranyl crotonate, ethyl geranate, geranyl isobutyrate, 3,7-dimethylethyl 2-noninoate-2,6-Octadienoic acid methyl ester, citronellyl valerate, 2-hexenyl cyclopentanone, cyclohexyl anthranilate, L-citronellyl tiglate, butyl tiglate, pentyl tiglate, geranyl caprylate, 9-decenyl acetate, 2-isopropyl-5-methylhexyl-1-butyrate, n-pentyl benzoate, 2-methylbutyl benzoate (and mixtures thereof with pentyl benzoate), dimethylbenzyl carbinyl propionate, dimethylbenzyl carbinyl Acetate, trans-2-hexenyl salicylate, dimethylbenzylcarbinyl isobutyrate, 3,7-dimethyloctyl formate, rosinyl formate, rosinyl isovalerate, rosinyl acetate, rosinyl butyrate, rosinyl propionate, cyclohexyl ethyl acetate, neryl butyrate, tetrahydrogeranyl butyrate, myrcenyl acetate, 2,5-dimethyl-2-ethenylhex-4-enoic acid methyl ester, 2,4-dimethylcyclohexane-1-methyl acetate tate, ocimenyl acetate, linalyl isobutyrate, 6-methyl-5-heptenyl-1-acetate, 4-methyl-2-pentyl acetate, n-pentyl 2-methylbutyrate, propyl acetate, isopropenyl acetate, isopropyl acetate, 1-methylcyclohex-3-ene-carboxylic acid, methyl ester, propyl tiglate, propyl / isobutylcyclopent-3-enyl-1-acetate (alpha vinyl), butyl 2-furoate, ethyl 2-pentenoate, (E) -Methyl 3-pentenoate, 3-methoxy-3-methylbutyl acetate, n-pentyl crotonate, n-pentyl isobutyrate, propyl formate, furfuryl butyrate, methyl angelate, methyl pivalate, prenyl caproate, furfuryl propionate, diethyl maleate, isopropyl 2-methylbutyrate, dimethyl malonate, bornyl formate, styrallyl acetate, 1-(2-furyl)-1-propanone, l-citronellyl acetate, 3,7-dimethyl-1,Examples of the aryl esters include, but are not limited to, 6-nonadiene-3-yl acetate, neryl crotate, dihydromyrcenyl acetate, tetrahydromyrcenyl acetate, lavandulyl acetate, 4-cyclooctenyl isobutyrate, cyclopentyl isobutyrate, 3-methyl-3-butenyl acetate, allyl acetate, geranyl formate, cis-3-hexenyl caproate, and mixtures thereof.

[0023] Preferred alcohol fragrance materials include benzyl alcohol, beta-gamma-hexenol (2-hexen-1-ol), cedrol, citronellol, cinnamic alcohol, p-cresol, cumin alcohol, dihydromyrcenol, 3,7-dimethyl-1-octanol, dimethylbenzylcarbinol, eucalyptol, eugenol, fenchyl alcohol, geraniol, hydratoic alcohol, isononyl alcohol (3,5,5-trimethyl-1-hexanol), and linalool. , Methyl Chavicol (Estragole), Methyl Eugenol (Eugenyl Methyl Ether), Nerol, 2-Octanol, Patchouli Alcohol, Phenylhexanol (3-Methyl-5-phenyl-1-pentanol), Phenethyl Alcohol, Alpha-Terpineol, Tetrahydrolinalool, Tetrahydromyrcenol, 4-Methyl-3-decen-5-ol, 1-3,7-Dimethyloctan-1-ol, 2-(Furfuryl-2)-heptanol, 6,8-Dimethyl-2-nonanol, Ethyl 1,2-Dimethyl-2-(2-hexenyl)-1-ol, 3,7-dimethyl-(2)-6-octen(adiene)-1-ol, trans-2-undecen-1-ol, 2-ethyl-2-prenyl-3-hexenol, isobutylbenzylcarbinol, dimethylbenzylcarbinol, ocimenol, 3,7-dimethyl-1,6-nonadiene-3-ol (cis&trans), tetrahydromyrcenol, alpha-terpineol, 9-decenol-1,2-(2-hexenyl)-1-ol, cyclopentanol, 2,6-dimethyl-2-heptanol, 3-methyl-1-octen-3-ol, 379-trimethyl-1,6-decadien-3-ol, 3,7-dimethyl-6-nonen-1-ol, 3,7-dimethyl-1-octyne-3-ol, 2,6-dimethyl-1,5,7-octatrienol-3, dihydromyrcenol, 2,6-trimethyl-5,9-undecadienol, 2,5-dimethyl-2-propylhex-4-enol-1, (Z)-3-hexenol, o,m,Examples of suitable ethanolamines include, but are not limited to, p-methyl-phenylethanol, 2-methyl-5-phenyl-1-pentanol, 3-methylphenethyl alcohol, para-methyldimethylbenzyl carbinol, methylbenzyl carbinol, p-methylphenylethanol, 3,7-dimethyl-2-octen-1-ol, 2-methyl-6-methylene-7-octen-4-ol, and mixtures thereof.

[0024] Preferred ketone fragrance materials include oxacycloheptadec-10-en-2-one, benzylacetone, benzophenone, L-carvone, cis-jasmone, 4-(2,6,6-trimethyl-3-cyclohexen-1-yl)-but-3-en-4-one, ethyl amyl ketone, alpha-ionone, ionone beta, ethanone, octahydro-2,3,8,8-tetramethyl-2-acetonaphthalene, alpha -irone, 1-(5,5-dimethyl-1-cyclohexen-1-yl)-4-penten-1-one, 3-nonanone, ethylhexyl ketone, menthone, 4-methyl-acetophenone, gamma-methyl ionone, methyl pentyl ketone, methyl heptenone (6-methyl-5-hepten-2-one), methyl heptyl ketone, methyl hexyl ketone, delta mucenone, 2-octanone, 2-pentyl-3-methyl-2-cyclopentenone cyclopentenone, 2-heptylcyclopentanone, alpha-methylionone, 3-methyl-2-(trans-2-pentenyl)-cyclopentenone, octenylcyclopentanone, n-amylcyclopentenone, 6-hydroxy-3,7-dimethyloctanoic acid lactone, 2-hydroxy-2-cyclohexen-1-one, 3-methyl-4-phenyl-3-buten-2-one, 2-pentyl-2,5,5-trimethylcyclopentanone, 2-cyclopentylcyclopentanol-1,5-methylhexan-2-one, gamma-dodecalactone, delta-dodecalactone, gamma-nonalactone, delta-nonalactone, gamma-octalactone, delta-undecalactone, gamma-undecalactone, alpha damascone, beta damascone, gamma damascone, delta damascone, and mixtures thereof.

[0025] Preferred ether fragrance materials include, but are not limited to, diphenyl oxide, p-cresyl methyl ether, 4,6,6,7,8,8-hexamethyl-1,3,4,6,7,8-hexahydro-cyclopenta(G)-2-benzopyran, beta-naphthyl methyl ether, methyl isobutenyl tetrahydropyran, 5-acetyl-1,1,2,3,3,6-hexamethylindane (phantolide), 7-acetyl-1,1,3,4,4,6-hexamethyltetralin (tonalide), 2-phenylethyl-3-methylbut-2-enyl ether, ethyl geranyl ether, phenylethyl isopropyl ether, and mixtures thereof.

[0026] Preferred alkene fragrance materials include, but are not limited to, allo-ocimene, camphene, beta-caryophyllene, cadinene, diphenylmethane, d-limonene, limolene, beta-myrcene, para-cymene, 2-alpha-pinene, beta-pinene, alpha-terpinene, gamma-terpinene, terpineolene, 7-methyl-3-methylene-1,6-octadiene, and mixtures thereof.

[0027] Preferred nitrile fragrance materials include, but are not limited to, 3,7-dimethyl-6-octenenitrile, 3,7-dimethyl-2(3),6-nonadienenitrile, (2E,6Z)-2,6-nonadienenitrile, n-dodecanenitrile, and mixtures thereof.

[0028] Preferred Schiff base fragrance materials include, but are not limited to, citronellyl nitrile, nonanal / methyl anthranilate, N-octylidene-anthranilic acid methyl ester, hydroxycitronellal / methyl anthranilate, methoxyphenylpropanal / methyl anthranilate, ethyl p-aminobenzoate / hydroxycitronellal, citral / methyl anthranilate, 2,4-dimethylcyclohex-3-enecarbaldehyde methyl anthranilate, hydroxycitronellal-indole, and mixtures thereof.

[0029] As used herein, the term "flavor" refers to an ingredient of a formulation that can impart or modify the taste and smell of a product, e.g., toothpaste or food. Flavors are usually used to impart an overall pleasant taste and odor, or taste and odor profile, to a product, either to provide a simply enjoyable experience, as in foods, or to mask unpleasant tastes and odors, as in medicines. A flavor or flavoring material can be described in terms of its aroma intensity, detection threshold, and quality. A "flavor" can be composed of one or more ingredients, which can be single chemicals, referred to herein as "flavoring materials," or a mixture of different "flavoring materials." Flavoring materials can be created by synthetic processes or extracted from natural, especially plants, to create naturally occurring plant and animal oils and exudates, e.g., vanilla. The synthetic and naturally derived flavoring materials can then be blended into flavors by skilled perfumers for use in consumer products. Flavoring materials can be obtained from specialized flavor suppliers, known as flavor houses, as individual chemicals, natural blends, or as proprietary specialty blends whose complete composition is not disclosed.Individual flavor materials, including known natural blends, can be found by consulting journals commonly used by those skilled in the art, such as "Perfume and Flavourist" or "Journal of Essential Oil Research", or journals listed in reference books, such as S. Arctander Perfume and Flavor Chemicals, 1969, Montclair, New Jersey, USA, and more recently republished by Allured Publishing Corporation Illinois (1994), "Perfume and Flavour Materials of Natural Origin", S. Arctander, Ed., Elizabeth, NJ, 1960, and "Flavourings", E. Ziegler and H. Ziegler (ed.), Wiley-VCH Weinheim, 1998. It will be understood that flavors can be volatile or have volatile components that are detected by the nose, similar to fragrances. Thus, flavor materials can also be classified according to their physical properties, such as volatility and hydrophobicity, using the methods described above for fragrance materials. Flavor materials can also be described according to their Hansen Solubility Parameters, using the method described above for fragrance materials.

[0030] Sources of flavoring materials include essential oils, floral oils, absolutes, resins, resinoids, balsams, and tinctures. Preferred flavoring materials include anise oil, ethyl-2-methylbutyrate, vanillin, cis-jasmone-3-heptenol, cis-jasmone-3-hexenol, trans-2-heptenal, butyl valerate, 2,3-diethylpyrazine, methylcyclo-pentenolone, benzaldehyde, valerian oil, 3,4-dimeth-oxyphenol, amyl acetate, amyl cinnamate, y-butyryllactone, trimethylpyrazine, phenylacetic acid, isopropyl alcohol, ethyl ketone ... Sovaleraldehyde, Ethyl Maltol, Ethyl Vanillin, Ethyl Valerate, Ethyl Butyrate, Cocoa Extract, Coffee Extract, Peppermint Oil, Spearmint Oil, Clove Oil, Anethole, Cardamom Oil, Wintergreen Oil, Cinnamaldehyde, Ethyl 2-Methylvalerate, g-Hexenyl Lactone, 2,4-Decadienal, 2,4-Heptadienal, Methylthiazole Alcohol (4-Methyl-5-b-Hydroxyethylthiazole), 2-Methylbutanethiol , 4-mercapto-2-butanone, 3-mercapto-2-pentanone, 1-mercapto-2-propane, benzaldehyde, furfural, furfuryl alcohol, 2-mercaptopropionic acid, alkylpyrazine, methylpyrazine, 2-ethyl-3-methylpyrazine, tetramethylpyrazine, polysulfides, dipropyl disulfide, methylbenzyl disulfide, alkylthiophenes, 2,3-dimethylthiophene, 5-methylfurfural, acetylfuran, 2, 4-Decadienal, Guacol, Phenylacetaldehyde, b-Decalactone, d-Limonene, Acetoin, Amyl Acetate, Maltol, Ethyl Butyrate, Levulinic Acid, Piperonal, Ethyl Acetate, n-Octanal, n-Pentanal, n-Hexanal, Diacetyl, Monosodium Glutamate, Monopotassium Glutamate, Sulfur-containing amino acids such as Cysteine, 2-Methylfuran-3-thiol, 2-Methyldihydrofuran-3-thiol, 2,5-dimethylfuran-3-thiol, tetramethylpyrazine, propylpropenyl disulfide, propylpropenyl trisulfide, diallyl disulfide, diallyl trisulfide, dipropenyl disulfide, dipropenyl trisulfide, 4-methyl-2-[(methylthio)-ethyl]-1,3-dithiolane, 4,5-dimethyl-2-(methylthiomethyl)-1,3-dithiolane, 4-methyl-2-(methylthiomethyl)-1,3-dithiolane, hop oil, citrus oil such as lemon, orange, lime, and grapefruit citrus oil.

[0031] As used herein, the term "butter" refers to a lipophilic aliphatic compound that has a reversible solid / liquid state change and contains a liquid fraction and a solid fraction at a temperature of 25° C. and atmospheric pressure (760 mmHg). Preferred butters include lanolin and its derivatives, such as lanolin alcohol, oxyethylenated lanolin, acetylated lanolin, lanolin esters, such as isopropyl lanolate, oxypropylenated lanolin; polymeric or non-polymeric silicone compounds, such as polydimethylsiloxanes of high molecular weight, polydimethylsiloxanes with alkyl or alkoxy type side chains having 8 to 24 carbon atoms, especially stearyl dimethicone; and vinyl polymers.

[0032] Preferably, the butter is of vegetable origin, such as those described in Ullmann's Encyclopaedia of Industrial Chemistry ("Fats and Fatty Oils", A. Thomas, published 15 June 2000). Examples include triglycerides C10 to C18, including the liquid and solid fractions at a temperature of 25° C. and atmospheric pressure (760 mmHg), shea butter, nilotica shea butter, garam butter, Borneo butter or Tengkawan tallow, Shorea butter, Illipe butter, Madhuca butter or Bassia Madhuca longifolia, Moller butter, Katiau butter, Phulwara butter, mango seed oil, murumuru butter, kokum butter, Ucuuba butter, Tucuma butter, Painha butter, coffee butter, apricot butter, macadamia butter, grape butter, avocado butter, olive butter, sweet almond butter, cocoa butter, sunflower butter, Astrocaryum Murumuru Seed Butter, Theobroma Grandiflorum Seed Butter, Irvingia Gabonensis Kernel Butter), jojoba esters (a mixture of wax and oil hydrogenated jojoba) and ethyl esters of shea butter, and combinations thereof.

[0033] As used herein, the term "wax" refers to a lipophilic compound that is solid at 25°C, has a reversible solid / liquid state change, and has a melting point of 30°C or more and 120°C or less.

[0034] Examples of waxes include hydrocarbon waxes such as beeswax, lanolin wax, and Chinese insect wax; rice wax, carnauba wax, Maydelilla wax, Ouricurry wax, alfa wax, cork fiber wax, sugar maye wax, Japan wax, and sumach wax; montan wax, microcrystalline wax, paraffin, and ozokerite; polyethylene waxes, waxes obtained by Fischer-Tropsch synthesis, waxy copolymers and their esters, and mixtures thereof.

[0035] Further examples include waxes obtained by catalytic hydrogenation of animal or vegetable oils having linear or branched C8 to C32 fatty chains, among which are hydrogenated jojoba oil, hydrogenated sunflower oil, hydrogenated castor oil, hydrogenated coconut oil and hydrogenated lanolin oil, di-tetrastearate (trimethylol-1,1,1 propane), di-(1,1,1-trimethylolpropane) tetrapropenate.

[0036] Further examples include waxes obtained by transesterification and hydrogenation of vegetable oils such as castor oil or olive oil.

[0037] Further examples include silicone waxes, such as polysiloxanes.Among the commercially available silicone waxes of this type, mention may be made in particular of those sold under the names Abilwax 9800, 9801 or 9810 (GOLDSCHMIDT), KF910 and KF7002 (SHIN ETSU), or 176-1118-3 and 176-11481 (GENERAL ELECTRIC).The silicone waxes that may be used may also be alkyl or alkoxy dimethicones, such as the following commercial products: Abilwax 2428, 2434 and 2440 (GOLDSCHMIDT), or VP 1622 and VP 1621 (WACKER), as well as (C20-C60) alkyl dimethicones, in particular (C30-C45) alkyl dimethicones, such as the silicone wax sold under the name SF-1642 by GE-Bayer Silicones. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0038] The inventors of the present invention have discovered a method for preparing a plant-derived protein colloidal dispersion in which a lipophilic phase, optionally containing an active ingredient, can be dispersed. The method allows for the formation of oil-in-water emulsions with excellent long-term physical stability, and has the added advantage that they are much less likely to induce allergic reactions than traditional emulsifiers, and therefore can be used in a wide range of consumer product applications.

[0039] The emulsions of the present invention contain small, substantially insoluble plant protein particles that stabilize a lipophilic phase by the Pickering mechanism in the absence of any conventional amphiphilic emulsifiers (i.e., the emulsions are Pickering emulsions).

[0040] The present invention relates to a method for the preparation of an emulsion, (a) forming a solution comprising one or more plant-derived proteins in a solvent system, the solvent system comprising miscible co-solvents, a first co-solvent increasing the solubility of the plant-derived proteins and a second co-solvent decreasing the solubility of the plant-derived proteins; (b) inducing the protein in the solution to undergo a sol-gel transition to form a plant-derived protein hydrogel; (c) subjecting the plant-derived protein hydrogel to a first shear step to form a first plant-derived protein hydrogel slurry; (d) subjecting the first plant-derived protein hydrogel slurry to a solvent reduction step to form a washed plant-derived protein hydrogel slurry; (e) subjecting the washed plant-derived protein hydrogel slurry to a second shear step to form a second plant-derived protein hydrogel slurry; (f) dispersing a lipophilic phase in the second plant-derived protein hydrogel slurry to form an emulsion; forming an emulsion having less than 1% protein solids by weight, based on the total weight of the emulsion.

[0041] Any suitable plant-derived protein can be used in the present invention.In a preferred method of the present invention, the plant-derived protein is obtained from broad bean, mung bean, pea, rice, potato, rapeseed, lentil, chickpea, sunflower seed, pumpkin seed, flax, chia, canola, lupin, alfalfa, moringa, wheat, corn zein or sorghum, and preferably the plant protein is selected from pea protein, potato protein, rapeseed protein, lentil protein, chickpea protein, broad bean protein, mung bean protein, sunflower seed protein, pumpkin seed protein, flax protein, chia protein, canola protein, lupin protein, alfalfa protein, moringa protein and / or rice protein.More preferably, the plant-derived protein is pea protein and / or potato protein.Such proteins are considered to be hypoallergenic proteins.

[0042] Suitable plant-derived proteins further include: Brassica: for example, Brassica balearica: Mallorca cabbage, Brassica carinata: Abyssinian mustard or Abyssinian cabbage, Brassica elongata: elongated mustard, Brassica fruticulosa: Mediterranean cabbage, Brassica hilarionis: St. Hilarion's cabbage, Brassica juncea: Indian mustard, brown mustard and mustard greens, Sarepta mustard, Brassica napus: rapeseed, canola, rutabaga, Brassica narinosa: broadbeaked mustard, Brassica nigra: black mustard, Brassica oleracea: kale, cabbage, collard greens, broccoli, cauliflower, Chinese broccoli, Brussels sprouts, kohlrabi, Brassica perviridis: tender greens, mustard spinach, Brassica rapa (also known as B. campestris): Chinese cabbage, turnip, rapini, komatsuna, Brassica rupestris: brown mustard, Brassica tournefortii: Asian mustard - Solanaceae: for example, tomato, potato, eggplant, bell pepper and chilli; - cereals: e.g. corn, rice, wheat, barley, sorghum, millet, oats, rye, triticale, fonio - Quasi-cereals: such as amaranth (also called amaranth, red amaranth, prince-of-Wales-feather), breadfruit, buckwheat, chia, cockscomb (also called quail grass or soko), pitseed goosefoot, qaniwa, quinoa and wattleseed (also called acacia seed); - legumes such as Acacia alata (Winged Wattle), Acacia decipiens, Acacia saligna (commonly known by various names including coojong, golden-leaved wattle, orange wattle and blue-leafed wattle), Arachis hypogaea (peanut), Astragalus galegiformis, Cytisus laburnum (common laburnum, golden chain or golden rain), Cytisus supinus, Dolichos lablab (commonly known as lablab-bean, bonavist bean / pea, dolichos bean, seim bean, bean, love love bean, Egyptian bean, Indian bean, bataw, and Australian pea), Ervum lens (lentil), Genista tinctoria (common names include dyer's whin, waxen woad, and waxen wood), Glycine max (soybean), Lathyrus clymenum (pea vine or lathyrus), Lathyrus odoratus (pea vine or lathyrus), Lathyrus sativus (pea vine or lathyrus), Lathyrus sylvestris (pea vine or lathyrus), Lotus tetragonolobus (asparagus-pea or winged pea), Lupinus albus (lupine), Lupinus angustifolius(lupine), Lupinus luteus(lupine), Lupinus polyphyllus(lupine), Medicago sativa(alfalfa), Phaseolus aureus(mungbean), Phaseolus coccineus(green bean), Phaseolusnanus (green beans), Phaseolus vulgaris (mung beans), Pisum sativum (peas), Trifolium hybridum (clover), Trifolium pretense (red clover), Vicia faba (broad beans), Vicia sativa (fava beans), Vigna unguiculate (cowpeas), -Non-legumes: for example: Acanshosicyos horrida, Aesculus hyppocastanum, Anacardium occidentale, Balanites aegyptica, Bertholletia excels, Beta vulgaris, Brassica napus, Brassica juncea, Brassica nigra, Brassica hirta, Cannabis sativa, Citrullus vulgaris, Citrus aurantiaca, Cucurbita maxima, Fagopyrum esculentum, Gossypium barbadense (extra long staple cotton), Heianthus annuus (sunflower), Nicotiana sp. (tobacco), Prunus avium (cherries), Prunus spp. (sour cherries), Prusus domestica (plums), Prusus amygdalus (almonds), Rricinus communis (castor beans / castor oil plant), Sasamum indicum (sesame), Sinapis alba (white mustard), and Terlfalrea pedata (persimmon nuts).

[0043] For the avoidance of doubt, the plant-derived emulsions of the present invention do not include plants in their natural state.

[0044] In step (a), the first co-solvent increases the solubility of the plant-derived protein. The first co-solvent may be considered as a solubilizing co-solvent. There may be one or more solubilizing co-solvents, which may fully or partially solubilize the plant-derived protein.

[0045] An example of a solubilizing co-solvent is an organic acid. An organic acid is an organic compound that has acidic properties. Preferably, the organic acid is sourced from a natural plant-derived or bio-derived feedstock.

[0046] In a preferred method of the present invention, the first co-solvent is an organic acid. Preferably, the organic acid is acetic acid, lactic acid, formic acid, gluconic acid, propionic acid, α-hydroxy acid and / or β-hydroxy acid. Preferred α-hydroxy acids include glycolic acid, acetic acid, lactic acid, malic acid, citric acid and / or tartaric acid, preferably acetic acid or lactic acid. Preferred β-hydroxy acids include β-hydroxypropionic acid, β-hydroxybutyric acid, β-hydroxyβ-methylbutyric acid, 2-hydroxybenzoic acid and carnitine. In a particularly preferred method of the present invention, the organic acid is acetic acid or lactic acid.

[0047] The use of organic acid allows plant protein to be solubilized and also allows for gentle hydrolysis of protein.For example, without wishing to be bound by theory, the solubility of plant-derived protein in organic acid is possible due to i) protein protonation, and ii) the presence of an anion solvation layer that contributes to reducing hydrophobic interactions.When initially dissolved in organic acid, the protonation of plant-derived protein can help stabilize them in its non-solvent, for example, water.

[0048] In step (a), the second co-solvent reduces the solubility of the plant-derived protein compared to the first co-solvent. The second co-solvent may be considered a desolubilizing co-solvent. There may be one or more desolubilizing co-solvents.

[0049] In a preferred method of the present invention, the second co-solvent is selected from water, ethanol and / or ethyl acetate, more preferably water and / or ethanol, even more preferably water.

[0050] In a preferred method of the invention, in the solvent system, the cosolvent ratio of the first cosolvent to the second cosolvent is about 10-90% v / v, preferably 20-90% v / v, preferably about 20-80% v / v, preferably about 20-60% v / v, about 25-55% v / v, about 30-50% v / v, about 20%, about 30%, about 40%, about 50% or about 60% v / v, most preferably about 30-50% v / v.

[0051] In a preferred method of the present invention, the concentration of the plant-derived protein in the solvent system is 25-200 mg / mL, more preferably 50-150 mg / mL. The ratio of organic acids may vary depending on the protein concentration, for example, a higher organic acid ratio may be used with increasing protein concentration.

[0052] In a preferred method of the invention, the degree of protein hydrolysis (i.e., the percentage of broken peptide bonds in the protein hydrolysate) is controlled to modify the properties of the resulting hydrogel. For example, increasing the acid concentration present during formation increases the degree of protein hydrolysis. A higher degree of protein hydrolysis results in the formation of a less rigid hydrogel.

[0053] In a preferred method according to the invention the degree of protein hydrolysis is between 0.1 and 10%, preferably between 0.1 and 5%, even more preferably between 0.1 and 2.5%.

[0054] To form a solution containing one or more plant-derived proteins, it may be necessary to apply a physical stimulus to the protein / solvent system mixture to allow the proteins to dissolve. Suitable physical stimuli include heating, sonication, stirring, high shear mixing, high shear homogenization or other physical techniques. A preferred technique is heating, optionally followed by sonication.

[0055] Preferably, the protein / solvent system mixture is subjected to a physical stimulus which is heating, and the solution is heated to about 70° C. or greater. More preferably, the protein / solvent system mixture is heated to about 75° C. or greater, about 80° C. or greater, about 85° C. or greater, or about 90° C. Even more preferably, the protein / solvent system mixture is heated to 85° C.

[0056] Preferably, the protein / solvent system mixture is subjected to a physical stimulus of heating for about 5 minutes, 10 minutes, 15 minutes, 20 minutes, 25 minutes, 30 minutes, or for a period of time greater than 30 minutes. The heated protein / solvent system mixture is optionally subjected to a subsequent ultrasonic treatment.

[0057] In a preferred method of the invention, in step (b), the protein solution is heated to a first temperature higher than the sol-gel transition temperature of the one or more plant-derived protein solutions and then reduced to a second temperature lower than the sol-gel transition temperature of the one or more plant-derived protein solutions to form a hydrogel.

[0058] The protein solution is heated so that the liquid solution is maintained above the sol-gel transition of the protein. By modifying the solvent system (e.g., through selection of the organic acid, the ratio of organic acid to additional solvent, or through additional means), it is possible to modify the sol-gel transition temperature of the protein. Through appropriate selection of conditions, it is possible to carefully control the sol-gel transition of the protein, and thereby control the formation of the hydrogel.

[0059] Preferably, the protein solution is heated to about 70° C. or greater. More preferably, the protein is heated to about 75° C. or greater, about 80° C. or greater, about 85° C. or greater, or about 90° C. Even more preferably, the protein is heated to 85° C.

[0060] The protein solution may be held at elevated temperature for about 5 minutes, 10 minutes, 15 minutes, 20 minutes, 25 minutes, 30 minutes, 45 minutes, or 1 hour. A preferred time is at least 30 minutes to allow complete solubilization of the protein. It is possible to hold the protein solution at elevated temperature for longer periods of time.

[0061] After heating the protein solution to a temperature above the sol-gel transition temperature, the temperature of the protein solution can be reduced to a second temperature below the sol-gel transition temperature to facilitate the formation of a hydrogel. The second temperature can be room temperature. The second temperature can be in the range of 5-25°C, preferably 10-20°C. The protein solution can be kept at the low temperature for an extended period of time, such as days or weeks, before carrying out the first shearing step in step (c). The protein solution can be kept at the low temperature for about 5 minutes, 10 minutes, 15 minutes, 20 minutes, 25 minutes or about 30 minutes. A particular shortened time is about 5 minutes.

[0062] The particular temperature will depend on the properties of the protein source, the solvent conditions used, and therefore the sol-gel transition temperature. Alternatively, the high and low temperatures may be relatively fixed (e.g., about 85° C., then about room temperature), with the co-solvent mixture conditions adjusted to ensure a suitable sol-gel transition temperature for the selected plant-derived protein.

[0063] Without wishing to be bound by theory, it is believed that when plant proteins are added to a solvent system, they form a dispersion of insoluble colloidal protein aggregates. Aggregate size can be measured by Dynamic Light Scattering (DLS). A suitable instrument for measuring aggregate size is the Zetasizer Nano S (Malvern).

[0064] It is believed that when a protein solution is heated above the sol-gel transition temperature in the presence of a co-solvent system, the plant protein is partially unfolded, exposing hydrophobic amino acids that were initially buried within the protein's native structure. Once partially unfolded, the co-solvent can interact with the unfolded protein molecule. For example, organic acids can not only favor protonating amino acid residues, but also form anionic salt bridges that stabilize hydrophobic interactions. Also, heating at high temperatures disrupts protein-protein non-covalent intermolecular contacts.

[0065] Furthermore, the application of mechanical agitation, e.g., ultrasonication, is believed to break down large colloidal protein aggregates into smaller aggregates and also disrupt protein intermolecular interactions.Using this approach, the size of protein aggregates can be significantly reduced to a particle size of less than 100 nm before gelation.Preferably, the above method includes protein aggregates with an average size of less than 200 nm, preferably less than 150 nm, less than 125 nm, less than 100 nm, less than 90 nm, less than 80 nm, less than 70 nm, less than 60 nm, less than 50 nm, less than 40 nm, or less than 30 nm.Therefore, at this stage of the method, the plant-derived protein is believed to have a protein secondary structure with a high level of α-helix and random coil.

[0066] Furthermore, cooling the protein solution below the sol-gel transition temperature is believed to allow protein-protein non-covalent intermolecular contacts and thus promote the self-assembly of interconnected protein aggregates of plant protein molecules into hydrogels.

[0067] After gelation, the aggregates may be fine strands. The aggregates may have a median average length of 50-500 nm. The aggregates may have an average length of 50-500 nm. 80% of the aggregates may have an average length of 50-500 nm. The aggregates may have a median height of 5-50 nm. The aggregates may have an average height of 5-50 nm. 80% of the aggregates may have an average height of 5-50 nm. In a preferred embodiment, the aggregates have a median average length of 50-500 nm and / or a median average height of 5-50 nm.

[0068] It is believed that the methods of the present invention allow plant proteins to aggregate into supramolecular structures through intermolecular hydrogen bonding interactions, in particular through interactions between β-strands.

[0069] The method of the present invention allows for the formation of materials in which there is a high level of β-sheet intermolecular interactions. Thus, in the method of the present invention, the plant derived protein has a protein secondary structure with at least 40% intermolecular β-sheets, at least 50% intermolecular β-sheets, at least 60% intermolecular β-sheets, at least 70% intermolecular β-sheets, at least 80% intermolecular β-sheets, or at least 90% intermolecular β-sheets, the % intermolecular β-sheet content being measured by FTIR (Fourier Transform Infrared Spectroscopy).

[0070] In the process of the invention, step (c) involves a first shear step. The single shear step may be a lower shear step.

[0071] In a preferred method of the invention, the first shearing step involves fragmenting the plant derived protein hydrogel into fragments. Preferably, at least 50% by weight of the fragments produced in the first shearing step have a particle size in the range of 1 mm to 100 mm, preferably 1 mm to 50 mm, preferably 5 mm to 30 mm, more preferably 10 mm to 30 mm. More preferably, at least 80% by weight of the fragments produced in the first shearing step have a particle size in the range of 1 mm to 100 mm, preferably 1 mm to 50 mm, preferably 5 mm to 30 mm, more preferably 10 mm to 30 mm. This can be measured by optical microscopy.

[0072] In a preferred method of the invention, the first shear step is carried out at a temperature below the sol-gel transition temperature of the plant derived protein.

[0073] In a preferred method of the invention, the first shearing step involves mechanical cutting, which means cutting with a knife edge (e.g. knife, extruder blade, etc.).

[0074] In an alternative preferred method of the invention, the first shearing step involves extrusion. For example, the plant-derived protein solution formed in step (a) can be extruded into a non-solubilizing solvent (e.g., water) to form the plant-derived protein hydrogel in large discrete fragments, e.g., the large discrete fragments can take the form of an extrudate having the form of threads or strings. In this way, the fragments can be directly subjected to a solvent reduction step, as described in more detail below. A first shearing step of this nature is more suitable for large-scale processing. In this case, the first shearing step can reduce at least one dimension of the large fragments, e.g., the diameter of the extrudate, to between 1 mm and 100 mm. Preferably, at least 50% by weight of the fragments produced in the first shearing step have at least one internal dimension in the range of between 1 mm and 100 mm, preferably between 1 mm and 50 mm, preferably between 5 mm and 30 mm, more preferably between 10 mm and 30 mm. More preferably, at least 80% by weight of the fragments produced in the first shearing step have an internal dimension in the range of 1 mm to 100 mm, preferably 1 mm to 50 mm, preferably 5 mm to 30 mm, more preferably 10 mm to 30 mm, as can be measured by optical microscopy.

[0075] In the method of the present invention, step (d) involves subjecting the first plant-derived protein hydrogel slurry to a solvent reduction step, preferably a solubilizing solvent reduction step.

[0076] By solubilizing solvent is meant a solvent or mixture of solvents in which the plant-derived protein hydrogel dissolves. Examples include organic acids such as acetic acid, lactic acid, formic acid, propionic acid, α-hydroxy acids and / or β-hydroxy acids. The α-hydroxy acids may preferably be selected from glycolic acid, acetic acid, lactic acid, malic acid, citric acid and / or tartaric acid. The β-hydroxy acids may preferably be selected from β-hydroxypropionic acid, β-hydroxybutyric acid, β-hydroxyβ-methylbutyric acid, 2-hydroxybenzoic acid and carnitine.

[0077] In a preferred method of the invention, the solvent reduction step comprises: (i) contacting a first plant-derived protein hydrogel slurry with a non-solubilizing solvent; (ii) separating the first plant-derived hydrogel slurry from the non-solubilizing solvent to obtain a washed plant-derived protein hydrogel slurry; (iii) optionally repeating steps (i) and (ii).

[0078] Step (i) involves contacting the first plant-derived protein hydrogel slurry with a non-solubilizing solvent, which means a solvent or mixture of solvents in which the plant-derived protein hydrogel does not dissolve. Examples include water or a mixture of water and ethanol.

[0079] In a preferred method of the invention, step (ii) involves mesh filtration or centrifugation, more preferably step (ii) involves mesh filtration using multiple size reducing meshes.

[0080] As will be appreciated by those skilled in the art, if the fragments produced in the first shearing step are too small, the solvent reduction step may be difficult because the fragments may eventually plug the mesh or the collection yield is low. However, if the fragments produced in the first shearing step are too large, the solvent reduction step may take excessive time due to slow mass transfer of the solvent from the center of the fragments.

[0081] Without wishing to be bound by theory, it is believed that due to the porosity of the hydrogel, the solvent reduction step can remove some or all of the solvent (e.g., organic acid) from the hydrogel via solvent exchange.

[0082] The strength of the protein hydrogel can be altered by varying the concentrations of protein and organic acids, among other variables.

[0083] In the method of the present invention, step (e) involves a second shear step to produce a second plant-derived protein hydrogel slurry. The second shear step may be a higher shear step.

[0084] In a preferred method of the present invention, the second shearing step involves further fragmenting the plant derived protein hydrogel.

[0085] In a preferred method of the invention, the second plant derived protein hydrogel slurry has a d of less than 100 μm, preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, more preferably less than 5 μm, more preferably less than 1 μm, as measured by laser diffraction. 50 has.

[0086] In a preferred method of the invention, the second plant derived protein hydrogel slurry has a d of less than 250 μm, preferably less than 100 μm, more preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, as measured by laser diffraction. 90 has.

[0087] In a preferred method of the present invention, the particle size distribution of the hydrogel fragments in the second plant-derived protein hydrogel slurry can be adjusted by varying the nature and intensity of the second shear step. In another preferred method, the particle size distribution of the hydrogel fragments in the second plant-derived protein hydrogel slurry can be adjusted by blending or combining two or more different hydrogel slurries that have been subjected to different second shear steps and have different particle size distributions.

[0088] In a preferred method of the invention, the second shear step is carried out at a temperature below the sol-gel transition temperature of the plant derived protein.

[0089] In a preferred method of the invention, the second shear step is carried out at a temperature below the protein denaturation temperature of the plant-derived protein.

[0090] In a preferred method of the invention, the second shearing step is carried out for at least 5 minutes, more preferably at least 1 minute.

[0091] In preferred methods of the invention, the second shearing step involves sonication (e.g., using equipment such as a Bandelin HD4200 or Hielscher UIP1000hdT), high shear mechanical stirring (e.g., using equipment such as a Silverson rotor-stator high shear mixer), high pressure homogenization, or cavitation, preferably sonication.

[0092] In a preferred method of the invention, the second shearing step involves one or more steps, preferably two steps.

[0093] In a preferred method of the invention, the protein solids of the second plant-derived protein hydrogel slurry have a biodegradation rate based on O2 consumption of 60-100%, more preferably 65-100%, even more preferably 70-100%, even more preferably 75-100%, even more preferably 80-100%, even more preferably 85-100%, and most preferably 90-100%, based on the biological oxygen demand (BOD) as a percentage of the theoretical oxygen demand, when measured according to ISO-14851 version 2019 after 28 days. ISO-14851 version 2019 describes a method to measure the biodegradability of materials in natural aqueous environments using biological oxygen demand in a closed respirometer. This is accomplished by exposing the material under laboratory conditions in an aqueous standard test medium to an inoculum from a previously unexposed, unadapted activated sludge. The measurements are calculated as a percentage of the theoretical oxygen demand calculated from the molecular formula. An internal standard of microcrystalline cellulose is also tested and if its % biodegradation is greater than 60% at the end of the test, the test is valid.

[0094] In a preferred method of the present invention, the second plant-derived protein hydrogel slurry is subjected to a pH adjustment step between steps (e) and (f).

[0095] In a preferred method of the present invention, the pH adjusting step involves adding a pH adjusting material to the second plant-derived protein hydrogel slurry. Preferably, the pH modifying material is a solution containing monovalent metal ions, divalent metal ions or ammonium ions, preferably an aqueous alkaline solution containing monovalent metal ions, divalent metal ions or ammonium ions. More preferably, the pH modifying material is an aqueous hydroxide solution, preferably sodium hydroxide, potassium hydroxide or ammonium hydroxide.

[0096] In a preferred method of the invention, the lipophilic phase comprises a solvent, a butter or a wax.

[0097] In a preferred method of the invention, the lipophilic phase comprises a solvent. Preferably, the solvent is a solvent with low volatility (e.g., having a vapor pressure of less than 0.1 Torr at 25° C., preferably less than 0.01 Torr at 25° C., preferably less than 0.001 Torr at 25° C.).

[0098] Preferably, the solvent has low or no odor.

[0099] Preferably, the solvent has at least two Hansen solubility parameters selected from atomic dispersion forces (δD) less than 20, dipole moment (δP) less than 8, and hydrogen bonding (δH) less than 11. More preferably, the solvent has at least two Hansen solubility parameters selected from atomic dispersion forces (δD) less than 20, dipole moment (δP) less than 4, and hydrogen bonding (δH) less than 5.

[0100] Preferably, the solvent contains only low levels of materials with alcohol functionality (e.g., primary alcohol functionality). In a preferred method of the invention, the solvent contains less than 40% by weight, more preferably less than 20% by weight, of alcohol-containing materials, based on the total weight of the solvent. In a particularly preferred method of the invention, the solvent is free of alcohol-containing materials. Without wishing to be bound by theory, it is believed that alcohols, especially primary alcohols with straight chain alkyl groups, can easily break emulsions.

[0101] In a preferred method of the invention, the lipophilic phase comprises a solvent selected from fatty acid esters, fatty acids, linear or branched hydrocarbons of natural mineral or synthetic origin, fatty alcohols or their ethers, vegetable oils, silicone oils, phthalate esters, rosin resins, diols, triols, benzyl benzoate, triethyl citrate and triacetin, or combinations thereof. Preferably, the solvent is Miglyol® 840, Miglyol® 812 N, Miglyol® 829, Miglyol® 829 ECO, Miglyol® Coco 810, Miglyol® 810 N, Miglyol® 128, Miglyol® 808, Miglyol® T-C7, Miglyol® 8810, Miglyol® PPG 810, Miglyol® OE, Miglyol® DO, and Miglyol® 818, Abalyn®, limonene, benzyl benzoate, diethyl phthalate, isopropyl myristate, triethyl citrate, dipropylene glycol, and propylene glycol, triacetin, glycerin, 1,3 propanediol, or combinations thereof, preferably Miglyol® 812 N.

[0102] Preferably, the solvent is selected from the group consisting of coconut oil, corn oil, canola oil, cottonseed oil, olive oil, palm oil, peanut oil, rapeseed oil, safflower oil, sesame oil, soybean oil, and sunflower oil, squash oil, grape seed oil, hazelnut oil, apricot oil, macadamia oil, avocado oil, meadowfoam seed oil Limnanthes Alba, macadamia nut oil, rosehip rose oil, apricot kernel oil, rice bran oil, argan oil, evening primrose oil, palm oil, rice germ oil, sweet almond oil, peanut seed oil, oil of Mortierella isabelline, safflower seed oil, Queensland nut oil. oil), macadamia intefolia seed oil, wheat germ oil, borage seed oil, shea oil, hazelnut oil), mango seed oil, pomegranate seed oil, Chinese cabbage seed oil, passion fruit seed oil, camellia japanese oil, green tea seed oil, corn germ oil, hoprosthete oil, brazil nut oil, musk rose seed oil, inca seed inch oil, babassu seed oil, sea buckthorn oil, marula seed oil, baobab seed oil, moringa seed oil, castor seed oil, blackcurrant seed oil, tea seed oil, raspberry seed oil, abyssinian crambe seed oil, rosehip seed oil, tomato seed oil, bitter almond oil, yuzu seed oil, pumpkin seed oil, dessert date seed oil, Japanese white pine seed oil, watermelon seed oil, walnut seed oil, nigella oil, carrot seed oil, cranberry seed oil, vanilla oil, cranberry seed oil, acai oil, peach kernel oil, mayonnaise oil and glycerides derived from plant sterols, karanja seed oil and lukuh oil, rosehip oil, coriander oil, linseed oil, chia oil, fenugreek oil, and hemp oil, or combinations thereof.

[0103] Preferably, the solvent is a hydrogenated vegetable oil selected from hydrogenated palm oil, hydrogenated coconut oil, hydrogenated rapeseed oil, hydrogenated castor oil, hydrogenated palm kernel oil, a triester of hydrogenated castor oil with isostearic acid, hydrogenated cottonseed oil, hydrogenated olive oil, hydrogenated peanut oil, and hydrogenated soybean oil, or combinations thereof.

[0104] A vegetable oil is an oil derived from a plant source. Alternatively, the solvent is derived from a vegetable oil. As will be understood by those skilled in the art, a vegetable oil solvent or a vegetable oil-derived solvent may provide additional benefits beyond its solvating properties, for example, as a moisturizing agent in cosmetic applications.

[0105] Preferred fatty acid esters include oils of the formulae R1COOR2 and R1OR2, where R1 represents a residue of a C8 to C29 fatty acid and R2 represents a branched or unbranched C3 to C30 hydrocarbon chain, such as pulcerin oil, isononyl isononanoate, isodecyl neopentanoate, isopropyl myristate, 2-ethylhexyl palmitate, dodecyl octyl-2-stearate, octyl-2-dodecyl erucate, isostearyl isostearate; hydroxylated esters, such as sostearyl lactate, esters such as propylene glycol dioctanoate, neopentyl glycol diheptanoate and diethylene glycol diisononanoate; and pentaerythritol esters such as pentaerythrityl tetraheptanoate (DUB PTB) or pentaerythrityl tetraisostearate (Prisorine 3631), triglycerides such as caprylic, capric, myristic and stearic acid triglycerides, triethylhexanoin, tribehenin, triisostearin, tricaprylin (or triacylglycerol), trihydroxymethoxystearin, and triheptanoin.

[0106] Preferred fatty acids include stearic acid, palmitic acid, myristic acid, lauric acid, capric acid, and caprylic acid.

[0107] Linear or branched chain hydrocarbons of natural mineral or synthetic origin include volatile or non-volatile paraffin oils and their derivatives, petrolatum, polydecene, hydrogenated polyisobutene, for example Parleam oil.

[0108] Preferred silicone oils include volatile or non-volatile polymethylsiloxanes (PDMS) having linear or cyclic silicone chains, which are liquid or pasty at room temperature, in particular cyclopolydimethylsiloxanes (cyclomethicones), such as cyclohexasiloxane and cyclopentasiloxane; polydimethylsiloxanes (or dimethicones) containing an alkyl group, an alkoxy group or a phenyl group having 2 to 24 carbon atoms in the middle or at the end of the silicone chain; phenyl silicones, such as phenyltrimethicone, phenyldimethicone, phenyltrimethylsiloxydiphenylsiloxane, diphenyldimethicone, diphenylmethyldiphenyltrisiloxane, 2-phenylethyltrimethylsiloxysilicate, and polymethylphenylsiloxane.

[0109] Preferred fatty alcohols include those having 8 to 26 carbon atoms, such as cetyl alcohol, stearyl alcohol and mixtures thereof (cetylstearyl alcohol), or octyldodecyl ester.

[0110] In a preferred method of the invention, the lipophilic phase comprises a wax selected from Softisan® 100, Softisan® 142, and Softisan® 154, or a combination thereof.

[0111] In a preferred method of the invention, the lipophilic phase comprises an active ingredient. Preferably, the active ingredient is selected from vitamins, minerals, flavor materials, fragrance materials, pro-flavors, pro-fragrances, flavor enhancers, malodor counteractants, nutraceuticals, probiotics, pharmaceuticals, antibacterial agents, antiviral agents, anti-inflammatory agents, antioxidants, insecticides, herbicides, fertilizers, fungicides, insecticides, animal repellents, anti-acne agents, anti-aging agents, skin brighteners, skin emollients, skin moisturizers (e.g., alpha-hydroxy acids or hyaluronic acid), occlusive agents, skin moisturizers, antiperspirants or deodorants, wrinkle control agents, fabric softener actives, surface cleaning actives, skin conditioning agents, hair conditioning agents, sunscreens, dyes, pigments, and adhesives, or combinations thereof.

[0112] Preferably, the pesticide is a natural substitute for synthetic materials, whether it is an insecticide, herbicide, fertilizer, fungicide, insecticide or animal repellent, and is based on plant extracts and / or plant essential oils (EOs) or on components of essential oils, for example, thymol.Preferably, the pesticide is a bio-pesticide.Preferably, the pesticide is suitable for use in formulations for the management and production of plants that can be certified organic by organizations such as the USDA (US Department of Agriculture) or Ecocert in Europe.

[0113] In a particularly preferred method of the invention, the active ingredient is at least one fragrance or flavor material, preferably selected from alcohols, aldehydes, ketones, esters, ethers, acetates, alkenes, nitriles, nitrogen heterocycles, sulfur heterocycles, and Schiff bases.

[0114] The fragrance and flavor materials used in the present invention may be of natural origin (i.e., they are extracted from natural sources and are not synthetically modified in any way).Preferred fragrance or flavor materials of natural origin include nutmeg extract, cardamom extract, ginger extract, cinnamon extract, patchouli oil, geranium oil, orange oil, mandarin oil, orange flower extract, cedarwood, vetiver, lavandin, ylang extract, tuberose extract, sandalwood oil, bergamot oil, rosemary oil, spearmint oil, peppermint oil, lemon oil, lavender oil, citronella oil, chamomile oil, clove oil, sage oil, neroli oil, labdanum oil, eucalyptus oil, verbena oil, mimosa extract, daffodil extract, jasmine extract, frankincense extract, rose extract, vanillin, coffee extract, hops oil, or combinations thereof.Preferably, the fragrance or flavor materials of natural origin are derived from plants. The naturally occurring fragrance or flavor materials may be used alone or in combination, or in combination with synthetic fragrance materials.

[0115] In a preferred method of the present invention, at least one fragrance or flavour material has a vapour pressure of 0.0001 Torr or greater at 25°C.

[0116] In a preferred method of the present invention, at least one fragrance or flavour material has a logP of 3.0 or greater, preferably 3.5 or greater, more preferably 4.0 or greater.

[0117] In a preferred method of the present invention, the at least one fragrance or flavor material has at least two Hansen solubility parameters selected from an atomic dispersion power (δD) of 14-20, a dipole moment (δP) of less than 8, and a hydrogen bond (δH) of 2.5-11.

[0118] In a preferred method of the invention, the at least one fragrance or flavour material is part of a fragrance or flavour.

[0119] Preferably, the fragrance or flavor contains at least 20% by weight, based on the total weight of the fragrance or flavor, of fragrance or flavor materials having a logP of 3.0 or greater, more preferably 3.5 or greater, more preferably 4.0 or greater.

[0120] Preferably, the fragrance or flavour contains at least 40% by weight, based on the total weight of the fragrance or flavour, of fragrance or flavour materials having a logP greater than 3.0, more preferably greater than 3.5, more preferably greater than 4.0.

[0121] Preferably, the fragrance or flavour contains at least 50% by weight, based on the total weight of the fragrance or flavour, of fragrance or flavour materials having a logP greater than 3.0, more preferably greater than 3.5, more preferably greater than 4.0.

[0122] Preferably, the fragrance or flavour contains at least 60% by weight, based on the total weight of the fragrance or flavour, of fragrance or flavour materials having a logP greater than 3.0, more preferably greater than 3.5, more preferably greater than 4.0.

[0123] Preferably, the fragrance or flavour contains at least 10% by weight, preferably at least 30% by weight, more preferably at least 50% by weight, more preferably at least 70% by weight of fragrance or flavour materials of natural origin, based on the total weight of the fragrance or flavour.

[0124] Preferably, the fragrance or flavor contains at least 10% by weight of fragrance or flavor material or essential oil having a biodegradability based on O2 consumption of 60-100%, more preferably 65%, even more preferably 70-100%, even more preferably 75-100%, even more preferably 80-100%, even more preferably 85-100%, and most preferably 90-100%, based on the biological oxygen demand (BOD) relative to the theoretical oxygen demand, measured according to ISO-14851 version 2019 after 28 days. Due to the low water solubility of the fragrance or flavor, the fragrance or flavor can be added to a biodegradation test on an inert support according to ISO 10634 version 2018: Water quality-Preparation and treatment of poorly water-soluble organic compounds for the subsequent evaluation of their biodegradability in an aqueous medium. In addition, the fragrance or flavor can be checked for an inhibitory effect on microorganisms, as detailed in the method.

[0125] Preferably, the fragrance or flavor contains at least 80% by weight, preferably at least 90% by weight, more preferably at least 95% by weight, of fragrance or flavor material having at least two Hansen solubility parameters selected from an atomic dispersion power (δD) of 14 to 20, a dipole moment (δP) of less than 8, and a hydrogen bond (δH) of 2.5 to 11, based on the total weight of the fragrance or flavor.

[0126] Preferably, the fragrance or flavor contains only low levels of materials with alcohol functionality (e.g., primary alcohol functionality). In a preferred method of the invention, the fragrance or flavor contains less than 40% by weight, more preferably less than 20% by weight, of alcohol-containing materials, based on the total weight of the fragrance or flavor. In a particularly preferred method of the invention, the fragrance or flavor does not contain any alcohol-containing materials.

[0127] Preferably the fragrance or flavour material has a high odour impact, which is advantageous as it ensures that even low levels of fragrance are perceived when released from the emulsion.

[0128] In an alternative particularly preferred method of the present invention, the active ingredient is a vitamin or mineral.Preferably, the active ingredient is a vitamin or mineral selected from vitamin A, vitamin B1, vitamin B2, vitamin B3, vitamin B5, vitamin B6, vitamin B7, vitamin B9, vitamin B12, vitamin C, vitamin D, vitamin E, vitamin K, magnesium, sodium, potassium, zinc, iron, calcium, iodine, omega-3, folic acid, thiamine, riboflavin, niacin and phosphorus, or mixtures thereof.More preferably, the active ingredient is vitamin D.

[0129] In preferred methods of the invention, step (f) involves membrane emulsification, high shear mechanical agitation, sonication, high shear mechanical agitation, and / or cavitation.

[0130] In a preferred method of the present invention, the second plant-derived protein hydrogel slurry is diluted with water, preferably deionized water, prior to step (f).

[0131] In a preferred process of the invention the emulsion has a protein solids content of less than 0.9wt%, preferably less than 0.8wt%, preferably less than 0.7wt%, preferably less than 0.6wt%, preferably less than 0.5wt%, preferably less than 0.4wt%, preferably less than 0.3wt%, preferably less than 0.2wt%, preferably less than 0.1wt%, based on the total weight of the emulsion.

[0132] In a preferred method of the invention, the emulsion is substantially free of soluble protein.

[0133] In a preferred method of the invention, the emulsion comprises at least 0.1% by weight, preferably at least 0.5% by weight, of a lipophilic phase, based on the total weight of the emulsion.

[0134] A preferred method of the invention further comprises the step of altering the pH of the plant-derived protein hydrogel slurry so that it differs from the isoelectric point of the plant-derived protein by more than 1 pH unit, preferably by more than 1.5 pH units.

[0135] In a preferred method of the invention, the step of altering the pH of the emulsion involves adding a pH adjusting material to the emulsion. Preferred pH adjusting materials are described above.

[0136] In a preferred method of the invention, the pH of the emulsion after the step of altering the pH of the emulsion is at least 1 pH unit, preferably at least 1.5 pH units, lower than the isoelectric point of the plant-derived protein.

[0137] In an alternative preferred method of the invention, the pH of the emulsion after the step of altering the pH of the emulsion is at least 1 pH unit, preferably at least 1.5 pH units higher than the isoelectric point of the plant derived protein.

[0138] In a preferred method of the invention, the step of altering the pH of the emulsion involves passing the plant-derived protein through its isoelectric point. The isoelectric point of a particular plant-derived protein can be measured using the method described in Helmick et al., Food Biophysics (2021) 16:474-483.

[0139] In a preferred method of the invention, the step of altering the pH of the emulsion involves increasing the pH.

[0140] In a preferred method of the present invention, the pH of the emulsion after the step of modifying the pH of the emulsion is in the range of 5.5 to 7.5, preferably 6.0 to 7.0. Such a pH range is particularly useful in cosmetic formulations that come into contact with the skin during use.

[0141] Without wishing to be bound by theory, it is believed that the protein hydrogel slurry of the present invention has an elongated fine strand morphology, which means that they can easily assemble around the droplets of lipophilic phase to form a stable emulsion.When the pH of the emulsion is changed as described above, as the isoelectric point of the plant-derived protein is approached, these fine strand-like particles are believed to entangle with high packing density, which further aids in the formation of a more stable emulsion.Furthermore, when the pH of the emulsion passes through the isoelectric point of the plant-derived protein at a sufficiently slow rate, increased aggregation can occur, which also contributes to increased emulsion stability.

[0142] The present invention also provides an emulsion obtained or obtainable by the above process.

[0143] The present invention also provides an emulsion comprising a lipophilic phase dispersed in a plant-derived protein hydrogel slurry comprising a plant-derived protein, the emulsion having less than 1% protein solids by weight based on the total weight of the emulsion.

[0144] The emulsion of the present invention is a Pickering emulsion.However, in contrast to conventional Pickering emulsions, the Pickering emulsion of the present invention is not composed of nanoparticles (average diameter less than 100 nm), which may cause concerns about human health safety due to their very small size.In addition, most conventional Pickering emulsions are not of plant origin, and many use inorganic particles such as fumed silica, which means that they cannot be used in "clean label" and organic products.

[0145] Preferred emulsions of the invention have a protein solids content of less than 0.9 wt.%, preferably less than 0.8 wt.%, preferably less than 0.7 wt.%, preferably less than 0.6 wt.%, preferably less than 0.5 wt.%, preferably less than 0.4 wt.%, preferably less than 0.3 wt.%, preferably less than 0.2 wt.%, preferably less than 0.1 wt.%, based on the total weight of the emulsion.

[0146] In a preferred emulsion of the present invention, the plant-derived protein is obtained from broad beans, mung beans, peas, rice, potato, rapeseed, lentils, chickpeas, sunflower seeds, pumpkin seeds, flax, chia, canola, lupin, alfalfa, moringa, wheat, corn zein or sorghum, preferably the plant protein is selected from pea protein, potato protein, rapeseed protein, lentil protein, chickpea protein, broad bean protein, mung bean protein, sunflower seed protein, pumpkin seed protein, flax protein, chia protein, canola protein, lupin protein, alfalfa protein, moringa protein and / or rice protein. More preferably, the plant-derived protein is pea protein and / or potato protein. Such proteins are considered to be hypoallergenic proteins.

[0147] In a preferred emulsion of the present invention, the plant-derived protein is pretreated with an organic acid. Preferably, the organic acid is acetic acid, lactic acid, formic acid, gluconic acid, propionic acid, α-hydroxy acid, and / or β-hydroxy acid, preferably acetic acid or lactic acid. Preferred α-hydroxy acids include glycolic acid, acetic acid, lactic acid, malic acid, citric acid, and / or tartaric acid, preferably acetic acid or lactic acid. Preferred β-hydroxy acids include β-hydroxypropionic acid, β-hydroxybutyric acid, β-hydroxyβ-methylbutyric acid, 2-hydroxybenzoic acid, and carnitine. In a particularly preferred emulsion of the present invention, the organic acid is acetic acid or lactic acid.

[0148] In preferred emulsions of the present invention, the plant derived protein hydrogel slurry has a diameter of less than 100 μm, preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, more preferably less than 5 μm, more preferably less than 1 μm, as measured by laser diffraction. 50 has.

[0149] In preferred emulsions of the present invention, the plant derived protein hydrogel slurry has a diameter, as measured by laser diffraction, of less than 250 μm, preferably less than 100 μm, more preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm. 90 has.

[0150] In a preferred emulsion of the invention, the solid material of the plant-derived protein hydrogel slurry has a biodegradation rate based on O2 consumption of 60-100%, preferably 65-100%, more preferably 70-100%, more preferably 75-100%, more preferably 80-100%, more preferably 85-100%, and even more preferably 90-100%, based on the biological oxygen demand (BOD) as a percentage of the theoretical oxygen demand, when measured according to ISO-14851 version 2019 after 28 days. ISO-14851 version 2019 describes a method to measure the biodegradability of materials in natural aqueous environments using biological oxygen demand in a closed respirometer. This is accomplished by exposing the material under laboratory conditions in an aqueous standard test medium to an inoculum from a previously unexposed, unadapted activated sludge. The measured value is calculated as a percentage of the theoretical oxygen demand calculated from the molecular formula. An internal standard of microcrystalline cellulose is also tested and if its % biodegradation is greater than 60% at the end of the test, the test is valid.

[0151] In preferred emulsions of the invention, the lipophilic phase comprises a solvent, a butter or a wax.

[0152] In preferred emulsions of the invention, the lipophilic phase comprises a solvent. Preferably, the solvent is a solvent of low volatility (e.g., having a vapor pressure of less than 0.1 Torr at 25° C., preferably less than 0.01 Torr at 25° C., preferably less than 0.001 Torr at 25° C.).

[0153] Preferably, the solvent has low or no odor.

[0154] Preferably, the solvent has at least two Hansen solubility parameters selected from atomic dispersion forces (δD) less than 20, dipole moment (δP) less than 8, and hydrogen bonding (δH) less than 11. More preferably, the solvent has at least two Hansen solubility parameters selected from atomic dispersion forces (δD) less than 20, dipole moment (δP) less than 4, and hydrogen bonding (δH) less than 5.

[0155] Preferably, the solvent contains only low levels of materials with alcohol functionality (e.g., primary alcohol functionality). In preferred emulsions of the invention, the solvent contains less than 40% by weight, more preferably less than 20% by weight, of alcohol-containing materials, based on the total weight of the solvent. In particularly preferred emulsions of the invention, the solvent is free of alcohol-containing materials.

[0156] In preferred emulsions of the invention, the lipophilic phase comprises a solvent selected from fatty acid esters, fatty acids, linear or branched hydrocarbons of natural mineral or synthetic origin, fatty alcohols or ethers thereof, vegetable oils, silicone oils, phthalate esters, rosin resins, diols, triols, benzyl benzoate, triethyl citrate and triacetin, or combinations thereof.

[0157] Preferred fatty acid esters, fatty acids, linear or branched hydrocarbons of natural mineral or synthetic origin, silicone oils, vegetable oils and fatty alcohols are described above.

[0158] Preferably, the solvent is Miglyol® 840, Miglyol® 812 N, Miglyol® 829, Miglyol® 829 ECO, Miglyol® Coco 810, Miglyol® 810 N, Miglyol® 128, Miglyol® 808, Miglyol® T-C7, Miglyol® 8810, Miglyol® PPG 810, Miglyol® OE, Miglyol® DO, and Miglyol® 818, Abalyn®, limonene, benzyl benzoate, diethyl phthalate, isopropyl myristate, triethyl citrate, dipropylene glycol, and propylene glycol, triacetin, glycerin, 1,3 propanediol, or combinations thereof, preferably Miglyol® 812 N.

[0159] In preferred emulsions of the present invention, the lipophilic phase comprises a wax selected from Softisan® 100, Softisan® 142, and Softisan® 154, or combinations thereof.

[0160] In the preferred emulsion of the present invention, the lipophilic phase comprises an active ingredient.Preferably, the active ingredient is selected from vitamins, minerals, flavor materials, fragrance materials, pro-flavors, pro-fragrances, flavor enhancers, malodor counteractants, nutraceuticals, probiotics, pharmaceuticals, antibacterial agents, antiviral agents, anti-inflammatory agents, antioxidants, insecticides, herbicides, fertilizers, fungicides, insecticides, animal repellents, anti-acne agents, anti-aging agents, skin brighteners, skin emollients, skin moisturizers (e.g., alpha-hydroxy acids or hyaluronic acid), occlusive agents, skin moisturizers, antiperspirants or deodorants, wrinkle control agents, fabric softener actives, surface cleaning actives, skin conditioning agents, hair conditioning agents, sunscreens, dyes, pigments, and adhesives, or combinations thereof.

[0161] Preferably, the pesticide, whether insecticide, herbicide, fertilizer, fungicide, insecticide or animal repellent, is a natural alternative to synthetic materials and is based on plant extracts and / or plant essential oils (EOs), or components of essential oils, for example, based on thymol.Preferably, the pesticide is a biopesticide.Preferably, the pesticide is suitable for use in formulations for the management and production of plants that can be certified organic by organizations such as the USDA (US Department of Agriculture) or Ecocert in Europe.

[0162] In particularly preferred emulsions of the present invention, the active ingredient is at least one fragrance or flavor material, preferably selected from alcohols, aldehydes, ketones, esters, ethers, acetates, alkenes, nitriles, nitrogen heterocycles, sulfur heterocycles, and Schiff bases.

[0163] The fragrance and flavor materials used in the present invention may be of natural origin (i.e., they are extracted from natural sources and are not synthetically modified in any way).Preferred fragrance or flavor materials of natural origin include nutmeg extract, cardamom extract, ginger extract, cinnamon extract, patchouli oil, geranium oil, orange oil, mandarin oil, orange flower extract, cedarwood, vetiver, lavandin, ylang extract, tuberose extract, sandalwood oil, bergamot oil, rosemary oil, spearmint oil, peppermint oil, lemon oil, lavender oil, citronella oil, chamomile oil, clove oil, sage oil, neroli oil, labdanum oil, eucalyptus oil, verbena oil, mimosa extract, daffodil extract, jasmine extract, frankincense extract, rose extract, vanillin, coffee extract, hops oil, or combinations thereof.Preferably, the fragrance or flavor materials of natural origin are derived from plants. The naturally occurring fragrance or flavor materials may be used alone or in combination, or in combination with synthetic fragrance materials.

[0164] In preferred emulsions of the present invention, at least one fragrance or flavor material has a vapor pressure of 0.0001 Torr or greater at 25°C.

[0165] In preferred emulsions of the present invention, at least one fragrance or flavor material has a logP of 3.0 or greater, preferably 3.5 or greater, more preferably 4.0 or greater.

[0166] In preferred emulsions of the present invention, at least one fragrance or flavor material has at least two Hansen solubility parameters selected from an atomic dispersion power (δD) of 14-20, a dipole moment (δP) of less than 8, and a hydrogen bond (δH) of 2.5-11.

[0167] In preferred emulsions of the present invention, at least one fragrance or flavor material is part of a fragrance or flavor.

[0168] Preferably, the fragrance or flavor contains at least 20% by weight, based on the total weight of the fragrance or flavor, of fragrance or flavor materials having a logP of 3.0 or greater, more preferably 3.5 or greater, more preferably 4.0 or greater.

[0169] Preferably, the fragrance or flavour contains at least 40% by weight, based on the total weight of the fragrance or flavour, of fragrance or flavour materials having a logP greater than 3.0, more preferably greater than 3.5, more preferably greater than 4.0.

[0170] Preferably, the fragrance or flavour contains at least 50% by weight, based on the total weight of the fragrance or flavour, of fragrance or flavour materials having a logP greater than 3.0, more preferably greater than 3.5, more preferably greater than 4.0.

[0171] Preferably, the fragrance or flavour contains at least 60% by weight, based on the total weight of the fragrance or flavour, of fragrance or flavour materials having a logP greater than 3.0, more preferably greater than 3.5, more preferably greater than 4.0.

[0172] Preferably, the fragrance or flavour contains at least 10% by weight, preferably at least 30% by weight, more preferably at least 50% by weight, more preferably at least 70% by weight of fragrance or flavour materials of natural origin, based on the total weight of the fragrance or flavour.

[0173] Preferably, the fragrance or flavor contains at least 10% by weight of fragrance or flavor material or essential oil having a biodegradability based on O2 consumption of 60-100%, preferably 65%-100%, more preferably 70-100%, more preferably 75-100%, more preferably 80-100%, more preferably 85-100%, even more preferably 90-100%, based on the ratio of biological oxygen demand (BOD) to theoretical oxygen demand, measured according to ISO-14851 version 2019 after 28 days. Since the fragrance or flavor has low water solubility, the fragrance or flavor can be added to a biodegradation test on an inert support according to ISO 10634 version 2018: Water quality - Preparation and treatment of poorly water-soluble organic compounds for the subsequent evaluation of their biodegradability in an aqueous medium. In addition, the fragrance or flavor can be checked for an inhibitory effect on microorganisms, as detailed in the method.

[0174] Preferably, the fragrance or flavor contains at least 80% by weight, preferably at least 90% by weight, more preferably at least 95% by weight, of fragrance or flavor material having at least two Hansen solubility parameters selected from an atomic dispersion power (δD) of 14 to 20, a dipole moment (δP) of less than 8, and a hydrogen bond (δH) of 2.5 to 11, based on the total weight of the fragrance or flavor.

[0175] Preferably, the fragrance or flavor contains only low levels of materials with alcohol functionality (e.g., primary alcohol functionality). In a preferred method of the invention, the fragrance or flavor contains less than 40% by weight, more preferably less than 20% by weight, of alcohol-containing materials, based on the total weight of the fragrance or flavor. In a particularly preferred emulsion of the invention, the fragrance or flavor is free of alcohol-containing materials.

[0176] Preferably the fragrance or flavour material has a high odour impact, which is advantageous as it ensures that even low levels of fragrance are perceived when released from the emulsion.

[0177] In an alternative particularly preferred emulsion of the present invention, the active ingredient is a vitamin or mineral.Preferably, the active ingredient is a vitamin or mineral selected from vitamin A, vitamin B1, vitamin B2, vitamin B3, vitamin B5, vitamin B6, vitamin B7, vitamin B9, vitamin B12, vitamin C, vitamin D, vitamin E, vitamin K, magnesium, sodium, potassium, zinc, iron, calcium, iodine, omega-3, folic acid, thiamine, riboflavin, niacin and phosphorus, or mixtures thereof.More preferably, the active ingredient is vitamin D.

[0178] In a preferred emulsion of the present invention, the plant-derived protein hydrogel slurry comprises pea protein and the active ingredient is vitamin D.

[0179] Preferred emulsions of the invention contain at least 0.1% by weight, preferably at least 0.5% by weight, of a lipophilic phase, based on the total weight of the emulsion.

[0180] In preferred emulsions of the present invention, the pH of the emulsion is such that it differs from the isoelectric point of the plant derived protein by more than 1 pH unit, preferably by more than 1.5 pH units.

[0181] Thus, in preferred emulsions of the invention, the pH of the emulsion is at least 1 pH unit, preferably at least 1.5 pH units, below the isoelectric point of the plant-derived protein.

[0182] In an alternative preferred emulsion of the present invention, the pH of the emulsion is at least 1 pH unit, preferably at least 1.5 pH units, higher than the isoelectric point of the plant derived protein.

[0183] In preferred emulsions of the present invention, the pH of the emulsion is in the range of 5.5 to 7.5, preferably 6.0 to 7.0. Such a pH range is particularly useful in cosmetic formulations that come into contact with the skin during use.

[0184] In preferred emulsions of the invention, the plant-derived protein has a protein secondary structure comprising at least 40% intermolecular β-sheets, at least 50% intermolecular β-sheets, at least 60% intermolecular β-sheets, at least 70% intermolecular β-sheets, at least 80% intermolecular β-sheets, or at least 90% intermolecular β-sheets, wherein the % intermolecular β-sheet content is measured by FTIR.

[0185] The present invention also relates to a composition comprising the emulsion prepared according to the above method. Preferably, the composition is a cosmetic composition, a fragrance composition (e.g., a fine fragrance or a laundry scent booster), a beverage composition, an oral care composition, a pharmaceutical composition, or an agricultural composition.

[0186] The present invention also relates to the use of the plant-derived protein hydrogel slurry as an emulsifier in a composition, preferably a cosmetic composition, a fragrance composition (e.g., a fine fragrance or a laundry scent booster), a beverage composition, an oral care composition, a pharmaceutical composition, or an agricultural composition. [Brief description of the drawings]

[0187] [Figure 1]FIG. 1 shows particle size distribution of pea protein hydrogel slurries of Examples 1A, 1B and 1C and the pea protein mixture of Example 2A. [Diagram 2] 1 shows the emulsion size distribution of emulsions of Examples 3A, 3B, 3C and 3D. [Diagram 3] 1 shows the emulsions of Example 3A (in triplicate) after being subjected to stress conditions. [Figure 4] 1 shows the emulsions of Example 3B (in triplicate) after being subjected to stress conditions. [Diagram 5] 1 shows the emulsions of Example 3C (in triplicate) after being subjected to stress conditions. [Figure 6] 1 shows the emulsions of Example 3D (in triplicate) after being subjected to stress conditions. [Figure 7] 1 shows the emulsion size distribution of emulsions of Examples 3E, 3F, 3G and 3H. [Figure 8] 1 shows the emulsions of Example 3E (in triplicate) after being subjected to stress conditions. [Figure 9] 1 shows the emulsions of Example 3F (in triplicate) after being subjected to stress conditions. [Figure 10] 1 shows the emulsions of Example 3G (in triplicate) after being subjected to stress conditions. [Figure 11] 1 shows the emulsions of Example 3H (in triplicate) after being subjected to stress conditions. [Figure 12] FIG. 1 shows particle size distribution of the pea protein hydrogel slurry of Example 4. [Figure 13] 1 shows the emulsion size distribution of the emulsions of Examples 5A and 5B. [Figure 14] 1 shows the emulsions of Example 5A (in triplicate) after being subjected to stress conditions. [Figure 15] 1 shows the emulsions of Example 5B (in triplicate) after being subjected to stress conditions. EXAMPLES

[0188] material Pea Protein Isolate (PPI) (80% protein) was purchased from Cambridge Commodities Ltd.

[0189] Lactic acid (food grade, ≧80%) was purchased from Cambridge Commodities Ltd.

[0190] Acetic acid (glacial acetic acid 99%) was purchased from Fisher Scientific.

[0191] Sodium benzoate was purchased from Fisher Scientific.

[0192] Potassium hydroxide (KOH) (>85%) was purchased from Sigma Aldrich.

[0193] Miglyol® 812N was purchased from IOI Oleochemical.

[0194] Hydrochloric acid was purchased from Sigma Aldrich.

[0195] Geraniol was purchased from Carvansons Ltd.

[0196] Undecavertol was purchased from Carvansons Ltd.

[0197] Delta damascone was purchased from Carvansons Ltd.

[0198] Dodecanenitrile was purchased from Carvansons Ltd.

[0199] Thymol was purchased from Fisher Scientific.

[0200] Measurement method viscosity Viscosity measurements were performed using an Anton Paar MCR 92 rheometer with a 50 mm plate and 1 degree angle at 20°C for 64 s. -1 The measurements were performed using a plate and cone measurement geometry with a constant shear rate of 100 Hz. Measurements were performed within 1 hour of sample preparation.

[0201] pH pH measurements were performed using a Mettler Toledo FiveEasy pH meter.

[0202] particle size Particle size measurements were performed using laser diffraction on an Anton Paar PSA 1190.

[0203] The measurements were performed by diluting the plant-derived protein hydrogel slurry with an aqueous solution containing acetic or lactic acid adjusted to the same pH. The slurry was diluted to the required concentration to have the desired optical density for the measurements (usually 5-15% obscuration). 50 is for the volume distribution. d of the volume distribution 90 Values ​​can also be obtained in this manner using laser diffraction.

[0204] Emulsion Size Particle size measurements were performed using laser diffraction on an Anton Paar PSA 1190.

[0205] The measurements were performed by diluting the emulsion to the required concentration in water adjusted to the same pH so as to have the desired optical density for the measurements (usually 5-15% obscuration). 50 is for the volume distribution. d of the volume distribution 90 Values ​​can also be obtained in this manner using laser diffraction.

[0206] Protein Solids Protein solids were measured as the mass remaining upon drying. Approximately 5 g of the plant-derived protein hydrogel slurry was pipetted into a small polypropylene dish and the mass was accurately recorded. The dish was placed in a 40° C. oven to dry overnight. The dry mass was measured immediately after removal from the oven and the solids of the protein hydrogel were calculated as a percentage of the initial wet mass.

[0207] Example 1: Preparation of pea protein hydrogel slurry a) Protein hydrogel formation A 450 g mixture was prepared consisting of 12.5% ​​(w / w) pea protein isolate in 40% (w / w) lactic acid solution.

[0208] The mixture was then heated in a water bath at 80° C. for 30 min, followed by a brief sonication to break up large colloidal aggregates (Bandelin HD4200 (200 W, 20 kHz, probe TS113, 80% amplitude)), after which a clear solution was obtained. The applied energy was 100 kJ.

[0209] The solution was then poured into a 220 mm Petri dish and left to cool at 5° C. overnight to yield a free-standing protein hydrogel.

[0210] b) Application of shear to protein hydrogels Shear was then applied to the hydrogel as follows: The protein hydrogel was cut into cubes of approximately 1 cm by a low shear cutting process. The cubes were placed inside a 75 μm filter bag, which was then submerged in a bucket containing 5 L of deionized water. This formed a coarse protein hydrogel slurry inside the filter bag. The hydrogel cubes were allowed to soak for 1.5 hours with occasional gentle stirring. This process was performed to reduce the concentration of acetic acid in the hydrogel by diffusion into the continuous aqueous phase. It was repeated five more times until the final pH of the aqueous solution was 3.3-3.5.

[0211] The distorted gel cubes (approximately 350 g) were transferred to a 500 mL bottle with 0.1 wt. % sodium benzoate and exposed to probe sonication (Bandelin HD4200 (200 W, 20 kHz, probe TS113, 40% amplitude) in a high shear step, the applied energy was 0.1 kJ per gram of distorted gel cube) to form a homogenous low-viscosity dispersion of fine fragments of the protein.

[0212] Steps a and b were carried out in duplicate to produce two samples of the slurry, which were combined into a single sample and filtered through a 75 μm sieve. The pH of the combined filtered sample was 3.52. The viscosity of the slurry was 64 s -1 The viscosity was 16.3 cps at 100°C. The solids content was measured to be 4.84% by weight.

[0213] The prepared slurry was divided into three portions.

[0214] The first portion (Example 1A) was adjusted to pH 3.0 with 85% lactic acid. The particle size of the dispersion was measured and the full distribution is shown in Figure 1. Example 1A had a particle size distribution of d 50 is 40.1 μm, and d 90 was 85.2 μm.

[0215] A second portion (100 mL sample, Example 1B) was adjusted to pH 3.0 with 85% lactic acid and sonicated (0.18 kJ / mL sonication) to further reduce the particle size distribution. The particle size of the dispersion was measured and the full distribution is shown in Figure 1. Example 1B had a particle size distribution of d 50 is 1.30 μm, and d 90 was 38.4 μm.

[0216] The third portion (100 mL sample, Example 1C) was adjusted to pH 3.0 with 85% lactic acid and sonicated (3.44 kJ / mL sonication) to further reduce the particle size distribution. The particle size of the dispersion was measured and the full distribution is shown in Figure 1. Example 1C had a particle size distribution of d 50 is 0.36 μm, and d 90 was 0.94 μm.

[0217] Example 2: Preparation of a pea protein mixture Example 2A was prepared by suspending 5.03 g of PPI in 94.6 g of deionized (DI) water with 0.1 g of sodium benzoate. The pH was adjusted to 3.0 with 1 M HCl, and the sample was sonicated to produce a small particle size (d less than 0.5 μm) comparable to that of Example 1C. 50 ) was achieved. The ultrasonic treatment energy was typically about 1.5 kJ / g. The particle size of the mixture was measured and the full distribution is shown in Figure 1. Example 2A was d 50 is 0.41 μm, and d 90 The viscosity of the mixture was 64s -1 The result was 3.4cps.

[0218] Example 3: Preparation of emulsions and stability testing Four different emulsions with 0.1% protein solids were prepared using the protein slurries of Examples 1A-C and the protein mixture of Example 2A according to the formulations shown in Table 1 below.

[0219] [Table 1]

[0220] If necessary, the pH of each aqueous phase was readjusted to pH 3.0 using 85% lactic acid (for the slurries of Examples 1A, 1B and 1C) and 1 M HCl (for the mixture of Example 2A). For each emulsion, 200 mL batches were prepared by pouring the oil phase into the aqueous phase and homogenizing the resulting mixture with a high shear mixer (Ultraturrax) at 20,000 rpm for 1 minute.

[0221] Each of the four different emulsions was divided into two portions. The first portion was adjusted to pH 7 using 10 wt % KOH aqueous solution under constant stirring using a magnetic stirrer. A summary of the four emulsions is shown in Table 2 below. The overall size distribution of the emulsion droplets was very similar for all four emulsions and is shown in Figure 2.

[0222] [Table 2]

[0223] Each emulsion was left at room temperature for 24-72 hours, divided into three centrifuge tubes (12 g each), and then centrifuged at 4347 g for 1 hour 47 minutes to separate the oil that was not stabilized by proteins. This test therefore gave an indication of the stability of the emulsions under these stress conditions. The results are shown in Figures 3-6. The separation index was calculated by dividing the volume of the upper oil layer by the volume of the emulsion and is shown in Table 2.

[0224] Figure 6 shows that Example 3D clearly separated into a bottom water layer, a middle protein-derived emulsion layer, and a large upper oil layer with a separation index of 1.5, demonstrating that the untreated PPI protein is unable to maintain a stable emulsion of oil, indicating that long-term stability in product applications is not expected.

[0225] Figure 5 shows that Example 3C formed only a bottom water layer, a middle protein-derived emulsion layer, and a very small top oil layer, with a separation index of 0.11. This is clearly an improvement in terms of emulsion stability compared to Example 3D made with untreated PPI. Without wishing to be bound by theory, it is believed that the protein aggregates in the protein hydrogel slurry of the present invention have elongated fine strand morphology, which allows them to form a tighter structural layer around the oil droplets, resulting in a more stable emulsion even when the particle size distribution is very similar.

[0226] Figures 3 and 4 show that Examples 3A and 3B formed a bottom water layer and an upper protein-derived emulsion layer, respectively, and the oil remained mostly emulsified by the protein hydrogel (as only a very small upper oil layer was observed). The separation index was both 0.13. This demonstrates that the protein hydrogel slurry with larger particle size than in Example 3C can still maintain most of the emulsified oil under these stress conditions, indicating that long-term stability in product applications can be expected.

[0227] Examples 3A, 3B and 3C demonstrate that low levels of acid-treated protein hydrogels with small particle size can emulsify high levels of oil in near-neutral aqueous formulations.Therefore, it is expected that the emulsions of the present invention will have useful applications in several different product formulations, such as cosmetic formulations.

[0228] A second portion of the emulsions prepared using the protein slurries of Examples 1A, 1B, and 1C and the protein mixture of Example 2A were left without pH adjustment. A summary of the four emulsions is shown below in Table 3. The overall size distribution of the emulsion droplets was very similar for all four emulsions and is shown in Figure 7.

[0229] [Table 3]

[0230] Each emulsion was left at room temperature for 24-72 hours, divided into three centrifuge tubes (12 g each), and then centrifuged at 4347 g for 1 hour 47 minutes to separate the oil that was not stabilized by proteins. This test therefore gave an indication of the stability of the emulsions under these stress conditions. The results are shown in Figures 8-10. The separation index was calculated by dividing the volume of the top oil layer by the volume of the emulsion and is shown in Table 3.

[0231] Figures 8-10 show that Examples 3E, 3F and 3G all formed a bottom aqueous layer and a top protein-derived emulsion layer, and the oil remained fully emulsified by the protein hydrogel. Thus, the separation index was 0 in all three cases. This demonstrates that the plant-derived protein hydrogel slurries of the present invention are able to keep the oil emulsified under these stress conditions at three different particle size distributions, indicating that long-term stability in product applications can be expected.

[0232] Figure 11 shows that Example 3H formed a bottom water layer, a middle protein-derived emulsion layer in which most of the oil remained emulsified by the protein hydrogel, and a small upper oil layer. The separation index was calculated to be 0.03. This demonstrates that the untreated PPI protein cannot maintain a completely stable emulsion of oil, indicating that long-term stability in product applications is difficult for products with acidic environments.

[0233] Without wishing to be bound by theory, it is believed that at acidic pH, the amorphous structure of untreated PPI can stabilize the oil droplets by agglomerating at the oil droplet interface. However, this is less effective than the stabilizing effect of the elongated fine strand morphology of the acid-treated protein hydrogel slurry of the present invention (which forms a more coherent structural layer around the oil droplets). Thus, untreated PPI can form an emulsion, but it is not as stable as that formed by the acid-treated protein hydrogel slurry. When the pH is increased above the isoelectric point of pea protein, the untreated PPI aggregates form a non-uniform layer and can no longer stabilize the oil droplet interface. However, under similar conditions, the acid-treated protein retains its morphology to maintain a stable layer at the oil droplet interface. As a result, in an industrial-scale manufacturing process where the pH of the product can change during processing, it is expected that the acid-treated protein emulsion of the present invention will be stable throughout, while emulsions with untreated PPI will not be stable.

[0234] Example 4 - Preparation of Protein Hydrogel Slurry with Acetic Acid a) Preparation of protein hydrogels 1120g of reverse osmosis (RO) water was added to a 2 litre stainless steel vessel and 216g of pea protein isolate was added. The vessel was placed in a 92°C water bath and mixed at 1500 rpm using an overhead stirrer. After stirring for 3 minutes, 480g of glacial acetic acid was added. The mixture was stirred at 1500 rpm for 15 minutes and then at 1200 rpm for 30 minutes, allowing the temperature of the mixture to exceed 85°C for at least 10 minutes. The mixture was poured into a tray to a depth of approximately 10mm and left at room temperature overnight.

[0235] b) Application of shear to protein hydrogels The hydrogel was then sheared as follows: The protein hydrogel was cut into approximately 1 cm cubes by a low shear cutting process. The cubes were divided between two 75 micron filter bags and then each was submerged in a bucket containing 16 L of RO water. This formed a coarse protein hydrogel slurry in the filter bag. The hydrogel cubes were soaked for 90-150 minutes while being stirred with an overhead stirrer at 600-800 rpm. This step was performed to reduce the concentration of acetic acid in the hydrogel by diffusion into the continuous water phase. The pH of the wash water was then measured and if it was above 3.2, soaking was continued for another 30 minutes. If it was below 2.9, half of the water was drained and replaced with fresh RO water and soaking was then continued for another 30 minutes. The filter bags were then hung over a bucket to drain for 5 minutes. The washed gel from both filter bags was transferred to a 5 liter beaker and homogenized using a Silverson mixer at 5000 rpm for 5 minutes, 6000 rpm for 5 minutes, and 7000 rpm for 5 minutes. The smooth slurry was then transferred to 1 L Nalgene bottles (800 g each) and exposed to high shear sonication (Hielscher UP500Hdt) with shaking every 75 kJ until 250 kJ was applied while cooling on ice. The hydrogel slurry was then passed through a 200 micron sieve before use.

[0236] The pH of the filtered sample was 2.9. Protein solids were measured according to the enclosed method and were 9.5% by weight. The particle size of the slurry was measured according to the enclosed method and the full particle size distribution of the dispersion is shown in Figure 12. 50 is reported to be 11.0 μm, and d 90 was reported to be 28.8 μm.

[0237] Example 5: Preparation and stability testing of emulsions with fragrance and thymol Fragrance A was prepared using the fragrance materials in Table 4 and then mixed with Miglio® 1812N in an 80:20 weight ratio.

[0238] [Table 4]

[0239] Two different emulsions with 0.9% protein solids were prepared using the protein slurry of Example 4 according to the formulations shown in Table 5 below.

[0240] [Table 5]

[0241] For each emulsion, a 200 mL batch was prepared by pouring the oil phase into the water phase and homogenizing the resulting mixture at 10,000 rpm for 5 minutes using a high shear mixer Silverson L5M-A. The overall size distribution of the emulsion droplets was very similar for both emulsions and is shown in Figure 13.

[0242] [Table 6]

[0243] Each emulsion was left at room temperature for 24-72 hours, divided into three centrifuge tubes (12 g each), and then centrifuged at 4347 g for 1 hour 47 minutes to separate the oil that was not stabilized by the protein. Thus, this test provided an indication of the stability of the emulsion under these stress conditions. The results are shown in Figures 14 and 15 for Examples 5A and 5B, respectively, and both examples formed a bottom water layer and a top protein-derived emulsion layer, with the oil remaining fully emulsified by the protein hydrogel. The separation index was calculated by dividing the volume of the oil in the top layer by the volume of the emulsion, and is shown in Table 6. For both Examples 5A and 5B, no separate oil phase was formed, and therefore the separation index was 0 for both, demonstrating that the plant-derived protein hydrogel slurries of the present invention are capable of retaining a variety of oils emulsified under these stress conditions, indicating that long-term stability in product applications can be expected.

[0244] Example 6: Coating of fragrance emulsion onto cards The emulsion of Example 5A was further diluted to 1% by weight of Fragrance A and coated onto 210 gsm white card. A piece of card measuring approximately 14 x 21 cm was clipped to a hard aluminum sheet and 20 mL of the diluted emulsion was applied. A 300 μm spiral bar coater (Elcometer) was used to coat the card and remove excess emulsion.

[0245] The cards were dried overnight in a fume cupboard and cut into 5×9 cm pieces for olfactory evaluation by an expert panel according to the following scale:

[0246] [Table 7]

[0247] An average rating of 3 indicated a medium fragrance intensity with fruity, sweet, orange peel characteristics.

Claims

1. 1. A method for the preparation of an emulsion, comprising: (a) forming a solution comprising one or more plant-derived proteins in a solvent system, the solvent system comprising miscible co-solvents, a first co-solvent increasing the solubility of the plant-derived proteins and a second co-solvent decreasing the solubility of the plant-derived proteins; (b) inducing the protein in the solution to undergo a sol-gel transition to form a plant-derived protein hydrogel; (c) subjecting the plant-derived protein hydrogel to a first shearing step to form a first plant-derived protein hydrogel slurry; (d) subjecting the first plant-derived protein hydrogel slurry to a solvent reduction step to form a washed plant-derived protein hydrogel slurry; (e) subjecting the washed plant-derived protein hydrogel slurry to a second shearing step to form a second plant-derived protein hydrogel slurry; (f) dispersing a lipophilic phase in the second plant-derived protein hydrogel slurry to form an emulsion, the emulsion has a protein solids content of less than 1 wt. %, based on the total weight of the emulsion, and the second plant-derived protein hydrogel slurry has a d of less than 250 μm, preferably less than 100 μm, more preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, as measured by laser diffraction. ９０ and forming a

2. 2. The method of claim 1, wherein the plant-derived protein is selected from pea protein, potato protein, rapeseed protein, lentil protein, chickpea protein, fava bean protein, mung bean protein, sunflower seed protein, pumpkin seed protein, flax protein, chia protein, canola protein, lupin protein, alfalfa protein, moringa protein and / or rice protein, preferably selected from pea protein and / or potato protein.

3. 3. The method of claim 1 or 2, wherein the first co-solvent is an organic acid, preferably the organic acid is acetic acid, lactic acid, formic acid, gluconic acid, propionic acid, an α-hydroxy acid, and / or a β-hydroxy acid, more preferably acetic acid or lactic acid.

4. 3. The method of claim 1 or 2, wherein the second co-solvent is selected from water, ethanol, and / or ethyl acetate, more preferably selected from water and / or ethanol, even more preferably water.

5. 3. The method of claim 1 or 2, wherein in step (b), the protein solution is heated to a first temperature higher than the sol-gel transition temperature of the one or more plant-derived protein solutions and then reduced to a second temperature lower than the sol-gel transition temperature of the one or more plant-derived protein solutions to form a hydrogel.

6. 3. The method of claim 1 or 2, wherein the first shearing step involves fragmenting the plant-derived protein hydrogel into fragments, and preferably the fragments produced in the first shearing step have a particle size, as measured by optical microscopy, in the range of from 1 mm to 100 mm, preferably from 1 mm to 50 mm, preferably from 1 mm to 30 mm, more preferably from 10 mm to 30 mm, more preferably from 15 mm to 30 mm, and even more preferably from 20 mm to 30 mm.

7. The solvent reduction step (i) contacting the first plant-derived protein hydrogel slurry with a non-solubilizing solvent; (ii) separating the first plant-derived hydrogel slurry from the non-solubilizing solvent to obtain a washed plant-derived protein hydrogel slurry; (iii) optionally repeating steps (i) and (ii).

8. The second shearing step involves further fragmenting the plant-derived protein hydrogel, preferably by: The second plant-derived protein hydrogel slurry has a d of less than 100 μm, preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, more preferably less than 5 μm, more preferably less than 1 μm, as measured by laser diffraction. ５０ 3. The method of claim 1 or 2, comprising:

9. 3. The method of claim 1 or 2, wherein the second plant-derived protein hydrogel slurry is subjected to a pH adjustment step between steps (e) and (f).

10. 3. The method of claim 1 or 2, wherein the lipophilic phase comprises a solvent, a butter, or a wax.

11. 11. The method of claim 10, wherein the lipophilic phase comprises a solvent selected from fatty acid esters, fatty acids, linear or branched hydrocarbons of natural mineral or synthetic origin, fatty alcohols or ethers thereof, vegetable oils, silicone oils, phthalate esters, rosin resins, diols, triols, benzyl benzoate, triethyl citrate and triacetin, or combinations thereof.

12. 3. The method of claim 1 or 2, wherein the lipophilic phase comprises an active ingredient, the active ingredient preferably being selected from vitamins, minerals, flavor materials, fragrance materials, pro-flavors, pro-fragrances, flavor enhancers, malodor counteractants, nutraceuticals, probiotics, pharmaceuticals, antibacterial agents, antivirals, anti-inflammatory agents, antioxidants, insecticides, herbicides, fertilizers, fungicides, insecticides, animal repellents, anti-acne agents, anti-aging agents, skin brighteners, emollients, skin moisturizers, occlusive agents, skin moisturizers, antiperspirants or deodorants, wrinkle control agents, fabric softener actives, surface cleaning actives, skin conditioning agents, hair conditioning agents, sunscreens, dyes, pigments, and adhesives, or combinations thereof.

13. the active ingredient is at least one fragrance or flavor material; the at least one fragrance or flavor material has a vapor pressure of 0.0001 Torr or greater at 25°C; and / or 13. The method of claim 12, wherein said at least one fragrance or flavor material has a log P of 3.0 or greater, preferably 3.5 or greater, more preferably 4.0 or greater.

14. 13. The method of claim 12, wherein the active ingredient is at least one fragrance or flavor material that is part of a fragrance or flavor, preferably the fragrance or flavor containing at least 20% by weight, based on the total weight of the fragrance or flavor, of fragrance or flavor material having a log P of 3.0 or greater, more preferably 3.5 or greater, more preferably 4.0 or greater.

15. 13. The method of claim 12, wherein the active ingredient is a vitamin or mineral, preferably selected from vitamin A, vitamin B1, vitamin B2, vitamin B3, vitamin B5, vitamin B6, vitamin B7, vitamin B9, vitamin B12, vitamin C, vitamin D, vitamin E, vitamin K, magnesium, sodium, potassium, zinc, iron, calcium, iodine, omega-3, folic acid, thiamine, riboflavin, niacin and phosphorus, or mixtures thereof, more preferably vitamin D.

16. 3. The method of claim 1 or 2, wherein the second plant-derived protein hydrogel slurry is diluted with water prior to step (f).

17. 3. The method of claim 1 or 2, wherein the emulsion has a protein solids content of less than 0.9wt%, preferably less than 0.8wt%, preferably less than 0.7wt%, preferably less than 0.6wt%, preferably less than 0.5wt%, preferably less than 0.4wt%, preferably less than 0.3wt%, preferably less than 0.2wt%, preferably less than 0.1wt%, based on the total weight of the emulsion.

18. 3. The method of claim 1 or 2, further comprising the step of altering the pH of the emulsion so that it differs from the isoelectric point of the plant-derived protein by more than 1 pH unit, preferably by more than 1.5 pH units.

19. 20. The method of claim 18, wherein altering the pH of the emulsion involves passing the plant-derived protein through its isoelectric point.

20. 19. The method of claim 18, wherein the pH of the emulsion after the step of modifying the pH of the emulsion is in the range of 5.5 to 7.5, preferably 6.0 to 7.

0.

21. 3. An emulsion obtained or obtainable by the method of claim 1 or 2.

22. 1. An emulsion comprising a lipophilic phase dispersed in a plant-derived protein hydrogel slurry comprising a plant-derived protein, said emulsion having a protein solids content of less than 1% by weight based on the total weight of said emulsion.

23. 23. An emulsion according to claim 22, wherein the emulsion has a protein solids content of less than 0.9wt%, preferably less than 0.8wt%, preferably less than 0.7wt%, preferably less than 0.6wt%, preferably less than 0.5wt%, preferably less than 0.4wt%, preferably less than 0.3wt%, preferably less than 0.2wt%, preferably less than 0.1wt%, based on the total weight of the emulsion.

24. 24. An emulsion according to claim 22 or 23, wherein the plant-derived protein is selected from pea protein, potato protein, rapeseed protein, lentil protein, chickpea protein, fava protein, mung bean protein, sunflower seed protein, pumpkin seed protein, flax protein, chia protein, canola protein, lupin protein, alfalfa protein, moringa protein and / or rice protein, preferably selected from pea protein and / or potato protein.

25. The emulsion according to claim 22 or 23, wherein the plant-derived protein is pretreated with an organic acid, and the organic acid is preferably acetic acid, lactic acid, formic acid, gluconic acid, propionic acid, an α-hydroxy acid, and / or a β-hydroxy acid, and more preferably lactic acid or acetic acid.

26. The plant-derived protein hydrogel slurry has, as measured by laser diffraction, d less than 100 μm, preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, more preferably less than 5 μm, more preferably less than 1 μm ５０ and / or The plant-derived protein hydrogel slurry has a d of less than 250 μm, preferably less than 100 μm, more preferably less than 50 μm, more preferably less than 30 μm, more preferably less than 10 μm, as measured by laser diffraction. ９０ 24. The emulsion of claim 22 or 23, wherein

27. 24. An emulsion according to claim 22 or 23, wherein the lipophilic phase comprises a solvent, a butter or a wax.

28. 28. The emulsion of claim 27, wherein the lipophilic phase comprises a solvent selected from fatty acid esters, fatty acids, linear or branched hydrocarbons of natural mineral or synthetic origin, fatty alcohols or ethers thereof, vegetable oils, silicone oils, phthalate esters, rosin resins, diols, triols, benzyl benzoate, triethyl citrate and triacetin, or combinations thereof.

29. 24. The emulsion of claim 22 or 23, wherein the lipophilic phase comprises an active ingredient, the active ingredient preferably being selected from vitamins, minerals, flavor materials, fragrance materials, pro-flavors, pro-fragrances, flavor enhancers, malodor counteractants, nutraceuticals, probiotics, pharmaceuticals, antibacterial agents, antivirals, anti-inflammatory agents, antioxidants, insecticides, herbicides, fertilizers, fungicides, insecticides, animal repellents, anti-acne agents, anti-aging agents, skin brighteners, emollients, skin moisturizers, occlusive agents, skin moisturizers, antiperspirants or deodorants, wrinkle control agents, fabric softener actives, surface cleaning actives, skin conditioning agents, hair conditioning agents, sunscreens, dyes, pigments, and adhesives, or combinations thereof.

30. the active ingredient is at least one fragrance or flavor material; the at least one fragrance or flavor material has a vapor pressure of 0.0001 Torr or greater at 25°C; and / or 30. An emulsion according to claim 29, wherein the at least one fragrance or flavour material has a log P of 3.0 or greater, preferably 3.5 or greater, more preferably 4.0 or greater.

31. 30. An emulsion according to claim 29, wherein the active ingredient is at least one fragrance or flavor material that is part of a fragrance or flavor, preferably the fragrance or flavor containing at least 20% by weight, based on the total weight of the fragrance or flavor, of fragrance or flavor material having a log P of 3.0 or greater, more preferably 3.5 or greater, more preferably 4.0 or greater.

32. 30. The emulsion of claim 29, wherein the active ingredient is a vitamin or mineral, preferably selected from vitamin A, vitamin B1, vitamin B2, vitamin B3, vitamin B5, vitamin B6, vitamin B7, vitamin B9, vitamin B12, vitamin C, vitamin D, vitamin E, vitamin K, magnesium, sodium, potassium, zinc, iron, calcium, iodine, omega-3, folic acid, thiamine, riboflavin, niacin and phosphorus, or mixtures thereof, more preferably vitamin D.

33. 24. The emulsion of claim 22 or 23, wherein the pH of the emulsion is such that it differs from the isoelectric point of the plant-derived protein by more than 1 pH unit, preferably by more than 1.5 pH units.

34. 24. The emulsion according to claim 22 or 23, wherein the pH of the emulsion is in the range of 5.5 to 7.5, preferably 6.0 to 7.

0.

35. 24. The emulsion of claim 22 or 23, wherein the plant-derived protein has a protein secondary structure with at least 40% intermolecular beta-sheet, at least 50% intermolecular beta-sheet, at least 60% intermolecular beta-sheet, at least 70% intermolecular beta-sheet, at least 80% intermolecular beta-sheet, or at least 90% intermolecular beta-sheet, wherein the % intermolecular beta-sheet content is measured by FTIR.

36. A composition comprising an emulsion prepared by the method of claim 1 or 2.

37. 37. The composition of claim 36, which is a cosmetic composition, a fragrance composition (e.g., a fine fragrance or a laundry scent booster), a beverage composition, an oral care composition, a pharmaceutical composition, or an agricultural composition, preferably a cosmetic composition.

38. 1. Use of a plant-derived protein hydrogel slurry as an emulsifier in a composition.

39. 39. The use according to claim 38, wherein the composition is a cosmetic composition, a fragrance composition (e.g. a fine fragrance or a laundry scent booster), a beverage composition, an oral care composition, a pharmaceutical composition, or an agricultural composition, preferably a cosmetic composition.

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