Protein encapsulation of nutritional and pharmaceutical compositions

Abstract

The present disclosure relates to microencapsulated compositions comprising one or more hydrophobic materials encapsulated by an encapsulant wherein the encapsulant comprises one or more modified proteins and / or peptides; and wherein the one or more modified proteins and / or peptides are obtained from a starting protein by subjecting the starting protein to a high cleavage process such that the average particle size of the one or more modified proteins and / or peptides is reduced relative to the starting protein. The present disclosure further relates to methods for protecting hydrophobic materials from oxidative degradation, for improving the oxidative stability of hydrophobic materials, for reducing surface free fat of microencapsulated compositions, and to stable emulsions and compositions comprising hydrophobic materials.

Description

[0001] Cross - reference to related applications

[0002] This application is a divisional application of the application with the filing date of October 16, 2020, application number: 202080085028.3 (PCT / AU2020 / 051120), and invention title "Protein Encapsulation of Nutritional and Pharmaceutical Compositions". Technical field

[0003] The present disclosure broadly relates to encapsulation compositions suitable for nutritional and pharmaceutical applications and methods for protecting hydrophobic materials in the encapsulation compositions from oxidation and oxidative degradation. Background art

[0004] It is well known that a variety of hydrophobic bioactive compounds such as long - chain polyunsaturated fatty acids ("LCPUFAs"), carotenoids, water - insoluble vitamins, phenolic compounds, flavors, and aromatic components provide a variety of health benefits. In particular, LCPUFAs are important nutritional components of the human diet, and many people fail to consume sufficient amounts of these essential fatty acids, especially ω - 3 fatty acids such as eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA). Numerous studies have found that ω - 3 fatty acids play important roles in heart, brain, and eye health, and their dietary intake is closely related to improved cardiovascular function and reduced incidence of various inflammatory diseases. For example, a recent study showed that EPA and DHA can have the ability to reduce heart rate and oxygen consumption during exercise, thus contributing to enhanced physical and mental performance in athletes (People et al., Journal of Cardiovascular Pharmacology, 2008, 52:540 - 547). Due to their important nutritional roles, compositions containing ω - 3 fatty acids are important both in nutritional supplements and as pharmaceuticals.

[0005] Therefore, there is an increasing trend to introduce ω - 3 fatty acids (such as fish oil, algal oil, and some plant seed oils) into foods to promote public health. However, since these fatty acids are prone to oxidation or degradation when exposed to oxygen, high temperature, or light (which often occurs during food production and storage), it is challenging to successfully fortify products with ω - 3 fatty acids while maintaining the stability and activity of the ω - 3 fatty acids. Oxidation and / or degradation of ω - 3 fatty acids produce undesirable oxidative decomposition products that may have an adverse impact on the sensory or physiological properties of the formulation. Therefore, the production, transportation, and storage of these functional foods are challenging.

[0006] Through the microencapsulation technique, bioactive compounds can be encapsulated in a physical protective shell material, and this microencapsulation technique has been successfully used to protect ω-3 fatty acids from oxidation and degradation. Spray drying is the most widely used technique for producing microencapsulated powders. Generally, spray-dried microencapsulated powders containing ω-3-rich oil have an oil loading of about 30% (w / w) and a surface free fat content of about 1% (w / w). Due to the excellent functional properties of Maillard reaction products (MRP), microencapsulated powders containing ω-3 oil with an oil loading as high as 48 ± 2% while maintaining a surface free fat content of about 1% (w / w) have been produced; however, the induction period (number of hours before the encapsulated oil starts to oxidize) of such products is usually only 50 hours.

[0007] There is a need to develop encapsulation and delivery systems that can improve the oxidative stability of hydrophobic compounds, especially ω-3 oils.

[0008] Disclosure

[0009] This disclosure is based on the unexpected discovery of the inventors that using an encapsulating agent comprising one or more modified proteins and / or peptides, wherein the modified proteins and / or peptides are obtained from starting proteins by subjecting the starting proteins to a high-shear process, can provide a composition comprising a hydrophobic material having both particularly high oxidative stability and a particularly low surface free fat content (i.e., high oil encapsulation efficiency). In a specific embodiment, one or more modified proteins and / or peptides are obtained from starting proteins by subjecting the starting proteins to a high-shear process such that the average particle size of the modified proteins and / or peptides is reduced relative to the starting proteins. In a specific embodiment, the average particle size of the modified proteins and / or peptides is about 70% or less of the average particle size of the starting proteins, such as about 65% or less of the average particle size of the starting proteins. In some embodiments, one or more modified proteins and / or peptides are used in the compositions or methods of this disclosure, wherein the one or more modified proteins are obtained from one or more corresponding starting proteins.

[0010] A first aspect of this disclosure provides a microencapsulated composition comprising one or more hydrophobic materials, wherein the encapsulating agent comprises one or more modified proteins and / or peptides, and wherein the modified proteins and / or peptides are obtained from starting proteins by subjecting the starting proteins to a high-shear process such that the average particle size of the modified proteins and / or peptides is reduced relative to the starting proteins. In a preferred embodiment, the average particle size of the modified proteins and / or peptides is about 70% or less of the average particle size of the starting proteins, such as about 65% or less of the average particle size of the starting proteins.

[0011] According to some preferred embodiments, the microencapsulated composition has a surface free fat content of less than about 1.8%, such as less than about 1%, such as less than about 0.8%.

[0012] According to some embodiments, the high-shear process is carried out at an alkaline pH, such as a pH of about 8. In some embodiments, the high-shear process comprises subjecting the starting protein to a pressure of about 20 mPa to about 300 mPa. In some embodiments, the high-shear process is a homogenization process. In some embodiments, the high-shear process is a microfluidization process.

[0013] According to some embodiments, one or more modified proteins and / or peptides are in the form of a protein component. According to some embodiments, the modified protein is a modified whey protein.

[0014] According to some embodiments, the encapsulating agent further comprises one or more carbohydrates, such as glucose syrup and dextrose monohydrate, or a combination thereof.

[0015] According to some embodiments, based on the total weight of the composition, one or more modified proteins and / or peptides are present at about 3% w / w to about 25% w / w.

[0016] According to some embodiments, the ratio of the modified protein component of the encapsulating agent to the carbohydrate component of the encapsulating agent is in the range of about 1:10 to 1:1.

[0017] According to some embodiments, the hydrophobic material is an edible oil. In some embodiments, the hydrophobic material comprises one or more long-chain polyunsaturated fatty acids (LCPUFAs). In some embodiments, the LCPUFAs comprise omega-3 fatty acids and / or omega-6 fatty acids. In some embodiments, the LCPUFAs are present in the form of triglycerides. In some embodiments, the LCPUFAs are present in one or more LCPUFA-containing oils; in some embodiments, one or more oils comprise fish oil. In some such embodiments, the fish oil is tuna oil.

[0018] According to some embodiments, the composition further comprises at least one source of vitamin C.

[0019] In some embodiments, the composition is in the form of an oil-in-water emulsion. In some embodiments, the composition is in the form of a spray-dried powder.

[0020] According to a second aspect, the present disclosure provides a method for protecting a hydrophobic material from oxidative degradation, comprising:

[0021] subjecting a starting protein to a high-shear process to produce one or more modified proteins and / or peptides such that the average particle size of the one or more modified proteins and / or peptides is reduced relative to the starting protein; and

[0022] Encapsulating one or more hydrophobic materials with an encapsulating agent comprising one or more modified proteins and / or peptides.

[0023] According to a third aspect, the present disclosure provides a method for improving the oxidative stability of a hydrophobic material, comprising:

[0024] Subjecting a starting protein to a high-shear process to produce one or more modified proteins and / or peptides such that the average particle size of the one or more modified proteins and / or peptides is reduced relative to the starting protein; and

[0025] Encapsulating one or more hydrophobic materials with an encapsulating agent comprising one or more modified proteins and / or peptides.

[0026] According to a fourth aspect, the present disclosure provides a method for reducing surface free fat in a microencapsulated composition comprising one or more hydrophobic materials encapsulated by an encapsulating agent, comprising subjecting one or more starting proteins and / or peptides to a high-shear process to produce one or more modified proteins and / or peptides such that the average particle size of the one or more modified proteins and / or peptides is reduced relative to the one or more starting proteins and / or peptides; and encapsulating one or more hydrophobic materials with an encapsulating agent comprising one or more modified proteins and / or peptides.

[0027] In some embodiments of the method according to the second, third, or fourth aspect, the average particle size of the one or more modified proteins and / or peptides is about 70% or less, such as about 65% or less, of the average particle size of the starting protein.

[0028] In some embodiments, the high-shear process is carried out at an alkaline pH, such as at a pH of about 8.

[0029] In some embodiments, the hydrophobic material comprises one or more LCPUFAs, such as in the form of triglycerides.

[0030] According to a fifth aspect, the present disclosure provides a stable emulsion comprising a hydrophobic material, wherein the emulsion further comprises one or more modified proteins and / or peptides, and wherein the one or more modified proteins and / or peptides are obtained from a starting protein by subjecting the starting protein to a high-shear process such that the average particle size of the one or more modified proteins and / or peptides is reduced relative to the starting protein.

[0031] In some embodiments, the average particle size of the one or more modified proteins and / or peptides is about 70% or less, such as about 65% or less, of the average particle size of the starting protein.

[0032] In some embodiments, the high-shear process is carried out at an alkaline pH, such as at a pH of about 8.

[0033] In some embodiments, the hydrophobic material comprises one or more LCPUFAs, for example in the form of triglycerides.

[0034] According to a sixth aspect, the present disclosure provides a composition comprising a hydrophobic material and one or more modified proteins and / or peptides, wherein the one or more modified proteins and / or peptides are obtained from a starting protein by subjecting the starting protein to a high shear process such that the average particle size of the one or more modified proteins and / or peptides is reduced relative to the starting protein. BRIEF DESCRIPTION OF THE DRAWINGS

[0035] The exemplary embodiments of the present disclosure are described herein by way of non-limiting examples only with reference to the following drawings.

[0036] Figure 1 . Interfacial tension of corn oil with 1.0% w / w uWPI and mWPI (native solution and pH 8 solution).

[0037] Figure 2 . Schematic diagram showing a method for preparing microencapsulated powder based on unmodified whey protein isolate (uWPI powder) and microencapsulated powder based on modified whey protein isolate (mWPI powder).

[0038] Figure 3 . Graph showing the Oxipres analysis results of microencapsulated uWPI and mWP powders containing ω-3 oil compared to microcapsule powders containing ω-3 oil encapsulated with Maillard reaction product (MRP).

[0039] Figure 4 . Total mass of microencapsulated uWPI and mWPI powders during 4-week accelerated exposure.

[0040] Figure 5 . Rancid odor and taste and marine odor and taste of microencapsulated uWPI and mWPI powders during 4-week accelerated exposure. DETAILED DESCRIPTION

[0041] Throughout this specification, unless the context requires otherwise, the word "comprise" or variations such as "comprises" or "comprising" will be understood to imply the inclusion of stated step or element or integer or group of steps or elements or integers but not the exclusion of any other step or element or integer or group of elements or integers. Thus, in the context of this specification, the term "comprise" means "comprising mainly, but not necessarily solely".

[0042] In the context of this specification, the term "about" is understood to refer to a numerical range that a person of ordinary skill in the art would consider equivalent to the recited value when achieving the same function or result.

[0043] In the context of this specification, the terms "a" and "an" refer to one or more than one (i.e., at least one) of the grammatical object of the article. For example, "an element" refers to one element or more than one element.

[0044] The term "protein" refers to a polymer composed of amino acids linked together by peptide bonds. The term "peptide" can also be used to refer to such a polymer, although in some cases a peptide can be shorter than a protein (i.e., composed of fewer amino acid residues). The terms "protein" and "peptide" can be used interchangeably herein.

[0045] As used herein, the term "oxidative stability" in relation to hydrophobic materials and compounds (such as LCPUFA) means the stability of the hydrophobic material (such as LCPUFA or an oil containing LCPUFA) in the presence of oxygen and its resistance to oxidation or oxidative degradation. Thus, a higher oxidative stability indicates a stronger resistance to oxidation and oxidative degradation. Generally, reference to improved oxidative stability resulting from encapsulation according to the present disclosure refers to an improvement relative to the oxidative stability observed in the absence of an encapsulating agent according to the present disclosure or in the presence of an alternative encapsulating agent.

[0046] According to an embodiment of the present disclosure, a modified whey protein is used as an encapsulating agent in a microencapsulated composition containing tuna oil. Modification of whey protein isolate by a high-shear process results in a reduction in its average particle size, which is believed to be due to the separation of water-soluble protein aggregates. In particular, at natural pH and alkaline pH (pH 8), the average particle size of the modified protein is about 51% of the starting protein.

[0047] This modified protein is used as a key encapsulant component to provide spray-dried microencapsulated powders that stabilize omega-3 oils with a high level of total oil loading (>45% total oil loading (w / w) (tuna oil), especially about 49%) and a low surface free fat content of less than 1.5 ± 0.1% (1.3 ± 0.5% and even lower, 0.6 ± 0.1% at pH 8). The resulting microencapsulated powders also exhibit very high oxidative stability, with an induction period far exceeding 100 hours and acceptable primary and secondary oxidation characteristics (including peroxide value, p-anisidine value, overall quality, and rancid and marine odors) during a 4-week rapid exposure period. The modification process disclosed herein can be applied to a range of proteins to provide microencapsulation systems that can be used to extend the shelf life of various sensitive hydrophobic compounds, including omega-3 oils, carotenoids, water-insoluble vitamins, phenolic compounds, flavors, and aromatic components.

[0048] Accordingly, specific embodiments of the present disclosure provide microencapsulated compositions comprising one or more hydrophobic materials, wherein the encapsulant comprises a modified protein and / or peptide, and wherein the modified protein and / or peptide is obtained from a starting protein by subjecting the starting protein to a high-shear process such that the average particle size of the modified protein and / or peptide is reduced relative to the starting protein.

[0049] Also provided are methods and compositions wherein the modified protein or peptide is used to encapsulate one or more hydrophobic materials to protect the one or more hydrophobic materials from oxidation or oxidative degradation. Protection from oxidation or oxidative degradation can be determined by any suitable method known to those skilled in the art.

[0050] The microencapsulated compositions of the present disclosure can be in the form of, for example, an emulsion or can be in solid form. The emulsion can include an oil-in-water emulsion. The solid form can be a powder. The powder can be obtained, for example, by spray-drying an emulsion. In one embodiment, the composition is a free-flowing powder. The powder can have an average particle size of about 10 μm to 1000 μm, or about 50 μm to 800 μm, or about 100 μm to 300 μm. In alternative embodiments, the composition can be in particulate form.

[0051] The compositions of the present disclosure are produced by microencapsulation, wherein the encapsulant comprises or consists of a modified protein and / or peptide. The "modified protein" or "modified peptide" is obtained from a starting protein by subjecting the starting protein to a high-shear process such that the average particle size of the modified protein or peptide is reduced relative to the starting protein. In some embodiments, one or more modified proteins are used in the compositions or methods of the present disclosure, wherein the one or more modified proteins and / or peptides are obtained from one or more starting proteins, respectively.

[0052] As will be readily understood from the relevant context, the "protein" referred to in this specification may refer to the starting protein, the modified protein, or both.

[0053] High-shear processes can be used to alter one or more properties of a protein, such as its particle size, solubility, foaming, gelling, and / or emulsifying properties. The fat globule size of an emulsion formed with an aqueous solution of such a protein and a fat can also be reduced, and the interfacial tension with an oil can also be reduced, particularly when the modified protein is subjected to a high-shear process and used in an aqueous solution at an alkaline pH, such as a pH of about 8. Any suitable high-shear process can be used to modify the protein, and those skilled in the art will be familiar with various high-shear processes.

[0054] In some embodiments, the high-shear process is a homogenization process. In some exemplary embodiments, the homogenization process can be a high-pressure homogenization process, where the protein is forced to flow at high speed through a narrow gap. In some embodiments, the homogenization process is microfluidization. The microfluidization process uses high shear rates and uniform processing pressures and advantageously provides consistent nanoscale particle sizes and narrow particle size distributions. Exemplary microfluidization devices are available from Microfluidics International Corporation of the United States. In some exemplary embodiments, the homogenization process can be an ultrasonic pressure homogenization process, where acoustic pressure waves are generated in the medium to cause homogenization. In some embodiments, the homogenization process can be a mechanical homogenization process, such as using a rotor-stator homogenizer (e.g., having multiple stages), or a blade-type homogenizer. Those skilled in the art will understand that the scope of the present disclosure is not limited to any particular homogenization process.

[0055] In some embodiments, the high-shear process includes multiple passes through a high-shear arrangement. For example, in embodiments using a high-pressure homogenization process, the material can undergo multiple passes through the narrow gap to achieve the desired homogenization. For example, the high-shear process can include 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more passes.

[0056] In some embodiments, the high-shear process includes subjecting the starting protein to a pressure of about 20 mPa to about 300 mPa, such as about 50 mPa to about 300 mPa, such as about 100 mPa to about 300 mPa, such as about 100 mPa to about 250 mPa, such as about 100 mPa to about 200 mPa, such as about 125 mPa to about 175 mPa, such as about 150 mPa, or alternatively, about 125 mPa to about 300 mPa, such as about 150 mPa to about 300 mPa, such as about 175 mPa to about 300 mPa, such as about 200 mPa to about 300 mPa, such as about 225 mPa to about 300 mPa, such as about 250 mPa to 300 mPa.

[0057] In some specific embodiments, the high-shear process includes a homogenization process, and the homogenization includes subjecting the starting protein to a pressure of about 20 mPa to about 300 mPa, such as about 50 mPa to about 300 mPa, such as about 100 mPa to about 300 mPa, such as about 100 mPa to about 250 mPa, such as about 100 mPa to about 200 mPa, such as about 125 mPa to about 175 mPa, such as about 150 mPa, or alternatively, about 125 mPa to about 300 mPa, such as about 150 mPa to about 300 mPa, such as about 175 mPa to about 300 mPa, such as about 200 mPa to about 300 mPa, such as about 225 mPa to about 300 mPa, such as about 250 mPa to 300 mPa.

[0058] In some specific embodiments, the high-shear process includes a homogenization process, and the homogenization includes subjecting the starting protein to a pressure of about 20 mPa to about 300 mPa, such as about 50 mPa to about 300 mPa, such as about 100 mPa to about 300 mPa, such as about 100 mPa to about 250 mPa, such as about 100 mPa to about 200 mPa, such as about 125 mPa to about 175 mPa, such as about 150 mPa, or alternatively, about 125 mPa to about 300 mPa, such as about 150 mPa to about 300 mPa, such as about 175 mPa to about 300 mPa, such as about 200 mPa to about 300 mPa, such as about 225 mPa to about 300 mPa, such as about 250 mPa to 300 mPa for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more passes.

[0059] In some specific embodiments, the high-shear process is carried out in an alkaline environment, such as in an alkaline aqueous solution, for example, subjecting the protein to the high-shear process in an aqueous solution with a pH of about 8.

[0060] Subjecting a starting protein to a high shear process can be used to provide a modified protein or peptide having a reduced average particle size relative to the starting protein. In particular, the average particle size of the modified protein or peptide can be about 70% or less of the average particle size of the starting protein, such as about 65% or less of the average particle size of the starting protein. In some embodiments, the average particle size of the modified protein or peptide can be about 60% or less of the average particle size of the starting protein, such as about 55% or less of the average particle size of the starting protein. The reduction in the average particle size of the protein can be readily determined by any suitable method readily available to those skilled in the art. A particular method that can be used to determine the average particle size of the starting protein and the modified protein or peptide and thus determine whether a reduction has occurred is to use the principle of dynamic light scattering, such as by using a Malvern Zetasizer (Malvern Panalytical).

[0061] The scope of the present disclosure should not be limited by any particular protein. Any suitable starting protein and modified protein or peptide can be used in the compositions and methods of the present disclosure. The protein can be, for example, in the form of a protein component obtained from a natural source such as a cell or tissue source. The cell or tissue source can be obtained from any suitable source, such as an animal or plant source. In an exemplary embodiment, the protein is whey protein isolate; the starting protein is unmodified whey protein isolate and the modified protein is modified whey protein isolate. In another exemplary embodiment, the protein is whey protein concentrate; the starting protein is unmodified whey protein concentrate and the modified protein is modified whey protein concentrate. In other embodiments, the protein can be derived from a plant source and can include, for example, proteins from pea or soy sources or pea protein isolate or soy protein isolate.

[0062] Proteins of any suitable molecular weight can be used in accordance with the present disclosure. For example, the starting protein and / or the modified protein or peptide can have a molecular weight in the range of about 500 Da to about 150 kDa. For example, the protein can have a molecular weight of up to about 500 Da, 1 kDa, 2 kDa, 3 kDa, 4 kDa, 5 kDa, 10 kDa, 15 kDa, 20 kDa, 25 kDa, 30 kDa, 35 kDa, 40 kDa, 45 kDa, 50 kDa, 55 kDa, 60 kDa, 65 kDa, 70 kDa, 75 kDa, 80 kDa, 85 kDa, 90 kDa, 95 kDa, 100 kDa, 105 kDa, 110 kDa, 115 kDa, 120 kDa, 125 kDa, 130 kDa, 135 kDa, 140 kDa, 145 kDa or up to about 150 kDa.

[0063] Proteins of any suitable molecular size can be used in accordance with the present disclosure. For example, the starting protein and / or the modified protein or peptide can have a particle radius in the range of about 0.5 nm to about 5 nm. For example, the protein can have the following particle radii: about 0.5 nm, 0.6 nm, 0.7 nm, 0.8 nm, 0.9 nm, 1.0 nm, 1.1 nm, 1.2 nm, 1.3 nm, 1.4 nm, 1.5 nm, 1.6 nm, 1.7 nm, 1.8 nm, 1.9 nm, 2.0 nm, 2.1 nm, 2.2 nm, 2.3 nm, 2.4 nm, 2.5 nm, 2.6 nm, 2.7 nm, 2.8 nm, 2.9 nm, 3.0 nm, 3.1 nm, 3.2 nm, 3.3 nm, 3.4 nm, 3.5 nm, 3.6 nm, 3.7 nm, 3.8 nm, 3.9 nm, 4.0 nm, 4.1 nm, 4.2 nm, 4.3 nm, 4.4 nm, 4.5 nm, 4.6 nm, 4.7 nm, 4.8 nm, 4.9 nm or about 5.0 nm.

[0064] The modified protein and / or peptide can be introduced into the emulsion or composition at any stage of preparing the emulsion or composition, thereby forming a uniform aqueous dispersion or slurry. Those skilled in the art will be able to optimize the amount and molecular weight of the protein and / or peptide to be introduced without undue burden or experimentation. In some preferred embodiments, the molecular weight of the protein and / or peptide can be low enough to facilitate microencapsulation, while the amount of the protein and / or peptide can be sufficient to provide effective protection as an encapsulating agent. In the case of an oil-in-water emulsion, the viscosity can also be controlled. If the viscosity is too high, it may hinder spray drying. Determining the appropriate protein content and appropriate viscosity is well within the capabilities of the skilled person.

[0065] In an exemplary embodiment, the modified protein and / or peptide can be present at about 3% (w / w) to about 30% (w / w) based on the total weight of the composition or about 3% (w / w) to about 25% (w / w) based on the total weight of the composition. In the case of an oil-in-water emulsion, this means about 3% (w / w) to about 30% (w / w) or about 3% (w / w) to about 25% (w / w) based on the total weight of the aqueous phase plus the oil phase. For example, based on the total weight of the composition, the protein and / or peptide can be present at about 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29% or 30% w / w.

[0066] In certain embodiments described herein, the encapsulant comprises compounds, substances or moieties other than the modified protein and / or peptide. For example, the encapsulant can comprise a combination of a modified protein with one or more polysaccharides or carbohydrate components. For example, carbohydrates having reducing sugar functional groups can react with the protein. Dextrose (including dextrose monohydrate), glucose, lactose, sucrose, oligosaccharides, and dried glucose syrup. In another embodiment, in some formulations, polysaccharides, high-methoxyl pectin or carrageenan can be added to the protein-carbohydrate mixture. Attention needs to be paid to the reaction of the protein and the carbohydrate to ensure that the conditions do not cause extensive gelation or coagulation of the protein, as this will prevent the protein from forming a good film.

[0067] In an exemplary embodiment, the compositions of the present disclosure can be prepared by dissolving the polysaccharide or carbohydrate component of the encapsulant in an aqueous phase comprising the modified protein, optionally using a high-shear mixer. The mixture can then be heated to a temperature of about 50 °C to 80 °C, after which one or more antioxidants can be added if desired. The hydrophobic material can be added inline to the aqueous mixture passing through the high-shear mixer to form a coarse emulsion. The coarse emulsion can then be homogenized. If a powdered product is desired, the emulsion can be pressured and spray dried at an inlet temperature of about 180 °C and an outlet temperature of 80 °C.

[0068] By way of example, suitable polysaccharide and carbohydrate components can include maltodextrin, dextrose (including dextrose monohydrate), glucose, lactose, sucrose, oligosaccharides, and dried glucose syrup, or a combination of one or more thereof. In another embodiment, polysaccharides, high-methoxyl pectin or carrageenan can be added to the protein-carbohydrate mixture in some formulations. Attention needs to be paid to the reaction of the protein and the carbohydrate to ensure that the conditions do not cause extensive gelation or coagulation of the protein, as this will prevent the protein from forming a good film. The ratio (by weight) of the modified protein of the encapsulant to the polysaccharide or carbohydrate component can be, for example, about 3:1, 2.5:1, 2:1, 1.5:1, 1:1, 1:1.5, 1:2, 1:2.5, 1:3, 1:3.5, 1:4, 1:4.5, 1:5, 1:5.5, 1:6, 1:6.5, 1:7, 1:7.5, 1:8, 1:8.5, 1:9, 1:9.5 or 1:10.

[0069] In certain embodiments, the ratio (by weight) of the protein component of the encapsulant to the carbohydrate component of the encapsulant can be from about 1:10 to about 1:1.5. For example, the ratio of the protein component to the carbohydrate component can be about 1:10, 1:9.5, 1:9, 1:8.5, 1:8, 1:7.5, 1:7, 1:6.5, 1:6, 1:5.5, 1:5, 1:4.5, 1:4, 1:3.5, 1:3, 1:2.5, 1:2 or 1:1.5. The ratio of the protein component to the carbohydrate component can be from about 1:5 to about 1:1.5, such as about 1:4, 1:3, 1:2.9, 1:2.8, 1:2.7, 1:2.6, 1:2.5, 1:2.4, 1:2.3, 1:2.2, 1:2.1, 1:2, 1:1.9, 1:1.8, 1:1.7, 1:1.6 or 1:1.5. The ratio of the protein component to the carbohydrate component can be from about 1:2 to about 1:1.9, such as about 1:2, 1:1.99, 1:1.98, 1:1.97, 1:1.96, 1:1.95, 1:1.94, 1:1.93, 1:1.92, 1:1.91 or 1:1.9. In one exemplary embodiment, the ratio of the protein component to the carbohydrate component is about 1:1.99.

[0070] The polysaccharide or carbohydrate component can have a DE value of about 0 to 100, about 10 to 70, about 20 to 60, or about 20 to 40. The DE value can be about 0, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100.

[0071] Those skilled in the art will understand that alternative carbohydrate sources can also be combined with one or more modified proteins for use in the encapsulant. For example, the carbohydrate source can comprise octenyl succinic anhydride modified starch and one or more, or two or more, reducing sugar sources having a dextrose equivalent value of about 0 to 80, as previously described in WO2012 / 106777, the disclosure of which is incorporated herein by reference. Briefly, the starch can comprise primary and / or secondary modification and can be an ester or semi-ester. Suitable octenyl succinic anhydride modified starches include, for example, those based on waxy maize and sold by Ingredion ANZ Pty Ltd, Seven Hills, NSW, Australia under the trade name PURITY IMF and HI Those sold by the IMF. Based on the total weight of the composition, the octenyl succinic anhydride modified starch may be present in an amount of less than about 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6.5%, 6%, 5.5%, 5%, 4.5%, 4%, 3.5%, 3%, 2.5%, 2% or less than 1%.

[0072] Sources of reducing sugars are well known to those skilled in the art and include monosaccharides and disaccharides such as glucose, fructose, maltose, galactose, glyceraldehyde and lactose. Suitable sources of reducing sugars also include oligosaccharides such as glucose polymers such as dextrin and maltodextrin and glucose syrup solids. Reducing sugars can also be derived from glucose syrups that typically contain no less than 20% by weight of reducing sugars.

[0073] The surface free fat content of the microencapsulated composition according to the present disclosure can be less than or about 10%, less than or about 9%, less than or about 8%, less than or about 7%, less than or about 6%, less than or about 5%, less than or about 4%, less than or about 3%, less than or about 2.5%, less than or about 2.4%, less than or about 2.3%, less than or about 2.2%, less than or about 2.1%, less than or about 2%, less than or about 1.9%, less than or about 1.8%, less than or about 1.7%, less than or about 1.6%, less than or about 1.5%, less than or about 1.4%, less than or about 1.3%, less than or about 1.2%, less than or about 1.1%, less than or about 1%, or less than or about 0.8%. In a particularly preferred embodiment, the surface free fat content is less than about 1.8%, such as less than about 1.5%, such as less than about 1.4%, such as less than about 1%. In some embodiments, for example where the protein is subjected to a high shear process at an alkaline pH, such as at a pH of about 8, the surface free fat content can be less than about 1%, such as less than about 0.8%. In certain embodiments, the surface free fat content is determined in a powder derived from or produced from an emulsion.

[0074] The oxidative stability of the microencapsulated composition according to the present disclosure can be measured, for example, according to the induction period, for example using an ML Oxipres (Mikrolab Aarhus) as described in Example 7 below (“Oxipres” is an indirect measure of potential oxidative stability). In a particularly preferred embodiment, the induction period of the microencapsulated composition according to the present disclosure when measured at 70 °C and a pressure of 5 bar is at least about 50 hours, such as at least about 60 hours, such as at least about 70 hours, such as at least about 80 hours, such as at least about 90 hours. In some embodiments, the induction period is at least about 100 hours. In some embodiments, the induction period is at least about 120 hours, such as at least about 130 hours.

[0075] The compositions and emulsions of the present disclosure comprise one or more hydrophobic materials. The term "hydrophobic material" includes pure hydrophobic compounds, hydrophobic mixtures, and hydrophobic compositions. The hydrophobic material can be any hydrophobic compound or composition required for microencapsulation according to the present disclosure. Examples of hydrophobic materials that can be used according to the present disclosure include bioactive substances such as LCPUFAs and oils containing LCPUFAs, carotenoids, water-insoluble vitamins such as vitamins A, D, E, and K, phenolic compounds, flavor and aromatic compounds, and edible oils. The hydrophobic materials can provide one or more health benefits when administered to a subject. In certain embodiments, the hydrophobic material can be one or more LCPUFAs, or an oil containing one or more LCPUFAs. Such oils can be naturally occurring or naturally derived, or can be synthesized from genetically modified or non-genetically modified sources. In the context of the present disclosure, the terms "naturally occurring" and "naturally derived" include oils and lipid compositions that can be extracted from natural sources such as the organisms listed herein, or those that can be derived or modified from oils or one or more lipids found in these natural sources. Those skilled in the art will understand that the scope of the present disclosure is not limited to the mention of the characteristics or sources of the hydrophobic materials or one or more LCPUFAs or oils containing one or more LCPUFAs.

[0076] Exemplary oils that are or can be modified to contain or be rich in LCPUFAs, or can be used without changing their LCPUFA content, include oils from marine organisms such as crustaceans like krill, mollusks like oysters, and fish such as tuna, salmon, trout, sardine, mackerel, sea bass, menhaden, herring, pilchard, pickled fish, eel, or whitebait. The oil can be from the fish eggs of one or more marine organisms (such as those listed herein). In an exemplary embodiment, the oil is or contains tuna oil, krill oil, or a lipid extract from fish eggs. In certain embodiments, the hydrophobic material is tuna oil.

[0077] Other exemplary oils that are or can be modified to contain or be rich in LCPUFAs, or can be used without changing their LCPUFA content, include plant and microbial sources. Plant sources include but are not limited to flaxseed, walnut, sunflower seed, rapeseed, safflower, soybean, wheat germ, corn, and green leafy plants such as kale, spinach, and parsley. Microbial sources include algae and fungi.

[0078] The hydrophobic material may be present in an amount of about 0.1% to 80%, or about 1% to 80%, or about 1% to 75%, or about 5% to 80%, or about 5% to 75%, or about 5% to 70% of the total weight of the composition. In an exemplary embodiment where the oil is tuna oil, the oil may be present in an amount of about 2%, 4%, 6%, 8%, 10%, 12%, 14%, 16%, 18%, 20%, 22%, 24%, 26%, 28%, 30%, 32%, 34%, 36%, 38%, 40%, 42%, 44%, 46%, 48%, 49%, 50%, 52%, 54%, 56%, 58%, 60%, 62%, 64%, 66%, 68%, 70%, 72%, 74%, 76%, 78% or 80% of the total weight of the composition.

[0079] The hydrophobic material comprising LCPUFA generally comprises one or more omega-3 fatty acids and / or one or more omega-6 fatty acids, or mixtures thereof. The fatty acids may include DHA, AA, EPA, DPA and / or stearidonic acid (SDA), or mixtures thereof. In one embodiment, the fatty acids include DHA and EPA.

[0080] The compositions contemplated by the present disclosure may also contain additional components such as antioxidants, anti-caking agents, flavoring agents, coloring agents, vitamins, minerals, amino acids, chelating agents, etc.

[0081] Suitable antioxidants are well known to those skilled in the art and may be water-soluble or oil-soluble. Suitable water-soluble antioxidants include, for example, sodium ascorbate, calcium ascorbate, potassium ascorbate, ascorbic acid, glutathione, lipoic acid and uric acid. In an embodiment, the water-soluble antioxidant may be present in the composition in the range of about 0-10% wt / wt of the total composition. Suitable oil-soluble antioxidants include, for example, tocopherols, ascorbyl palmitate, tocotrienols, phenols, polyphenols, etc. In an embodiment, the oil-soluble antioxidant is present in the oil phase in the range of about 0-10% wt / wt of the total composition.

[0082] Anti-caking agents compatible with the compositions of the present disclosure will be well known to those skilled in the art and include calcium phosphates (such as tricalcium phosphate) and carbonates (such as calcium carbonate and magnesium carbonate) as well as silica.

[0083] The composition may also comprise one or more low molecular weight emulsifiers. Suitable low molecular weight emulsifiers include, for example, monoglycerides and diglycerides of glycerol, lecithin, and sorbitan esters. Other suitable low molecular weight emulsifiers will be known to those skilled in the art. The low molecular weight emulsifier may be present in an amount of from about 0.1% to 3% of the total weight of the composition, or from about 0.1% to 2% of the total weight of the composition, or from about 0.1% to 0.5% of the total weight of the composition, or from about 0.1% to 0.3% of the total weight of the composition. For example, the low molecular weight emulsifier may be present in an amount of about 0.1%, 0.2%, 0.3%, 0.4%, 0.5%, 0.6%, 0.7%, 0.8%, 0.9%, 1%, 1.1%, 1.2%, 1.3%, 1.4%, 1.5%, 1.6%, 1.7%, 1.8%, 1.9% or 2% of the total weight of the composition.

[0084] The compositions contemplated herein may be formulated for administration to a subject by any suitable route, typically oral administration. The composition may be in liquid or solid form and may be taken as such (e.g., in the form of a syrup or other suitable liquid, or as a capsule or other suitable solid form). Alternatively, the composition may be incorporated into a food or beverage product.

[0085] Those skilled in the art will appreciate that various changes and / or modifications may be made to the invention without departing from the spirit or scope of the invention as broadly described. Accordingly, the embodiments of the present disclosure are to be considered in all respects as illustrative and not restrictive.

[0086] Any reference in this specification to any prior publication (or information derived therefrom) or to any matter which is known should not be taken as an admission or acknowledgment or any form of suggestion that the prior publication (or information derived therefrom) or known matter forms part of the common general knowledge in the technical field to which this specification pertains.

[0087] The invention will now be described in more detail by reference to the following specific examples, which should not be construed as limiting the scope of the invention in any way.

[0088] Examples

[0089] Example 1 – Modification of Whey Protein Isolate

[0090] Whey protein isolate (WPI) and whey protein concentrate (WPC) were each dissolved in water at 10% (w / w). The pH of some of the WPI solution was adjusted to 8. The solutions (WPI, WPC, and WPI (pH 8)) were stirred at 50 °C for 30 minutes under gentle shear. Subsequently, the mixture was homogenized at 1500 bar (150 mPa) in 6 passes to induce modification of the whey proteins. During homogenization, the temperature of the WPI and WPC was maintained below 60 °C using ice packs.

[0091] Example 2 - Particle Size Analysis of Protein Aqueous Solutions

[0092] The protein particle sizes of 1.0% w / w solutions of unmodified whey protein isolate (uWPI) and modified whey protein isolate (mWPI), as well as unmodified whey protein concentrate (uWPC) and modified whey protein concentrate (mWPC) obtained in Example 1, were measured using a Malvern Zetasizer by the principle of dynamic light scattering. Backscatter (BS) examines a wide particle size spectrum, while forward scatter (FS) captures a larger particle size range. The results are shown in Table 1 below.

[0093] Table 1

[0094]

[0095] All samples were polydisperse, so the presence of very large particles could significantly affect the average particle size (Z-Av) as shown in Table 1. Regardless of pH, modification of whey protein isolate (mWPI) resulted in a significant reduction in protein particle size compared to the unmodified version (uWPI). This is thought to be due to pressure modification largely separating soluble protein aggregates. uWPC had a similar average particle size to uWPI, but the soluble protein aggregates were significantly smaller, as shown by the FS results. When applied to whey protein concentrate (WPC), the degree of particle size reduction by pressure modification was similar. Both WPI and WPC were pressure-modified at 1500 bar / 6 passes, and the average protein particle size was reduced by nearly 2-fold.

[0096] Example 3 - Surface Charge Analysis of Protein Aqueous Solutions

[0097] The surface charge of 1.0% w / w aqueous solutions / dispersions of uWPI and mWPI obtained in Example 1 at natural pH (i.e., without any pH adjustment) and pH 8 was measured using a Zetasizer that measures the electromotive force. The results are shown in Table 2 below.

[0098] Table 2

[0099]

[0100] The small difference in the surface charge (Zeta potential; ZP) of the mWPI solution can be attributed to the reduction of soluble protein aggregates. An alkaline pH of 8 was used to improve the hydration properties of WPI, and more negative surface charge was observed.

[0101] Example 4 - Interfacial Tension between Protein Aqueous Solutions and Corn Oil

[0102] The interfacial tension of 1.0% w / w aqueous solutions of uWPI and mWPI obtained in Example 1 is as Figure 1 shown.

[0103] The interfacial tension between corn oil and water is about 27 mN / m. The 1.0% w / w WPI solution effectively reduces the interfacial tension between corn oil and water, demonstrating good surface activity and adsorption behavior at the interface. Compared with the uWPI solution, the mWPI solution has a lower average particle size and better hydration (pH 8), so it diffuses to the interface faster and further reduces the interfacial tension value.

[0104] Example 5 - Protein / Oil Emulsion

[0105] Use the 1% w / w aqueous solutions of uWPI and mWPI obtained in Example 1 and refined tuna oil containing mixed natural tocopherols to prepare an oil-in-water emulsion (weight ratio of protein to oil is 1:3). The mixture of the WPI solution and tuna oil was roughly homogenized for 10 minutes at 10,000 RPM using an UltraTurrax. The median oil droplet size d(0.5) and the average oil droplet size D[4.3] (in microns) were measured using a particle size analyzer (Malvern Instruments, Mastersizer MS3000) based on the principle of laser diffraction; the results are shown in Table 3 below. "EAI" shown in Table 3 refers to the emulsion activity index, and "ESI" refers to the emulsion stability index. EAI reflects the adsorption ability of the protein at the oil-water interface and ESI represents the ability to resist emulsion instability (such as flocculation and emulsification).

[0106] Table 3

[0107]

[0108] The median oil droplet size d(0.5) and the average oil droplet size D[4.3] of mWPI (pH 8) are smaller. Regardless of modification or pH treatment, these two parameters increase with time, but after a 1-week storage period, the change range of mWPI (pH 8) is the smallest. This corresponds to the better interfacial activity of the mWPI (pH 8) solution as described in Example 4 and the adsorption behavior that confers good emulsion stability over time.

[0109] Example 6 - Encapsulation of Hydrophobic Materials Using Unmodified and Modified Protein Encapsulants

[0110] The unmodified whey protein isolate (uWPI) and modified whey protein isolate (mWPI) obtained in Example 1 were used to prepare microencapsulation compositions. Refined tuna oil containing mixed natural tocopherols was used as the hydrophobic core material. The formulation of each microencapsulation composition is shown in Table 4 below. The preparation method of each composition is as Figure 2 shown and is discussed in detail below.

[0111] Table 4. Formulation of Tuna Oil Microencapsulated Powder

[0112]

[0113] Preparation of microencapsulated powder compositions (“uWPI - microencapsulated powder”) using uWPI and carbohydrate encapsulants

[0114] Dissolve WPI (15.00% (w / w)), dextrose monohydrate (14.50% (w / w)), dry glucose syrup (DE value of 30) (15.10% (w / w)), and sodium ascorbate (5.35% (w / w)) in water. Stir the aqueous phase at 50 °C for 35 minutes under gentle shear. Then add tuna oil containing antioxidant (50.05% (w / w)), and then prepare an emulsion as follows: Produce a coarse emulsion using high - shear mixing at 10,000 rpm for 10 - 15 minutes, and then perform two - stage homogenization three passes at 400 / 200 bar (total 600 bar) to produce a refined emulsion. Spray - dry the final oil - in - water emulsion using a bench - top spray dryer with inlet and outlet temperatures of 170 °C and 90 - 100 °C, respectively. Load the produced powder into aluminum bags under N 2 as a protective gas. The uWPI powder is stored at 25 °C before use. The total oil loading in the uWPI powder is 50% (w / w). Preparation of microencapsulated powder compositions (“mWPI - microencapsulated powder”) using mWPI and carbohydrate encapsulants

[0115] Modify WPI as described in Example 1. To the aqueous phase of mWPI, add dextrose monohydrate (14.50% (w / w)), dry glucose syrup (DE value of 30) (15.10% (w / w)), and sodium ascorbate (5.35% (w / w)) at 50 °C. Add refined tuna oil containing mixed natural tocopherols (50.05% (w / w)), and then prepare an emulsion as follows: Produce a coarse emulsion using high - shear mixing at 10,000 rpm for 10 - 15 minutes, and then perform two - stage homogenization three passes at 400 / 200 bar (40 / 20 mPa) (total 600 bar (60 mPa)) to produce a refined emulsion. Spray - dry the final oil - in - water emulsion using a bench - top spray dryer with inlet temperature range and outlet temperature range of 170 °C and 90 - 100 °C, respectively. Load the produced powder into aluminum bags under N 2 as a protective gas. The total oil loading in the mWPI powder is 50% (w / w).

[0116] Preparation of microencapsulated powder compositions (“mWPI - microencapsulated powder (pH8)”) using mWPI (pH 8 solution) and carbohydrate encapsulants

[0117] Adjust the WPI solution to pH 8 and modify it as described in Example 1. To the aqueous phase of mWPI, add Dextrose Monohydrate (14.50% (w / w)), dry glucose syrup (DE value of 30) (15.10% (w / w)), and sodium ascorbate (5.35% (w / w)) at 50 °C. Add refined tuna oil containing mixed natural tocopherols (50.05% (w / w)), and then prepare an emulsion as follows: Produce a coarse emulsion using high-shear mixing at 10,000 rpm for 10 - 15 minutes, and then perform two-stage homogenization 3 passes at 400 / 200 bar (40 / 20 mPa) (total 600 bar (60 mPa)) to produce a refined emulsion. Spray-dry the final oil-in-water emulsion using a bench-top spray dryer with an inlet temperature range and an outlet temperature range of 170 °C and 90 - 100 °C, respectively. Package the produced powder in aluminum bags under N 2 as a protective gas. The total oil loading in the mWPI powder is 50% (w / w).

[0118] Example 7 - Evaluation of the Oxidation Stability of Surface Free Fat and Tuna Oil in Microencapsulated Powders

[0119] Use Oxipres as a rapid and reliable instrumental method to analyze the oxidation stability of the microencapsulated powder. Seal the microencapsulated powder with a total of 4 g of oil in a container and heat it at 70 °C under 5 bar (0.5 mPa) of oxygen. Record the time when the oxygen pressure in the container starts to decline as the induction period (IP), indicating that oxidation has occurred. Figure 3 Shows the Oxipres analysis of microencapsulated powders containing ω-3 oil compared to microencapsulated powders containing ω-3 oil encapsulated with Maillard reaction products (MRP) as described in US7374788B2.

[0120] Measure the percentage of surface free fat as follows: Subject the powder to petroleum solvent for a short time (15 minutes) to extract surface free fat; remove the wall material / encapsulated oil through filter paper, then evaporate the solvent containing the "washed" fat, and divide the residual weight (i.e., oil) by the weight (g) of the powder used, multiply by 100% to obtain the surface free fat %. The results are shown in Table 5 below.

[0121] Table 5

[0122]

[0123] As Figure 3As shown, the induction period was greatly extended by using the modified protein encapsulant. As shown in Table 5, the mWPI microencapsulated powder had significantly lower surface free fat (SFF) values than uWPI. mWPI (pH 8) had an SFF of less than 1%, which meets typical powder requirements while also providing a high (~50%) oil loading and good oxidative stability. All samples showed good oxidative stability by Oxipres (70 °C, 5 bar), with an IP exceeding 100 hours.

[0124] The good oxidative stability in terms of primary and secondary oxidation properties is further illustrated in Table 6 below, where the microencapsulated powders were subjected to exposure at 40 °C for 4 weeks. By the end of 4 weeks, the peroxide value (POV; 5 meq O 2 / Kg fat) and p-anisidine value (p-AV; 20) values of all samples were well within the specifications.

[0125] Table 6

[0126]

[0127] The sensory attributes of the microencapsulated uWPI and mWPI were also evaluated during a 4-week accelerated exposure period. The results are as Figure 4 and Figure 5 shown. The highest score of 15 indicates excellent quality / attributes. By the end of the storage period, the overall quality of all samples ( Figure 4 ) was rated as good, with no perceivable rancid odor and taste and no fishy odor and taste ( Figure 5 ).

Claims

1. A microencapsulation composition, the microencapsulation composition comprising one or more hydrophobic materials encapsulated by an encapsulating agent, wherein the encapsulating agent comprises one or more modified proteins and / or peptides; and wherein the one or more modified proteins and / or peptides are obtained from a starting protein by subjecting the starting protein to a high-shear process such that the average particle size of the one or more modified proteins and / or peptides is about 70% or less of the average particle size of the starting protein.

2. The microencapsulation composition according to claim 1, having a surface free fat content of less than about 1.8%.

3. The microencapsulation composition according to claim 2, having a surface free fat content of less than about 0.8%.

4. The microencapsulation composition according to any one of claims 1 to 3, wherein the high-shear process is carried out at an alkaline pH.

5. The microencapsulation composition according to claim 4, wherein the high-shear process is carried out at a pH of about 8.

6. The microencapsulation composition according to any one of claims 1 to 5, wherein the high-shear process comprises subjecting the starting protein to a pressure of about 20 mPa to about 300 mPa.

7. The microencapsulation composition according to any one of claims 1 to 6, wherein the high-shear process is a homogenization process or a microfluidization process.

8. The microencapsulation composition according to any one of claims 1 to 7, wherein the modified protein is a modified whey protein.

9. The microencapsulation composition according to any one of claims 1 to 8, wherein the encapsulating agent further comprises one or more carbohydrates, optionally, wherein the one or more carbohydrates are selected from glucose syrup and dextrose monohydrate or a combination thereof.

10. The microencapsulation composition according to claim 9, wherein the ratio of the modified protein component of the encapsulating agent to the carbohydrate component of the encapsulating agent is in the range of about 1:10 to 1:

1.

11. The microencapsulation composition according to any one of claims 1 to 10, wherein the one or more modified proteins and / or peptides are present at about 3% w / w to about 25% w / w based on the total weight of the composition.

12. The microencapsulation composition according to any one of claims 1 to 11, wherein the hydrophobic material comprises one or more long-chain polyunsaturated fatty acids (LCPUFAs).

13. The microencapsulation composition according to claim 12, wherein the LCPUFAs are present in the form of triglycerides and / or in one or more LCPUFA-containing oils.

14. The microencapsulation composition according to claim 13, wherein the one or more oils comprise fish oil, optionally, wherein the fish oil is tuna oil.

15. The microencapsulation composition according to any one of claims 1 to 14, wherein the composition is in the form of an oil-in-water emulsion or a spray-dried powder.

16. A method for protecting a hydrophobic material from oxidative degradation, improving the oxidative stability of a hydrophobic material or reducing the surface free fat of a microencapsulation composition comprising a hydrophobic material, comprising: Subject the starting protein to a high-shear process to produce one or more modified proteins and / or peptides such that the average particle size of the one or more modified proteins and / or peptides is about 70% or less of the average particle size of the starting protein; and encapsulate the hydrophobic material with an encapsulating agent comprising the one or more modified proteins and / or peptides.

17. The method according to claim 16, wherein the high-shear process is carried out at an alkaline pH.

18. The method according to claim 17, wherein the high-shear process is carried out at a pH of about 8.

19. The method according to any one of claims 16 to 18, wherein the hydrophobic material comprises one or more LCPUFAs.

20. A stable emulsion comprising a hydrophobic material, wherein the emulsion further comprises one or more modified proteins and / or peptides, and wherein the one or more modified proteins and / or peptides are obtained from a starting protein by subjecting the starting protein to a high-shear process such that the average particle size of the one or more modified proteins and / or peptides is about 70% or less of the average particle size of the starting protein.

21. The stable emulsion according to claim 20, wherein the high-shear process is carried out at an alkaline pH.

22. The stable emulsion according to claim 21, wherein the high-shear process is carried out at a pH of about 8.

23. The stable emulsion according to any one of claims 20 to 22, wherein the hydrophobic material comprises one or more LCPUFAs.

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