Patent Application
20240415148
The present invention relates to fluid gels which can impart stickiness-free viscosity and a rich taste, good melt in mouth, foaming property, and the like to semi-solid foods, and which itself is superior in emulsifying property, and production methods thereof, emulsifiers and semi-solid foods containing the fluid gel, and the like.
Generally, in semi-solid foods such as yoghurt, mayonnaise, whipped cream, and the like, thickeners such as saccharides, starch, and the like are added to increase the viscosity. When, for example, a thickener is added to low-fat mayonnaise, the melt in mouth becomes poor, giving rise to a sticky texture. In recent years, on the other hand, due to changes in consumer needs, there has been an increasing demand for alternative foods such as low-fat and low-calorie foods and foods that use plant proteins instead of animal proteins. In those alternative foods, one of the goals is provision of properties similar to those of the original foods. Also in semi-solid foods, for example, since low-fat mayonnaise and mayonnaise made with plant proteins instead of animal proteins are too thin, thickeners, emulsifiers, and the like are added, but the addition of these causes a sticky texture. In addition, whipped cream made with vegetable fat does not foam well as compared with whipped cream made with fresh cream. Therefore, there is a demand for components, compositions, and the like that can impart semi-solid foods with viscosity free of stickiness, foaming property, and the like.
For property improvement in semi-solid foods, a creamer containing sugar, fat, and a protein having a spherical protein denaturation degree within a specific range, and having a viscosity within a specific range is known as a creamer that can achieve long-term stability, high whitening ability, and a pleasant mouthfeel (JP 2014-512193 A, which is incorporated herein by reference in its entirety). In addition, an edible composition containing water, a fat phase, microgel particles, a stabilizing emulsifier, and an unstabilizing emulsifier, which has an elastic modulus within a specific range, has properties similar to those of mayonnaise or a spread, and can be spooned or spread is known (JP 2003-506061 A, which is incorporated herein by reference in its entirety). Also, a method for producing ice cream and the like having a rich and smooth texture is known, in which a frozen gel obtained by heating and then freezing a whey protein concentrate, which is a protein gel, is used as a fat substitute (JP H03-280834 A, which is incorporated herein by reference in its entirety). However, none of these provide a satisfactory balance of stickiness, viscosity, rich taste, melt in mouth, and the like, or improve the balance of these.
On the other hand, methods using enzymes have been developed as a technique for modifying foods. For example, transglutaminase is an enzyme that catalyzes the cross-linking of proteins and is widely used as an adhesive enzyme for food materials. In addition, protein gelation by transglutaminase is known (JP S64-27471 A and JP H06-113844 A, which are incorporated herein by reference in their entireties).
As methods for producing food gels, a method including dissolving agar or the like in hot water and cooling the solution while stirring, a method including heating protein such as whey while stirring, and the like are known.
Accordingly, it is an object of the present invention to provide a fluid gel which can impart stickiness-free viscosity and a rich taste, good melt in mouth, foaming property, and the like to semi-solid foods, and which itself is superior in emulsifying property, and a production method thereof, emulsifiers and semi-solid foods containing the fluid gel, and the like.
This and other objects, which will become apparent during the following detailed description, have been achieved by the present inventors' discovery that a fluid gel can be obtained by stirring a solution containing a protein and transglutaminase, and that addition of this fluid gel to low-fat mayonnaise, whipped cream using vegetable fat, and the like can provide properties closer to those of full-fat mayonnaise and whipped cream produced by stirring high-fat raw milk, respectively; specifically, viscosity and texture that are free of stickiness, good foaming property, and good melt in mouth, and have completed the present invention by conducting further studies based on such finding.
Accordingly, the present invention provides the following.
The present invention can provide a fluid gel which can impart good properties such as stickiness-free viscosity and rich taste, good melt in mouth, foaming property, and the like to semi-solid foods, and which itself is superior in emulsifying property.
A more complete appreciation of the invention and many of the attendant advantages thereof will be readily obtained as the same become better understood by reference to the following detailed description when considered in connection with the accompanying drawings, wherein:
The present invention provides a method for producing a fluid gel, including stirring a solution containing a protein and transglutaminase (hereinafter to be referred to as “the production method of the present invention”).
In the present specification, the “fluid gel” is also called “liquid gel”, “fluid-state gel”, “fluid gel” and the like, and refers to an aggregate in which microgels are dispersed. Fluid gels have fluidity as a whole while gelling in the microgel parts, and behave differently from general gels which gelatinize as a whole, lose fluidity, and behave like a solid. In the present invention, the microgel is a microgel whose dispersoid is a protein treated with transglutaminase. The particle size of the microgel is not particularly limited. For example, the proportion of gel particles that pass through a 10,000 μm sieve is preferably not less than 50 wt %, more preferably not less than 70 wt %, further preferably not less than 90 wt %, of the total amount of the fluid gel.
The particle size of the fluid gel obtained by the production method of the present invention is preferably 0.1 μm to 1,000 μm as the median diameter (D50 particle size; hereinafter also referred to as “D50 particle size”), more preferably 0.1 μm to 500 μm, further preferably 0.1 μm to 200 μm. The median diameter can be measured, for example, using a laser diffraction⋅scattering particle size distribution measuring device LA-960 (Horiba, Ltd.).
As the dispersion medium constituting the fluid gel, water suitable for use in food production, such as purified water, distilled water, deionized water, tap water, and the like is preferred. Also, buffer solutions such as acetate buffer, phosphate buffer, and aqueous solutions suitable for use in food production, such as an aqueous sodium carbonate solution, can be used. The content of these dispersion media in the fluid gel is preferably 0.1 wt % to 30 wt %, more preferably 0.5 wt % to 20 wt %, and further preferably 1 wt % to 15 wt %.
Proteins include plant proteins, animal proteins, and mixtures of these, and the like.
Plant proteins are proteins derived from plants or compositions containing them, and also include those in which the protein content has been increased by processing plants. Specific examples of the plant protein include soy protein, wheat protein, green pea protein, mung bean protein, broad bean protein, green soy protein, rape seed protein, chia seed protein, corn protein, rice protein, buckwheat protein, sweet potato protein, asparagus protein, broccoli protein, avocado protein, oat protein, almond protein and the like, and soy protein is preferred.
More specifically, the plant protein is not particularly limited as long as it contains a protein derived from a plant. For example, the soy protein is not particularly limited as long as it contains a protein derived from soybeans, and refers to proteins that can be obtained by processing soybeans, such as concentrated soy protein, isolated soy protein, fibrous soy protein, extracted soy protein, and the like. Specific examples include, but are not limited to, “New FUJIPRO SEH” (Fuji Oil Co., Ltd.).
Operations such as plant processing, plant protein separation, and the like can be performed by a conventional method, for example, operations such as soybean processing, soy protein separation, and the like, and can be performed according to the methods described in Journal of the Japan Oil Chemists' Society, Vol. 19, No. 8, p. 826 (1970), Journal of the Japan Oil Chemists' Society, Vol. 28, No. 10, p. 781 (1979), which are incorporated herein by reference in their entireties, and the like, or methods similar thereto.
As the plant protein, one type of plant protein may be used, or two or more types of plant proteins may be used.
Animal protein is a protein derived from an animal or a composition containing the same, and specific examples include milk protein (whey protein, casein protein, etc.), egg white protein, meat protein, fish protein, etc., of which milk protein or egg white protein is preferred, and casein protein is particularly preferred.
More specifically, the animal protein is not particularly limited as long as it contains a protein derived from an animal. For example, casein protein is not particularly limited as long as it contains a protein fraction obtained by removing whey and milk fat from raw milk, and refers to proteins such as micellar casein and sodium caseinate.
The animal protein may be prepared by oneself or may be a commercially available product such as “Sodium Caseinate 180” (Fonterra Japan K.K.) and the like.
As the animal protein, one type of animal protein may be used, or two or more types of animal proteins may be used.
Transglutaminase (TG) is an enzyme that has the activity of catalyzing an acyl transfer reaction in which a glutamine residue in a protein or peptide is used as a donor and a lysine residue is used as a receptor, and transglutaminase of various origins is known, such as those derived from mammals, those derived from fish, and those derived from microorganisms. The origin of the transglutaminase used in the present invention is not particularly limited as long as it has the aforementioned activity, and transglutaminase of any origin may be used, and recombinant enzymes may also be used. The transglutaminase used in the present invention may be a commercially available product, and specific examples include, but are not limited to, microorganism-derived transglutaminase commercially available under the trade names “Activa (registered trademark) TG-AK” (Ajinomoto Co., Inc.), “Activa (registered trademark) TG-S” (Ajinomoto Co., Inc.), “Activa TG (registered trademark)” (Ajinomoto Co., Inc.), and the like.
The amount of transglutaminase used in the production method of the present invention is not particularly limited, and may vary depending on the production conditions. It is preferably an amount that is 0.001 U (unit) to 1,000 U, more preferably an amount that is 0.01 U to 500 U, and further preferably an amount that is 0.1 U to 100 U, per 1 g of protein.
In the present invention, the activity unit of transglutaminase is measured and defined as follows. That is, transglutaminase is allowed to act in a reaction system in which benzyloxycarbonyl-L-glutamylglycine and hydroxylamine are used as substrates in Tris buffer at 37° C. and pH 6.0, and the hydroxamic acid produced is allowed to form an iron complex in the presence of trichloroacetic acid. The absorbance at 525 nm is then measured, and the amount of hydroxamic acid is calculated using a calibration curve, and the amount of enzyme required to produce 1 μmol of hydroxamic acid per minute is defined as 1 unit (1 U) (see JP S64-27471 A).
As solvents for the solution, water suitable for use in food production, such as purified water, distilled water, deionized water, tap water, and the like is preferably used. Buffer solutions such as acetate buffer and phosphate buffer, and aqueous solutions suitable for use in food production, such as an aqueous sodium carbonate solution, can also be used.
The concentration of the protein in the solution is preferably 0.1 wt % to 40 wt %, more preferably 0.5 wt % to 30 wt %, and further preferably 1 wt % to 20 wt %.
The temperature at which the solution containing the mixture of protein and transglutaminase is stirred is preferably a temperature at which the protein does not denature, and depends on other conditions, but is preferably 0° C. to 60° C., more preferably 10° C. to 60° C., further preferably 20° C. to 50° C. The stirring speed when the solution is stirred depends on other conditions. For example, 100 rpm to 30,000 rpm is preferred, 150 rpm to 20,000 rpm is more preferred, and 200 rpm to 15,000 rpm is further preferred. In one embodiment, 1,000 rpm to 30,000 rpm is more preferred and 2,000 rpm to 20,000 rpm is further preferred. Depending on other conditions, for example, a stirring speed of 100 rpm or more is preferred because it is less likely to cause the entire solution to gelatinize as it is. While the stirring time when the solution is stirred depends on other conditions, it is preferably 1 minute to 12 hours, more preferably 5 minutes to 6 hours, and further preferably 10 minutes to 3 hours.
In one embodiment, the production method of the present invention can be performed by stirring the solution containing the protein while adding transglutaminase.
In the production method of the present invention, components other than the protein and transglutaminase may be added as long as they do not impair the effects of the present invention. Examples of other components include other enzymes such as glucose oxidase and the like, alkaline agents (pH adjusters) such as sodium carbonate, potassium carbonate, calcined calcium, and the like, redox agents such as sodium ascorbate, glutathione, cysteine, and the like, and the like. As the other components, one type of component may be used, or two or more types of components may be used in combination.
In the production method of the present invention, the timing of adding the above-mentioned other components to the solution containing the protein and transglutaminase is not particularly limited.
In the production method of the present invention, the amount of other components to be used is not particularly limited, but is preferably an amount that is not more than 10 wt %, more preferably an amount that is not more than 5 wt %, and further preferably an amount that is not more than 1 wt %, in the solution containing the protein and transglutaminase.
The present invention also provides a fluid gel containing a protein treated with transglutaminase, and having a median diameter of 0.1 μm to 1000 μm.
Transglutaminase, protein, fluid gel, and median diameter are as explained above in the production method of the present invention. The method of making transglutaminase act on protein is not particularly limited. An example is a method of stirring a solution containing a mixture of protein and transglutaminase as explained above in the production method of the present invention.
The present invention also provides a fluid gel containing a protein treated with transglutaminase and satisfying one or more of the following properties at 25° C. (hereinafter referred to as the “fluid gel of the present invention”):
In one embodiment, the present invention provides a fluid gel containing a protein treated with transglutaminase, which satisfies two or more of the above-mentioned properties (1) to (3) at 25° C.
In one embodiment, the present invention provides a fluid gel containing a protein treated with transglutaminase, which satisfies all of the above-mentioned properties (1) to (3) at 25° C.
Transglutaminase, protein, and fluid gel are as explained above in the production method of the present invention. The method of making transglutaminase act on protein is not particularly limited. An example is a method of stirring a solution containing a mixture of protein and transglutaminase as explained above in the production method of the present invention.
The complex modulus refers to the complex expression of the elastic modulus with respect to oscillatory stress and strain in linear viscoelasticity (Chemical Dictionary, 2nd Edition, Morikita Publishing (2009)). The complex modulus can be measured, for example, using a rheometer such as the Stress Controlled Rheometer MCR501 (Anton Paar Japan Co., Ltd.).
In the fluid gel of the present invention, the complex modulus at an angular frequency of 1 rad/sec is preferably 5 Pa to 5,000 Pa, more preferably 10 Pa to 2,000 Pa.
The coordination number is information relating to the spatial distribution of virtual flow unit lattices in the system (RHEOLOGY TORONKAI KOEN YOSHISHU (Proceedings of the Rheology Symposium), vol.: 66th, p. 322-323 (Oct. 17, 2018) which is incorporated herein by reference in its entirety), and the gel strength indicates the strength of the mechanical interaction between the above-mentioned flow unit lattices (RHEOLOGY TORONKAI KOEN YOSHISHU (Proceedings of the Rheology Symposium), vol.: 66th, p. 322-323 (Oct. 17, 2018) which is incorporated herein by reference in its entirety). Both the coordination number and gel strength can be derived from the angular frequency dependence data of the above-mentioned complex modulus using a weak-gel model (J Biorheol, 32 (1), 9-14 (2018), Rheologica Acta, 40, 120-127 (2001), which are incorporated herein by reference in their entireties, etc.). That is, first, the angular frequency dependency data in the angular frequency range of 0.1 to 100 rad/sec is plotted on a graph with the complex modulus (Pa) on the vertical axis and the angular frequency (rad/sec) on the horizontal axis, and an approximate line is drawn on the graph by the least squares method, and when the vertical intercept of the approximate line at an angular frequency of 1 rad/sec is b and the slope of the approximate line is a, the gel strength Af (Pas1/z) in the angular frequency range of 0.1 to 100 rad/sec is expressed as 10b, and the coordination number z is expressed as 1/a. In addition, the complex modulus, coordination number, gel strength, and angular frequency have the following relationship in the weak-gel model (Rheologica Acta, 40, 120-127 (2001) which is incorporated herein by reference in its entirety).
In the formula, G* represents the complex modulus (Pa), Af represents the gel strength (Pas1/z), ω represents the angular frequency (rad/sec), and z represents the coordination number.
In the fluid gel of the present invention, the coordination number in the angular frequency range of 0.1 to 100 rad/sec is preferably 0.1 to 15, more preferably 0.1 to 10. In addition, the gel strength in the angular frequency range of 0.1 to 100 rad/sec is preferably 0.1 Pas1/z to 80 Pas1/z, more preferably 0.1 Pas1/z to 60 Pas1/z.
The shear stress can also be measured using a rheometer such as the Stress Controlled Rheometer MCR501 (Anton Paar Japan Co., Ltd.), and the viscosity coefficient can be analyzed using the shear stress and the shear rate set during measurement with the rheometer, along with the H-B (Herschel-Bulkley) index and yield stress, using the analysis software Universal Software US200 (Paar Physica) according to the following Herschel-Bulkley equation (Kolloid-2, 39, 291 (1926) which is incorporated herein by reference in its entirety), an empirical equation that describes non-Newtonian flow.
In the formula, σ represents shear stress (Pa), k represents viscosity coefficient (Pasn), γ represents shear rate (1/sec), n represents H-B index (no unit), and σy represents yield stress (Pa).
In the fluid gel of the present invention, the shear stress at a shear rate of 10/sec is preferably 2 Pa to 200 Pa, more preferably 5 Pa to 100 Pa. Also, the viscosity coefficient at a shear rate range of 1 to 100/sec is preferably 0.1 Pasn to 80 Pasn, more preferably 0.1 Pasn to 60 Pasn.
The average particle size of the fluid gel of the present invention is preferably 0.1 μm to 1,000 μm, more preferably 0.1 μm to 500 μm, and further preferably 0.1 μm to 200 μm. The average particle size can be measured, for example, using a laser diffraction⋅scattering particle size distribution measuring device LA-960 (Horiba, Ltd.).
The fluid gel of the present invention can be produced, for example, by the above-mentioned production method of the present invention.
In one embodiment, the present invention provides a fluid gel that can be obtained by stirring a solution containing a protein and transglutaminase.
In one embodiment, the present invention also provides a fluid gel that contains a protein treated with transglutaminase, the fluid gel having an average particle size of 0.1 μm to 1,000 μm. This fluid gel can also be produced, for example, by the above-mentioned production method of the present invention.
The present invention also provides an emulsifier containing the fluid gel of the present invention (hereinafter referred to as the “emulsifier of the present invention”).
The emulsifier of the present invention may be the fluid gel of the present invention used alone, or may contain other components as long as the effect of the present invention is not impaired. Examples of other components include other emulsifiers such as sucrose fatty acid ester, glycerol fatty acid ester, sorbitan fatty acid ester, sodium caseinate, lecithin, saponin, and the like, thickeners such as xanthan gum, gellan gum, gum arabic, carrageenan and the like, proteins such as egg white and the like, carbohydrates such as glucose, lactose, and the like, fats and oils such as soybean oil and the like, sweeteners such as aspartame, acesulfame potassium, and the like, flavoring materials such as sodium chloride, sodium L-glutamate, and the like, colorants such as annatto dye, turmeric dye, gardenia dye, and the like, flavors such as ethyl acetoacetate, orange, lavender and the like, preservatives such as benzoic acid, sodium benzoate, sorbic acid, and the like, and the like.
The content of the fluid gel of the present invention in the emulsifier of the present invention is not particularly limited. It is preferably 0.01% to 100 wt %, more preferably 1 wt % to 100 wt %, 10 wt % to 100 wt %, 30 wt % to 100 wt %, or 50 wt % to 100 wt %, further preferably 70 wt % to 100 wt %, or 80 wt % to 100 wt %, particularly preferably 90 wt % to 100 wt %.
The content of the above-mentioned other components in the emulsifier of the present invention is not particularly limited. It is preferably 0.0001 wt % to 30 wt %, more preferably 0.001 wt % to 20 wt %, further preferably 0.01 wt % to 10 wt %, in total.
A method for producing the emulsifier of the present invention is now described.
The emulsifier of the present invention may be produced by using the fluid gel of the present invention as it is, or, for example, by adding the above-mentioned other components to the fluid gel of the present invention and mixing them by a general method.
The emulsifier of the present invention can be added, for example, to emulsified foods, cosmetics, and the like.
The emulsified foods to which the emulsifier of the present invention is added are preferably oil-in-water emulsified foods. Examples of the oil-in-water emulsified food include yoghurt, mayonnaise, whipped cream, ice cream, custard cream, cafe au lait, coffee cream, coffee drinks, and the like.
The content of the emulsifier in the emulsified food is not particularly limited, but is preferably 0.01 wt % to 30 wt %, more preferably 0.05 wt % to 20 wt %, and further preferably 0.1 wt % to 10 wt %. The timing of adding the emulsifier of the present invention to an emulsified food is not particularly limited. For example, it may be mixed together with the other ingredients of the emulsified food, or it may be added after mixing the other ingredients. The emulsifier of the present invention may also be added to an emulsified food in combination with other emulsifiers such as sucrose fatty acid ester, glycerol fatty acid ester, sorbitan fatty acid ester, sodium caseinate, lecithin, saponin, and the like.
Examples of the cosmetics to which the emulsifier of the present invention is added include basic cosmetics such as emulsion, cream, lotion, facial cleanser, and the like, hair cosmetics such as shampoo, rinse, treatment and the like, makeup cosmetics such as liquid foundation and the like, and the like.
The content of the emulsifier in the cosmetics is not particularly limited, but is preferably 0.01 wt % to 80 wt %, more preferably 0.05 wt % to 60 wt %, further preferably 0.1 wt % to 40 wt %. The timing of the addition of the emulsifier of the present invention to a cosmetic is not particularly limited. For example, the emulsifier may be mixed together with the other ingredients of the cosmetic, or may be added after mixing the other ingredients. The emulsifier of the present invention may also be added to a cosmetic in combination with other emulsifiers such as sodium caseinate, saponin, and the like.
The present invention also provides a semi-solid food containing the fluid gel of the present invention (hereinafter to be referred to as “the semi-solid food of the present invention”).
Semi-solid foods include yoghurt, mayonnaise, whipped cream, cafe au lait, dressings, sauces, and the like, and yoghurt, mayonnaise, whipped cream, and cafe au lait are preferred. Here, semi-solid foods include alternative semi-solid foods; for example, mayonnaise includes conventional mayonnaise, as well as alternative mayonnaise such as low-fat mayonnaise and mayonnaise using plant protein instead of animal protein; whipped cream includes whipped cream using milk fat (raw milk) (hereinafter referred to as “milk fat”), which is animal fat with high fat content, as well as alternative whipped cream such as whipped cream using milk fat with low fat content and whipped cream using vegetable fat (hereinafter referred to as “vegetable fat”).
Low-fat mayonnaise, mayonnaise using plant protein instead of animal protein, and the like have a thin viscosity, and therefore, a thickener such as xanthan gum is generally added. This results in a sticky texture, and whipped cream using milk fat with low fat content and whipped cream using vegetable fat have low foaming property. Thus, until now it has been difficult to achieve the properties of conventional mayonnaise and whipped cream using milk fat with high fat content, respectively. Therefore, alternative semi-solid foods such as alternative mayonnaise and whipped cream in place of low-fat mayonnaise, which is prone to problems in terms of property, mayonnaise using plant protein instead of animal protein, whipped cream using milk fat with low fat content, whipped cream using vegetable fat, and the like are more preferred as semi-solid foods.
A method for producing the semi-solid food of the present invention is now described.
The semi-solid food of the present invention can be produced, for example, by adding the fluid gel of the present invention to the raw materials of the food during the production process of the semi-solid food and mixing them by a general method. The raw materials of the food refer to food materials for producing the food, and are not particularly limited as long as the food can be produced, and anything that is generally used as a raw material for the food can be used. The raw materials of the food also include intermediate products of the food at any stage during the production process of the food.
The present invention also provides a method for producing a semi-solid food and a method for improving the property of a semi-solid food, which is characterized by mixing the fluid gel of the present invention with the raw materials of the semi-solid food.
The semi-solid food and the raw materials of the food are each the same as those described above for the semi-solid food of the present invention.
The method for producing a semi-solid food and the method for improving the property of the present invention can be performed, for example, by adding the fluid gel of the present invention to the raw materials of the semi-solid food during the production process of the semi-solid food and mixing them by a general method.
For example, when the semi-solid food is mayonnaise, the property of the mayonnaise is improved (stickiness-free viscosity and a rich taste, good melt in mouth and the like are obtained), when the semi-solid food is whipped cream, the property of the whipped cream is improved (foaming property is improved), and when the semi-solid food is cafe au lait, the property of the cafe au lait is improved (rich taste similar to that of oil and fat, and the mid-to late-stage thickness are imparted).
Other features of the invention will become apparent in the course of the following descriptions of exemplary embodiments which are given for illustration of the invention and are not intended to be limiting thereof.
Soy protein is added to a mixture of 185.9 mL of distilled water and 2.1 mL of 10 mM Na CO3 aqueous solution (pH 10.5), stirred and dissolved in a homomixer at 40° C. and 15,000 rpm for 1 hr, and the mixture is defoamed in a centrifuge at 2,000 rpm for 5 min to obtain a soy protein solution. Transglutaminase is added to the resulting solution, and the mixture is stirred in a homomixer at 40° C. and 5,000 rpm for 30 min. The resulting solution is heated in a microwave oven (900 W, 30 sec), and then heated in an oil bath at 75° C. or higher for 5 min to inactivate the transglutaminase. The solution is then defoamed in a centrifuge at 2,000 rpm for 10 min to obtain a fluid gel.
Soy protein is added to 188.0 mL of distilled water, and 4.0 mL of ethanol is added to preliminarily disperse the soy protein. It is then stirred and dissolved in a homomixer at 60° C. and 15,000 rpm for 1 hr, and defoamed in a centrifuge at 2,000 rpm for 5 min to obtain a soy protein solution. Transglutaminase is added to the resulting solution, and the mixture is stirred in a homomixer at 40° C. and 5,000 rpm for 30 min. The resulting solution is heated in a microwave oven (900 W, 30 sec), and then heated in an oil bath at 75° C. or higher for 5 min to inactivate the transglutaminase. The solution is then defoamed in a centrifuge at 2,000 rpm for 10 min to obtain a fluid gel.
Following the method described in Preparation Example 1, 5 wt %, 6 wt %, and 7 wt % soy protein solutions were obtained from soy protein “New FUJIPRO SEH” (Fuji Oil Co., Ltd.), distilled water, and 10 mM Na CO3 aqueous solution (pH 10.5). Transglutaminase “Activa (registered trademark) TG” was added to each of the obtained solutions so that the concentration thereof was 12.2 U/g, and each was stirred in a homomixer for 30 min at 40° C. and 300 rpm instead of 5,000 rpm. The obtained solutions were heated in a microwave oven (900 W, 30 sec), and then heated in an oil bath at 75° C. or higher for 5 min to inactivate the transglutaminase. The solutions were then defoamed in a centrifuge at 2,000 rpm for 10 min. As a control, the same procedure was performed without adding transglutaminase.
As a result, when transglutaminase was added, a shape resembling a fluid gel particle was visually observed regardless of the concentration of soy protein solution used, but when transglutaminase was not added, a shape resembling a fluid gel particle was not visually observed regardless of the concentration of soy protein solution used.
Following the method described in Preparation Example 1, 5 wt % soy protein solution was obtained from soy protein “New FUJIPRO SEH” (Fuji Oil Co., Ltd.), distilled water, and 10 mM Na CO3 aqueous solution (pH 10.5). Transglutaminase “Activa (registered trademark) TG” was added to the obtained solution so that the concentration thereof was 1.22 U/g, 3.66 U/g or 6.10 U/g, and each was stirred in a homomixer for 30 min at 40° C. and 5,000 rpm. The obtained solutions were heated in a microwave oven (900 W, 30 sec), and then heated in an oil bath at 75° C. or higher for 5 min to inactivate the transglutaminase. The solutions were then defoamed in a centrifuge at 2,000 rpm for 10 min.
Photographs of the resulting mixtures are shown in
Following the method described in Preparation Example 2, wt % soy protein solution was obtained from soy protein “New 5 FUJIPRO SEH” (Fuji Oil Co., Ltd.) and distilled water. Transglutaminase “Activa (registered trademark) TG” was added to the obtained solution so that the concentration thereof was 1.22 U/g, 3.66 U/g or 6.10 U/g, and each was stirred in a homomixer for 30 min at 40° C. and 5,000 rpm. The obtained solutions were heated in a microwave oven (900 W, 30 sec), and then heated in an oil bath at 75° C. or higher for 5 min to inactivate the transglutaminase. The solutions were then defoamed in a centrifuge at 2,000 rpm for 10 min.
Photographs of the resulting mixtures are shown in
For each fluid gel obtained when transglutaminase was added in Example 1, the angular frequency dependence of complex modulus (G*) was measured under the following conditions, and then the coordination number (z) in the angular frequency range of 0.1 to 100 rad/sec was derived.
The coordination number (z) in the angular frequency range of 0.1 to 100 rad/sec was derived by plotting the angular frequency dependency data of the above-mentioned complex modulus (G*) (Pa) in the angular frequency range of 0.1 to 100 rad/sec on a graph with the complex modulus (Pa) on the vertical axis and the angular frequency (rad/sec) on the horizontal axis, drawing an approximation line by the least squares method, and calculating 1/a from the slope a of the approximation line.
The results thereof are shown in
The shear stress was measured under the following conditions for each fluid gel obtained in Example 2 and Example 3.
The results thereof are shown in
The viscosity coefficient was derived from the shear stress measured in Experimental Example 2 for each fluid gel obtained when transglutaminase “Activa (registered trademark) TG” was added to 1.22 U/g and 3.66 U/g in Example 2 (alkaline conditions) and Example 3 (neutral conditions).
In other words, the viscosity coefficient was calculated by analyzing the shear stress obtained in Experimental Example 2 and the shear rate (1/sec) set during measurement with the above-mentioned rheometer using the following Herschel-Bulkley equation using analysis software Universal Software US200 (Paar Physica).
In the formula, σ represents shear stress (Pa), k represents viscosity coefficient (Pasn), γ represents shear rate (1/sec), n represents H-B index (no unit), and σy represents yield stress (Pa).
The results thereof are shown in
The complex modulus (G*) of each fluid gel obtained when the transglutaminase “Activa (registered trademark) TG” was added to 1.22 U/g and 3.66 U/g in Example 2 was measured under the following conditions.
Then, the gel strength Af (Pas1/z) at an angular frequency of 1 rad/sec was derived by plotting the angular frequency dependency data of the above-mentioned complex modulus (G*) (Pa) in the angular frequency range of 0.1 to 100 rad/sec on a graph with the complex modulus (Pa) on the vertical axis and the angular frequency (rad/sec) on the horizontal axis, drawing an approximation line by the least squares method, and calculating 10b from the vertical intercept b of the approximation line at an angular frequency of 1 rad/sec.
The results thereof are shown in
Mayonnaise was prepared with the composition shown in Table 1.
The soybean 6% fluid gel used was a fluid gel obtained from a 6 wt % soy protein solution prepared in the same manner as in Example 1. Half mayonnaise corresponds to low-fat mayonnaise.
Dynamic viscoelasticity was measured for each mayonnaise obtained in Example 4, under the following conditions and using an ARES G-2 (manufactured by TA Instruments) as the measuring device. Specifically, about 2 ml of each sample was dropped directly under the jig, and after it reached the gap, the protruding sample was wiped off, and the measurement was performed.
G′ (storage modulus (index of elastic property)), G″(loss modulus (index of viscous property)), and Tan δ (loss tangent (G′/G″)) were measured at distortion rates of 0.3%, 1%, 5%, 10%, 20%, 50%, 100%, 200%, 400%, 500%, 800% and 1,000%, and the results were used to perform principal component analysis of the top parameters at each distortion rate to obtain a score plot.
The results thereof are shown in
A mug was filled with (1) milk fat with a low fat content (fat content 35%), (2) vegetable fat (fat content 41%), or (3) vegetable fat (fat content 41%) (about 100 ml), and the mug was immersed in a bowl of ice water. 7.5 g of sugar and, in the case of (3), 2% (2 g) of fluid gel obtained from a 5 wt % soy protein solution prepared in the same manner as in Example 1 were added. The mixture was whipped using a Bamix until the corners stood up, and then leveled with and placed in a plastic cup to prepare whipped cream, which was then weighed.
The results thereof are shown in Table 2 and
As shown in Table 2 and
Dynamic viscoelasticity was measured for each whipped cream obtained in Example 5, under the following conditions and using an ARES G-2 (manufactured by TA Instruments) as the measuring device. Specifically, about 2 ml of each sample was dropped directly under the jig, and after it reached the gap, the protruding sample was wiped off, the measurement was performed, and G′ (storage modulus (index of elastic property)) was calculated.
The results thereof are shown in
7 g of a fluid gel sample or a comparison sample and 3.5 g of canola oil were added to a 15 ml Eppendorf tube, and emulsified by stirring at 5,000 rpm for 1 min with a homogenizer. Thereafter, the appearance was measured 1 hr later. As fluid gel samples, fluid gels obtained from 5 wt %, 6 wt %, and 7 wt % soy protein solutions (samples No. 1, No. 2, and No. 3, respectively) prepared in the same manner as in Example 1 were used, and as comparison samples, samples No. 4, No. 5, and No. 6 with compositions shown in Table 3 were used (only sample No. 4 was over 7 g).
A photograph of the appearance after 1 hr is shown in
Mayonnaise was prepared with the composition shown in Table 4.
The fluid gel used was “soybean 6% fluid gel 300 rpm”, which was obtained by adding transglutaminase “Activa (registered trademark) TG” to the soy protein solution to a concentration of 3.66 U/g and stirring at 300 rpm instead of 5,000 rpm in Example 2, or “soybean 6% fluid gel 5,000 rpm”, which was obtained by adding transglutaminase “Activa (registered trademark) TG” to the soy protein solution to a concentration of 3.66 U/g in Example 2.
Each mayonnaise prepared in Example 6 was frozen at −20° C. overnight and then left at room temperature for 1 hr, and the emulsified state was observed.
The results thereof are shown in
Cafe au lait was prepared with the composition shown in Table 5.
Note that ICP refers to instant creaming powder that is added to luxury beverages such as coffee drinks as a substitute for cream, and Marim (registered trademark) (Ajinomoto AGF Co., Ltd.) was used. For the reduced-fat ICP, Marim (registered trademark) (Ajinomoto AGF Co., Ltd.) with 20% less fat was used.
The premix was prepared from instant coffee powder, sodium bicarbonate, and granulated sugar according to the method described in JP-A-2005-144600.
The fluid gel used was the one obtained in Example 2 by adding transglutaminase “Activa (registered trademark) TG” to the soy protein solution to 3.66 U/g.
The mid-to late-stage thickness of each cafe au lait prepared in Example 7 was evaluated by four panelists skilled in evaluation through discussion, using the mid-to late-stage thickness of cafe au lait measured using ICP as the standard and according to the following evaluation scale. The “mid-to late-stage thickness” refers mainly to the thickness derived from fats and oils and milk, and indicates a sensation of intensification of the flavor without changing the balance.
The results thereof are shown in Table 5. As shown in Table 5, in the cafe au lait using reduced-fat ICP, the thickness in the mid-to late-stage was much less than that using ICP, and it was watery, thin, less thick and rich, and less milky; however, in the cafe au lait using reduced-fat ICP and fluid gel, the thickness in the mid-to late-stage was equivalent to that using ICP.
Milk protein “Sodium Casainate 180” (Fonterra Japan Co., Ltd.) was added to water at 60° C. so that the protein concentration was 8 wt %, and mixed using a homogenizer at 10,000 rpm for 1 min, and then at 5,000 rpm for 59 min to obtain 500 mL of a protein solution. After the temperature of the obtained solution was lowered to 40° C., transglutaminase “Activa (registered trademark) TG” was added to 300 mL of the solution so that the concentration thereof was 3.66 U/g, and the mixture was stirred in a homomixer at 40° C. and 1,0000 rpm for 30 min. The obtained solution was heated in an oil bath at 75° C. or higher for 5 min or more to inactivate the transglutaminase. The mixture was then defoamed in a centrifuge at 2,000 rpm for 10 min to obtain a fluid gel.
14 g of the fluid gel prepared in Example 8, 126 g of water, and 60 g of canola oil were mixed for 5 min at 5,000 rpm using a homogenizer. As a control, the same procedure was performed using a protein solution obtained according to the method described in Example 8 instead of the fluid gel prepared in Example 8.
The appearance of each solution obtained was observed immediately after mixing, after 60 min, and after freezing overnight at −20° C. and thawing.
The results thereof are shown in
The particle sizes of each fluid gel prepared using a 6 wt % soy protein solution instead of the 5 wt % soy protein solution and stirring at 10,000 rpm instead of 5,000 rpm in Example 2, and the protein solution prepared using a 6 wt % soy protein solution instead of the 5 wt % soy protein solution and stirring at 10,000 rpm instead of 5,000 rpm without adding transglutaminase “Activa (registered trademark) TG” in Example 2 were measured using a laser diffraction⋅scattering particle size distribution measuring device LA-960 (Horiba, Ltd.).
The results thereof (D50 particle size) are shown in Table 6.
In addition, the particle size was measured using a laser diffraction⋅scattering particle size distribution measuring device LA-960 (HORIBA, Ltd.) for a fluid gel prepared using a 6 wt % soy protein solution instead of the 5 wt % soy protein solution in Example 2, and a fluid gel prepared using a 6 wt % soy protein solution instead of the 5 wt % soy protein solution and stirring at 300 rpm instead of 5,000 rpm in Example 2.
As a result, the D50 particle size was approximately 200 μm when stirred at 5,000 rpm, and the D50 particle size was about 1,000 μm when stirred at 300 rpm.
The particle sizes of the fluid gel prepared in Example 8, the fluid gel prepared by adding transglutaminase “Activa (registered trademark) TG” to 1.22 U/g, 2.44 U/g, or 6.10 U/g instead of 3.66 U/g in Example 8, the fluid gel prepared by adding transglutaminase “Activa (registered trademark) TG” to 6.10 U/g instead of 3.66 U/g and then not stirring with a homomixer in Example 8, and the protein solution obtained according to the method described in Example 8 were measured using a laser diffraction⋅scattering particle size distribution measuring device LA-960 (HORIBA, LTD.).
The results thereof (D50 particle size) are shown in Table 7.
The present invention provides a fluid gel which can impart good properties such as stickiness-free viscosity and a rich taste, good melt in mouth, foaming property, and the like to semi-solid foods, and which itself is superior in emulsifying property, and a production method thereof, emulsifiers and semi-solid foods containing the fluid gel, and the like. In addition, according to the production method, a fluid gel can be obtained without heating at a high temperature. Furthermore, by using the fluid gel, for example, low-calorie mayonnaise or whipped cream that has property closer to full-fat mayonnaise or whipped cream that uses high-fat milk fat can be obtained, even when low-fat raw materials are used. Therefore, the present invention is useful in the food industry.
Where a numerical limit or range is stated herein, the endpoints are included. Also, all values and subranges within a numerical limit or range are specifically included as if explicitly written out.
As used herein the words “a” and “an” and the like carry the meaning of “one or more.”
Obviously, numerous modifications and variations of the present invention are possible in light of the above teachings. It is therefore to be understood that, within the scope of the appended claims, the invention may be practiced otherwise than as specifically described herein.
All patents and other references mentioned above are incorporated in full herein by this reference, the same as if set forth at length.
| Number | Date | Country | Kind |
|---|---|---|---|
| 2022-032720 | Mar 2022 | JP | national |
This application is a continuation of International Patent Application No. PCT/JP2023/008032, filed on Mar. 3, 2023, and claims priority to Japanese Patent Application No. 2022-032720, filed on Mar. 3, 2022, both of which are incorporated herein by reference in their entireties.
| Number | Date | Country | |
|---|---|---|---|
| Parent | PCT/JP2023/008032 | Mar 2023 | WO |
| Child | 18821019 | US |
