Method for improving long-term dispersion stability

Abstract

The present application aims to improve the long-term dispersion stability of a composition containing plant protein mixed with a heated liquid food product by suppressing a decrease in dispersibility of the composition over a long period of time. The long-term dispersion stability of a composition containing plant protein can be improved by mixing a composition containing plant protein treated with a protein deamidating enzyme with a heated liquid food product.

Description

Technical Field

[0001] This invention relates to a technique for improving the long-term dispersion stability of liquid beverage mixtures containing plant-based proteins, which are obtained by mixing a composition containing plant-based proteins with a hot liquid beverage. Background Technology

[0002] Beverages rich in protein and other nutrients have historically been popular due to their convenient availability of nutrients. In recent years, driven by factors such as the rise of vegetarianism, allergy issues, and religious reasons, plant-based milks, which use grains like peas, rice, and oats, as well as nuts like almonds, cashews, and peanuts as protein sources, are gaining popularity as an alternative to animal milk, such as cow's milk.

[0003] On the other hand, in food and beverage products that use animal milk, when plant-based milk is substituted for animal milk, it is often observed that the same functionality cannot be obtained due to the different types of proteins. An example of this functionality is dispersibility. For example, it is known that if soy milk is added to coffee, a coagulation and insolubility phenomenon occurs (Patent Document 1); and when coconut milk is used in food and beverage products, precipitation occurs during the manufacturing process (Patent Document 2), etc.

[0004] Existing technical documents Patent documents Patent Document 1: Japanese Patent Application Publication No. 2006-158295 Patent Document 2: Japanese Patent Application Publication No. 2003-325147 Summary of the Invention

[0005] The technical problem that the invention aims to solve The aggregation of such plant-based milk (compositions containing plant-based proteins) becomes particularly pronounced when added to hot liquid beverages. Aggregation occurring when plant-based protein compositions are added to hot liquid beverages or similar liquid drinks is due to the sudden exposure of the plant-based protein composition to the hot liquid beverage, resulting in a rapid temperature rise, or, in addition to a rapid temperature rise, a rapid change in pH and / or composition. Furthermore, starting with the aggregation that occurs at this point, aggregation continues over time. Therefore, mixtures of plant-based protein-containing liquid beverages obtained by mixing plant-based protein compositions with hot liquid beverages not only have poor dispersibility at the time of mixing (initial dispersibility) but also experience further reduction in dispersibility over time, resulting in poor dispersion stability.

[0006] Therefore, the objective of this invention is to improve the long-term dispersion stability of a composition containing plant-based proteins that is mixed with heated liquid beverages over a long period of time by suppressing the decrease in dispersibility.

[0007] Technical solutions for solving technical problems In the course of repeated research into the aforementioned issues, the inventors discovered that by pre-treating a liquid composition containing plant-based proteins with a protein deamidase before mixing it with a heated liquid beverage, the decline in dispersion state that occurs over a long period after mixing with the heated liquid beverage can be suppressed, i.e., long-term dispersion stability can be improved. This invention was completed based on further repeated research following this discovery.

[0008] That is, the present invention provides an invention in the manner described below.

[0009] Item 1. A method for improving the long-term dispersion stability of a composition containing plant protein, comprising: a step of mixing a composition containing plant protein treated with a protein deamidase with a heated liquid beverage.

[0010] Item 2. The method described in Item 1, wherein the plant protein is selected from legumes (grains), cereals and seeds.

[0011] Item 3. The method described in Item 1 or 2, wherein the plant protein is a protein selected from plants such as soybeans, corn, peanuts, cashews, hazelnuts, walnuts, and coconuts.

[0012] Item 4. A liquid beverage mixture containing plant-based protein, obtained by mixing a composition containing plant-based protein treated with protein deamidase with a heated liquid beverage, and intended for consumption after being stored for more than 60 minutes after mixing.

[0013] Invention Effects According to the present invention, the long-term dispersion stability of a composition containing plant-based proteins mixed with heated liquid beverages can be improved by suppressing the decrease in dispersibility over a long period of time. Detailed Implementation

[0014] 1. Methods to improve long-term dispersion stability The method for improving long-term dispersion stability of the present invention is characterized by comprising a step of mixing a composition containing plant-based proteins treated with a protein deamidase with a heated liquid beverage. In the present invention, "long-term" refers to a time of 20 minutes or more after mixing with the heated liquid beverage. Preferably, a long-term duration is 30 minutes or more, more preferably 60 minutes or more, further preferably 120 minutes or more, and even more preferably 240 minutes or more. There is no particular limitation on the upper limit of this time; for example, durations of 480 minutes or less, 300 minutes or less, 250 minutes or less, 150 minutes or less, 100 minutes or less, 60 minutes or less, or 40 minutes or less are possible. Specific ranges for a long time include, for example, 20 minutes to 480 minutes, 30 minutes to 480 minutes, 60 minutes to 480 minutes, 120 minutes to 480 minutes, 240 minutes to 480 minutes, 20 minutes to 300 minutes, 20 minutes to 250 minutes, 20 minutes to 150 minutes, 20 minutes to 100 minutes, 20 minutes to 60 minutes, or 20 minutes to 40 minutes, etc.

[0015] Furthermore, the improved long-term dispersion stability refers to the suppression of the decrease in dispersibility of the plant protein-containing composition when mixed with heated liquid beverages over a long period of time, compared to the case where the composition containing plant protein has not been treated with protein deamidase.

[0016] 1-1. A composition containing plant-based protein treated with protein deamidase The composition containing plant protein treated with protein deamidase (hereinafter also referred to as "enzyme-treated composition containing plant protein") is obtained by treating a liquid composition containing plant protein with a protein deamidase.

[0017] 1-1-1. A liquid composition containing plant-based proteins As for liquid compositions containing plant proteins that are treated by protein deamidases, there are no particular limitations as long as they contain both plant proteins and water. Specific forms of liquid compositions containing plant proteins include: (i) liquids obtained by using dried powder of plant materials (organs or parts of plants from which the plant protein originates) as the plant material, dispersing the plant material or its aqueous extracts in water, and further removing water-insoluble matter derived from the plant material by any means such as centrifugal filtration, filtration, filter bags, or sieves, as needed; and (ii) liquids obtained by using the plant material itself or its dried form as the plant material, breaking down and dispersing the plant material or its aqueous extracts in water, and further removing water-insoluble matter derived from the plant material by any means such as centrifugal filtration, filtration, filter bags, or sieves, as needed. (iii) A liquid obtained by means of a plant material; (iv) A liquid obtained by using the plant material itself or a micronized product (powder, puree, paste, etc.) of its dried product as a plant material and diluting the micronized product with water; (v) A liquid obtained by treating any of the liquids described in (i) to (iii) above to remove part or all of the components other than plant protein, thereby increasing the content ratio of plant protein; (vi) A liquid obtained by using a dried powder prepared from any of the liquids described in (i) to (iv) above as a plant material and dissolving and / or dispersing the plant material or its aqueous extract in water.

[0018] As a plant-based raw material, there are no particular limitations as long as it contains plant-based protein. Examples include: legumes (soybeans, peas, lentils, chickpeas, black beans, broad beans, mung beans, lupins, kidney beans, etc.); cereals (wheat, barley, oats, sorghum, rice, rye, buckwheat, barnyard millet, chestnuts, teff, corn, potatoes, etc.); and seeds (almonds, coconuts, peanuts, cashews, hazelnuts, pecans, macadamia nuts, pistachios, walnuts, Brazil nuts, pili nuts, chestnuts, sesame seeds, pine nuts, hemp seeds (industrial hemp), chia seeds, quinoa, amaranth seeds, canary grass seeds, flax seeds, etc.). Furthermore, plant-based protein is preferably natural protein, but it can also be any of the following: partially broken down by acid or alkali, chemically modified by various reagents, or synthesized protein.

[0019] In this invention, the plant protein may be derived from a single plant material or from a combination of two or more of the aforementioned plant materials.

[0020] Among the aforementioned plant-based raw materials, soybeans, coconuts, hazelnuts, cashews, peanuts, walnuts, and corn are preferred. From the viewpoint of further improving long-term dispersion stability and enhancing the effect, soybeans, coconuts, hazelnuts, cashews, and peanuts are more preferred, and soybeans and coconuts are even more preferred.

[0021] The content of plant-based protein in the liquid composition containing plant-based protein can be, for example, 0.001% by weight or more, preferably 0.01% by weight or more, or 0.1% by weight or more, more preferably 0.2% by weight or more, or 0.3% by weight or more, and even more preferably 0.4% by weight or more. There is no particular limitation on the upper limit of this content range; for example, it can be 50% by weight or less, preferably 40% by weight or less, 30% by weight or less, 20% by weight or less, or 15% by weight or less, more preferably 10% by weight or less, 7.5% by weight or less, 5% by weight or less, 2.5% by weight or less, 2% by weight or less, 1.5% by weight or less, 1% by weight or less, or 0.75% by weight or less. Specific ranges for the content of plant-based protein in a liquid composition containing plant-based protein include, for example, 0.001 wt% to 50 wt%, 0.001 wt% to 40 wt%, 0.01 wt% to 30 wt%, 0.01 wt% to 20 wt%, 0.1 wt% to 15 wt%, 0.1 wt% to 10 wt%, 0.2 wt% to 7.5 wt%, 0.2 wt% to 5 wt%, 0.3 wt% to 2.5 wt%, 0.3 wt% to 2 wt%, 0.4 wt% to 1.5 wt%, 0.4 wt% to 1 wt%, or 0.4 wt% to 0.75 wt%.

[0022] The content (dry weight equivalent) of plant material in a liquid composition containing plant protein can be, for example, 0.1% to 70% by weight, 0.2% to 60% by weight, or 0.3% to 50% by weight, preferably 0.5% to 40% by weight, or 0.7% to 30% by weight, and more preferably 0.8% to 20% by weight, or 0.8% to 18% by weight.

[0023] In a liquid composition containing plant-based proteins, the composition may include one or more of any other ingredients besides the plant-based protein, or it may not include any other ingredients. Examples of other ingredients include components other than the plant-based protein source, other food ingredients, and food additives. Examples of food additives include thickeners, binders, flavorings, pH adjusters, buffers, colorings, and fragrances.

[0024] 1-1-2. Protein deamidases As for the protein deamidase used to process the liquid composition containing plant protein, there are no particular limitations on its type and source, as long as it is an enzyme that does not involve the cleavage of peptide bonds or the cross-linking of proteins and exhibits the function of decomposing the amide-containing side chains of proteins.

[0025] Examples of protein deamidases include enzymes that deamidate glutamine residues in proteins to glutamate (e.g., protein glutaminase) and enzymes that deamidate asparagine residues in proteins to aspartic acid (e.g., protein asparaginase).

[0026] More specific examples of protein deamidases include those derived from the genera *Chryseobacterium*, *Flavobacterium*, *Empedobacter*, *Sphingobacterium*, *Aureobacterium*, *Myroides*, *Luteimicrobium*, *Agromyces*, *Microbacterium*, or *Leifsonia*. These protein deamidases are well-known and can be referenced, for example, in JP2000-50887A, JP2001-218590A, WO2006 / 075772A1, and WO2015 / 133590. These protein deamidases can be used alone or in combination.

[0027] Among these protein deamidases, from the viewpoint of further improving the effect of long-term dispersion stability, protein glutaminase is preferably mentioned, more preferably protein glutaminase derived from the genus Chryseobacterium, and even more preferably protein glutaminase derived from the species Chryseobacterium proteolyticum.

[0028] Protein deamidases can be prepared from the culture medium of microorganisms that serve as the source of the aforementioned protein deamidases. Specific preparation methods include recovering the protein deamidase from the culture medium or bacterial cells of these microorganisms. For example, when using protein deamidase-secreting microorganisms, the bacterial cells can be recovered from the culture medium beforehand by filtration, centrifugation, etc., and the enzyme can then be separated and / or purified. Alternatively, when using non-secreting protein deamidase microorganisms, the bacterial cells can be recovered from the culture medium beforehand, and the enzyme can be exposed by pressure treatment, ultrasonic treatment, etc., after the bacterial cells are broken up, and then the enzyme can be separated and / or purified. Known protein separation and / or purification methods can be used without particular limitation, such as centrifugation, UF concentration, salting out, and various chromatographic methods using ion exchange resins. The separated and / or purified enzyme can be powdered by freeze-drying, vacuum drying, or other drying methods. Alternatively, appropriate excipients and / or drying aids can be used in these drying methods to achieve powdering. Alternatively, the isolated and / or purified enzymes can be liquefied enzymes obtained by adding appropriate additives and then filtration sterilization.

[0029] Regarding the amount of protein deamidase used, based on the protein deamidase activity per 1g of plant protein, it can be used, for example, at a rate of 0.05U or more. From the viewpoint of further improving the long-term dispersion stability, preferably 0.1U or more, or 0.5U or more, more preferably 0.8U or more, 1U or more, 2U or more, 3U or more, or 4U or more. There is no particular upper limit to the range of protein deamidase usage, based on the protein deamidase activity per 1g of plant protein, for example, 50U or less, 30U or less, 10U or less, 9U or less, 8U or less, 7U or less, 6U or less, 5U or less, 4U or less, 3U or less, 2U or less, or 1.5U or less. The specific range for the amount of protein deamidase used is calculated based on the protein deamidase activity per 1g of plant protein. Examples include 0.05U–50U, 0.1U–30U, 0.5U–10U, 0.8U–9U, 0.8U–8U, 0.8U–7U, 0.8U–6U, 1U–5U, 1U–3U, 1U–2U, 1U–1.5U, 2U–6U, 2U–5U, 3U–5U, 4U–5U, or 2U–3U.

[0030] Regarding the activity of protein deamidases, using benzyloxycarbonyl-L-glutamine glycine (Z-Gln-Gly) as a substrate, 1 free protein was released within 1 minute. μ The amount of enzyme in mol of ammonia is taken as 1 unit (1U).

[0031] In the enzyme treatment step of the method for improving long-term dispersion stability of the present invention, enzymes other than protein deamidases may not be used concurrently, provided that the effect of the present invention is not impaired. Examples of such enzymes, whether used concurrently or not, include protein-cleaving enzymes (proteases, peptidases, etc.), protein cross-linking enzymes (laccases, transglutaminases, etc.), lipid-degrading enzymes (lipases, etc.), and starch-degrading enzymes (amylases, etc.). In a preferred embodiment of the present invention, enzymes other than protein deamidases are not used concurrently.

[0032] 1-1-3. Protein deamidase treatment conditions The conditions for treating liquid compositions containing plant proteins with protein deamidase are not particularly limited as long as they can improve the long-term dispersion stability of the liquid compositions containing plant proteins. The reaction temperature and reaction time can be set appropriately.

[0033] Specifically, the temperature conditions can be determined based on the optimal temperature of the protein deamidase used, for example, 20°C to 65°C, preferably 40°C to 60°C, more preferably 45°C to 55°C, and even more preferably 47°C to 53°C.

[0034] The pH condition can be determined based on the optimal pH of the protein deamidase used. For example, a pH of 4 to 9 can be used at 25°C, preferably 5 to 8, and more preferably 6 to 8.

[0035] The reaction time can be determined based on the reaction scale, for example, 0.5 hours to 24 hours, preferably 0.5 hours to 12 hours, and more preferably 1 hour to 6 hours, or 1.5 hours to 2.5 hours.

[0036] After the reaction, post-processing such as enzyme inactivation and homogenization can be performed as needed.

[0037] 1-1-4. Characteristics, etc. The properties of a composition containing plant-based protein that has been treated with protein deamidase (a composition containing plant-based protein that has been treated with enzymes) when mixed with a heated liquid beverage can be either in a liquid state or a dry state.

[0038] Furthermore, the temperature at which the enzyme-treated composition containing plant protein is mixed with the heated liquid beverage is not particularly limited, as long as it is lower than the temperature of the heated liquid beverage. Preferred examples of the temperature at which the enzyme-treated composition containing plant protein is mixed with the heated liquid beverage include, for example, 1°C to 25°C, more preferably 1°C to 15°C, more preferably 1°C to 10°C, and even more preferably 1°C to 5°C or 2°C to 5°C.

[0039] 1-2. Heated liquid beverages Regarding the degree of heating of the heated liquid beverage, there is no particular limitation as long as it results in a decrease in the dispersion state over time after the liquid beverage is mixed with a composition containing plant-based protein (wherein, no protein deamidase treatment is used). Specifically, for example, it is 50°C or higher, preferably 60°C or higher, or 70°C or higher, more preferably 80°C or higher, further preferably 85°C or higher, and most preferably 90°C or higher. The upper limit of the high temperature is, for example, 100°C. Specific temperature ranges for the heated liquid beverage include, for example, 50°C to 100°C, 60°C to 100°C, 70°C to 100°C, 80°C to 100°C, 85°C to 100°C, or 90°C to 100°C.

[0040] There is no particular limitation on the pH of the liquid beverage at this heating temperature, but preferably it is 4 to 6.5, more preferably it is 4.3 to 5.5, and even more preferably it is 4.5 to 5.2.

[0041] As liquid beverages, examples include soft drinks and liquid foods. A soft drink refers to a liquid (a substance capable of becoming a final product) ingested through the act of direct consumption; a typical example is a beverage. A liquid food refers to a liquid dish (a substance capable of becoming a final product), or a liquid intermediate or raw material (which may also contain additives) used to manufacture the aforementioned soft drinks or dishes.

[0042] Specific examples of beverages include: coffee (containing 5.0g or more of green coffee beans per 100g), coffee beverages (containing 2.5g or more but less than 5.0g of green coffee beans per 100g), tea (tea extracts such as black tea, green tea, and oolong tea, concentrated and reduced extracts, and liquids obtained by diluting dried extracts (freeze-dried products, etc.) with water), tea beverages (beverages obtained by adding flavorings, sweeteners, animal milk, and / or fruit juice to tea (e.g., flavored tea, milk tea, lemon tea, etc.)), fruit juice (juicing of fruit, concentrated and reduced extracts, and liquids obtained by diluting dried juices (freeze-dried products, etc.) with water), fruit juice beverages (beverages obtained by adding flavorings, sweeteners, and / or animal milk to fruit juice), cocoa and chocolate beverages, and isotonic beverages (sports drinks, etc.). Specific examples of liquid foods, as final product forms, include: nutritional supplements (protein drinks, nursing drinks, etc.), soups (bouillon soups, stews, broccoli soups, beetroot soups, vegetable soups (e.g., tomato soup, corn soup, thick soup, pumpkin soup, etc.), miso soup, etc.), curries, etc., as well as liquid intermediates or raw materials used to manufacture them (e.g., vegetable juice, broth, etc.).

[0043] In a preferred embodiment of the method for improving long-term dispersion stability of the present invention, coffee is used in a beverage, enabling the enzyme-treated composition containing plant-based proteins to be used as a plant-based coffee creamer, plant-based milk, or plant-based cream.

[0044] 1-3. Liquid food and beverage mixtures containing plant-based protein By mixing an enzyme-treated composition containing plant-based proteins with a heated liquid beverage, a liquid beverage mixture containing plant-based proteins can be obtained.

[0045] The mixing ratio of the enzyme-treated composition containing plant protein to the heated liquid beverage can be appropriately determined based on the type of beverage being replaced by the liquid beverage mixture containing plant protein. For example, regarding this mixing ratio, a ratio of 0.01% to 2% by weight of plant protein in the enzyme-treated composition to the liquid beverage mixture containing plant protein is preferred. From the viewpoint of further improving the effect of long-term dispersion stability, a ratio of 0.01% to 1% by weight is preferred, more preferably 0.01% to 0.5% by weight, even more preferably 0.01% to 0.3% by weight, and even more preferably 0.01% to 0.2% by weight or 0.01% to 0.15% by weight is preferred. Furthermore, since the liquid beverage mixture containing plant protein of the present invention exhibits excellent long-term dispersion stability, the mixing ratio can be: the plant protein in the enzyme-treated composition containing plant protein is 0.03% to 2% by weight, 0.05% to 2% by weight, or 0.08% to 2% by weight in the liquid beverage mixture containing plant protein.

[0046] Because liquid beverage mixtures containing plant-based proteins exhibit excellent long-term dispersion stability, they can be stored for a specified period from preparation (i.e., after mixing the enzyme-treated composition containing plant-based proteins with a heated liquid beverage) until consumption. Examples of storage times include, for instance, 20 minutes or more, preferably 30 minutes or more, more preferably 60 minutes or more, even more preferably 120 minutes or more, and even more preferably 240 minutes or more. There is no particular limitation on the upper limit of the storage time; for example, it may be less than 480 minutes, less than 300 minutes, less than 250 minutes, less than 150 minutes, less than 100 minutes, less than 60 minutes, or less than 40 minutes. Specific ranges for storage time include, for example, 20 minutes to 480 minutes, 30 minutes to 480 minutes, 60 minutes to 480 minutes, 120 minutes to 480 minutes, 240 minutes to 480 minutes, 20 minutes to 300 minutes, 20 minutes to 250 minutes, 20 minutes to 150 minutes, 20 minutes to 100 minutes, 20 minutes to 60 minutes, or 20 minutes to 40 minutes.

[0047] Example The present invention will be specifically described below with examples, but the present invention is not to be construed as being limited to the following examples.

[0048] [Experimental Example 1] (1. Experimental methods) [A. Materials] • Plant-based protein materials: Use the materials shown in Table 1 below.

[0049] [Table 1]

[0050] Commercially available instant coffee: Nestle's "NESCAFE GOLD BLEND" • Protein deamidase: Protein glutaminase (PG) [B. Protein Deamidase Activity Assay] Add 0.1 mL of the sample solution containing protein deamidase to 1 mL of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, incubate at 37 °C for 10 minutes, then add 1 mL of 0.4 MtCA solution to stop the reaction. As a blank, add 1 mL of 0.4 MtCA solution to 1 mL of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, then add 0.1 mL of the sample solution containing protein deamidase, and incubate at 37 °C for 10 minutes.

[0051] For the solution obtained above, the amount of ammonia generated in the reaction solution was determined using Ammonia-testWako (Fujifilm and Koden Chemical). A calibration curve showing the relationship between ammonia concentration and absorbance (630 nm) was prepared using an ammonia standard solution (ammonium chloride), and the ammonia concentration in the reaction solution was determined using this calibration curve.

[0052] 1 will be generated within 1 minute μ The enzyme content of mol of ammonia is taken as 1 unit (1U), and the activity of protein deamidase is calculated by the following formula. In the formula, the reaction solution volume is 2.1, the enzyme solution volume is 0.1, and Df is the dilution factor of the enzyme solution. Additionally, 17.03 is the molecular weight of ammonia.

[0053] [Number 1]

[0054] [C. Production of plant-based milk using protein deamidases] The material shown in “A. Material” above was diluted with tap water to a protein concentration of 0.5% by weight to prepare plant-based milk (a neutral liquid composition containing plant protein). For the plant-based milk, PG was added at a rate of 1 U, 2.5 U, or 5 U per 1 g of plant protein, reacted at 50°C for 2 hours, and homogenized at 2500 psi to prepare PG-treated plant-based milk (for the examples). Alternatively, the same treatment was performed without adding PG to prepare untreated plant-based milk (for the comparative examples).

[0055] [D. Evaluation of long-term dispersion stability] 10 mL of PG-treated plant-based milk (for the example) or untreated plant-based milk (for the comparative example) obtained in "C. Manufacturing of Plant-Based Milk Treated with Protein Deamidase" (4°C) above, and 40 mL of hot coffee (90°C, pH approximately 5 at this temperature) prepared by dissolving commercially available instant coffee shown in "A. Materials" above in hot water, were mixed to prepare a liquid beverage mixture (coffee containing plant-based milk), and then allowed to stand directly. At various time points, including 0 minutes after mixing (immediately after preparation) and 20 minutes later, samples were taken from the upper layer of the coffee containing plant-based milk, and the turbidity (absorbance at 660 nm) was measured. A higher absorbance value indicates higher dispersibility. The absorbance at 660 nm of the upper layer after 0 minutes of mixing was set as 100%, and the relative value (%) of the absorbance at 660 nm of the upper layer at each sampling time point was derived. A larger relative value indicates that the reduction in dispersibility is more suppressed. The results are shown in Tables 2-8.

[0056] (2. Experimental Results) [Table 2]

[0057] [Table 3]

[0058] [Table 4]

[0059] [Table 5]

[0060] [Table 6]

[0061] [Table 7]

[0062] [Table 8]

[0063] The inventors confirmed that coffee containing plant-based milk prepared by adding untreated plant-based milk to hot coffee exhibited poor dispersibility (agglomeration) during preparation, while coffee containing plant-based milk prepared by adding PG-treated plant-based milk to hot coffee exhibited good dispersibility (no agglomeration) during preparation. Furthermore, as shown in Tables 2-8, coffee containing plant-based milk prepared by adding untreated plant-based milk to hot coffee showed a decline in dispersion over a long period (Comparative Examples 1-7), while this deterioration in dispersion was suppressed in coffee containing plant-based milk prepared by adding PG-treated plant-based milk to hot coffee, thus confirming the improvement in dispersion stability (Examples 1-10).

[0064] Furthermore, for soy milk, coconut milk, hazelnut milk, cashew milk, and peanut milk, coffee containing plant-based milk prepared by adding untreated plant-based milk to hot coffee exhibited extremely poor dispersion stability over a long period of time (Comparative Examples 1-5). However, coffee containing plant-based milk prepared by adding treated plant-based milk to hot coffee improved this extremely poor dispersion stability (Examples 1-8). Among these, the improvement in dispersion stability was particularly high for soy milk and coconut milk (Examples 1-5).

Claims

1. A method for improving the long-term dispersion stability of a composition containing plant-based protein, characterized in that, Includes: a process of mixing a composition containing plant-based protein that has been treated with protein deamidase with a heated liquid beverage.

2. The method according to claim 1, wherein, The plant protein is selected from legumes, cereals, and seeds.

3. The method according to claim 1, wherein, The plant-based protein is selected from the proteins of plants such as soybeans, corn, peanuts, cashews, hazelnuts, walnuts, and coconuts.

4. A liquid beverage mixture containing plant-based protein, characterized in that, It is obtained by mixing a composition containing plant-based protein treated with protein deamidase with a heated liquid beverage, and is intended to be consumed after being stored for more than 60 minutes after mixing.

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