Gel composition and production method for gel composition

Abstract

Provided is a novel gel composition.　The present invention provides a gel composition that contains an active enzyme and a gelling component that contains at least one gelling agent. The present invention also provides a production method for the gel composition that includes an enzyme addition step for adding an enzyme to a gelling component that contains at least one gelling agent, the enzyme being added to the gelling component under temperature conditions that are below the deactivation temperature of the enzyme.

Description

Gel composition and method for producing gel composition

[0001] The present technology relates to a gel composition and a method for producing a gel composition.

[0002] Enzyme-containing preparations are sold in the form of medicines and supplements. Enzyme preparations have generally been provided in the form of tablets, capsules, granules, liquids, etc. However, considering that they are widely consumed by people of all ages and genders, there is a demand for preparations in various forms.

[0003] For example, Patent Document 1 discloses an oral composition with excellent fluidity, which is formulated with microcapsules encapsulating water-soluble functional ingredients such as digestive enzymes, with good dispersibility and reduced elution of the encapsulated substances.

[0004] Furthermore, for example, gummy and jelly forms are popular and in high demand among a wide range of age groups, from small children to elderly people with swallowing difficulties.

[0005] For example, Patent Document 2 discloses a gummy candy that contains 0.5 to 7% by weight of date juice enzymatically decomposed with amylase, thereby masking the unpleasant odor and unpleasant taste derived from collagen.

[0006] JP 2011-79787 A JP 2011-177036 A

[0007] As mentioned above, gummy and jelly-like gel forms are in high demand, but there is a concern that enzyme activity may decrease during gelation. Therefore, even if enzymes are used in the gummy candy manufacturing process as in Patent Document 2, the enzymes are inactivated during the manufacturing process, and gel compositions in which activity remains sufficient have yet to be developed.

[0008] Therefore, a main object of the present technology is to provide a novel gel composition.

[0009] The present technology first provides a gel composition containing an active enzyme and a gelling component containing one or more gelling agents. The enzyme used in the gel composition of the present technology may have a deactivation temperature higher than the gelling temperature of the gelling component. Furthermore, the enzyme used in the gel composition of the present technology may be stable at the gelling pH of the gelling component. A bioavailable enzyme can be used as the enzyme used in the gel composition of the present technology. The bioavailable enzyme may be an enzyme that aids digestion. The enzyme that aids digestion may be amylase.

[0010] The present technology next provides a method for producing a gel composition, which includes an enzyme addition step of adding an enzyme to a gelling component containing one or more gelling agents, wherein the enzyme is added to the gelling component at a temperature below the deactivation temperature of the enzyme. The method for producing a gel composition according to the present technology may also include a gelation step of gelling the gelling component that has been subjected to the enzyme addition step, and the enzyme may be stable in the gelation step.

[0011] Preferred embodiments for carrying out the present technology will be described below. Note that the embodiments described below are examples of typical embodiments of the present technology, and the scope of the present technology should not be construed as being narrow.

[0012] 1. Gel Composition The gel composition according to the present technology contains an active enzyme and a gelling component (hereinafter also referred to as "gelling component") containing one or more gelling agents. The gelling component may contain a gelling aid, other components, etc., as needed. Each component will be described in detail below.

[0013] (1) Enzymes The enzymes contained in the gel compositions according to the present technology are characterized by their activity. That is, the gel compositions are characterized by containing enzymes whose enzymatic activity remains effective in the final product, rather than enzymes added solely for the enzymatic treatment of raw materials in the production process of the gel compositions. Note that even enzymes added for the purpose of enzymatic treatment of raw materials in the production process of the gel compositions can be used in the gel compositions according to the present technology as long as they are contained in the final product in a state where they have enzymatic activity.

[0014] In order to allow the enzyme to remain in the final product in a state where its enzymatic activity is effective, it is preferable that the enzyme be stable in the gelation step in the production method described below. Specifically, it is preferable that the enzyme be stable at the gelation temperature and gelation pH.

[0015] Since general gel compositions are liquid at high temperatures and often become gelatinous when the temperature drops below the gelation temperature, it is preferable that the deactivation temperature of the enzyme used be higher than the gelation temperature of the gelling component (a component containing a gelling agent, as described below, and optionally a gelling aid, a solvent, and other components). More specifically, the deactivation temperature of the enzyme used is preferably 10°C or more higher than the gelation temperature of the gelling component, more preferably 15°C or more higher, even more preferably 20°C or more higher, even more preferably 25°C or more higher, and particularly preferably 30°C or more higher. Using an enzyme with a deactivation temperature within this range makes it easier to adjust the temperature when dissolving and / or dispersing each component in the liquid gelling component before gelation.

[0016] In the present technology, the "enzyme inactivation temperature" refers to the temperature at which the residual activity of an enzyme becomes 10% or less when the enzyme is dissolved in water and allowed to stand at each temperature for 30 minutes.

[0017] Furthermore, it is preferable that the deactivation pH of the enzyme used is not near the gelation pH of the gelling component. More specifically, the deactivation pH of the enzyme used is preferably outside the range of ±0.1, ±0.3, ±0.5, ±1.0, or ±2.0 relative to the gelation pH of the gelling component, more preferably outside the range of ±2.5, even more preferably outside the range of ±3.0, even more preferably outside the range of ±3.5, and particularly preferably outside the range of ±4.0. Using an enzyme with a deactivation pH within this range facilitates pH adjustment when dissolving and / or dispersing each component in the liquid gelling component before gelation. In this technology, "outside the range of ±○○" means "outside the range of -○○ to +○○."

[0018] In the present technology, the "enzyme inactivation pH" refers to the pH at which the residual activity of an enzyme becomes 10% or less when the enzyme is dissolved in a buffer solution adjusted to various pH levels and left at 30°C for 30 minutes.

[0019] The enzymes that can be used in the gel composition of the present technology can be freely selected from one or more types as long as they do not impair the action and effect of the present technology. In particular, the enzymes used in the present technology are preferably enzymes that are bioavailable. Examples of bioavailable enzymes include enzymes that aid digestion and enzymes that aid metabolism. Among these, the present technology preferably uses enzymes that aid digestion. Examples of enzymes that aid digestion include carbohydrate-degrading enzymes, protease enzymes, and lipid-degrading enzymes.

[0020] Examples of carbohydrate-degrading enzymes include α-amylase, β-amylase, glucoamylase, pullulanase, isoamylase, maltotriohydrolase, cyclodextrin glucanotransferase, transglucosidase, 4-α-glucanotransferase, dextranase, maltase, sucrase, lactase, trehalase, cellulase, hemicellulase, pectinase, mannanase, glucosidase, hyaluronidase, and lysozyme. Examples of proteolytic enzymes include pepsin, trypsin, peptidase, and protease. Examples of lipid-degrading enzymes include lipase. Of these, α-amylase and lactase will be described in more detail.

[0021] [α-Amylase] α-Amylase is an enzyme that acts on starch and mainly hydrolyzes α-1,4-glucosidic bonds. α-Amylase that can be used in the present technology has α-amylase activity and may also have other functions as long as they do not impair the functions and effects of the present technology.

[0022] The origin of the α-amylase that can be used in the present technology is not particularly limited as long as it does not impair the action and effect of the present technology. For example, examples of filamentous fungi include Aspergillus aureus, Aspergillus foetidus, Aspergillus niger, and Aspergillus oryzae; examples of actinomycetes include Saccharomonospora viridis, Streptomyces avermitilis, Streptomyces griseus, Streptomyces thermoviolaceus, Streptomyces violaceoruber, and Thermomonospora viridis; examples of bacteria include Alcaligenes latus, Streptomyces erythrocytes ... latus), Arthrobacter spp., Bacillus amyloliquefaciens, Bacillus circulans, Bacillus licheniformis, Bacillus stearothermophilus, Bacillus subtilis, Cellulosimicrobium cellulans, Microbacterium imperiale, Paenibacillus alginolyticus, and Sulfolobus solfataricus.Preferably, α-amylase derived from the genus Bacillus or α-amylase derived from the genus Aspergillus is used, and more preferably, α-amylase derived from Bacillus amyloliquefaciens or α-amylase derived from Bacillus licheniformis is used.

[0023] The content of α-amylase in the gel composition according to the present technology is not particularly limited as long as it does not impair the action and effect of the present technology. The lower limit of the α-amylase content can be set to, for example, 0.004 U or more, preferably 0.02 U or more, more preferably 0.04 U or more, 0.01 U or more, 1 U or more, 5 U or more, and even more preferably 9 U or more, 10 U or more, 16 U or more, 20 U or more, 30 U or more, 40 U or more, 50 U or more, 60 U or more, 70 U or more, or 80 U or more per 1 g of the gel composition. The upper limit of the content of α-amylase per 1 g of the gel composition is, for example, 90,000 U or less, 80,000 U or less, 70,000 U or less, 60,000 U or less, 50,000 U or less, 40,000 U or less, 30,000 U or less, 20,000 U or less, 18,000 U or less, 9,000 U or less, 8,000 U or less, 7,000 U or less, 6,000 U or less, 5,000 U or less, 4,000 U or less, 3 It can be set to 600U or less, 2000U or less, 1800U or less, 1000U or less, 500U or less, 400U or less, 300U or less, 200U or less, 180U or less, 150U or less, 135U or less, 120U or less, 99U or less, 80U or less, 70U or less, 60U or less, 50U or less, 40U or less, 36U or less, 27U or less, 20U or less, 19U or less, or 18U or less.

[0024] In this technology, α-amylase activity is defined as one unit (1 U) of enzyme amount that reduces the color of potato starch caused by iodine by 10% in one minute when treated with 1% potato starch as a substrate at pH 5.0 and 37° C. Details of the method for measuring α-amylase activity in this technology will be described in the α-amylase activity measurement method described in the Examples below.

[0025] [Lactase] Lactase is an enzyme that hydrolyzes lactose into galactose and glucose. The lactase that can be used in the present technology has lactase activity and may also have other functions as long as they do not impair the function or effect of the present technology.

[0026] The origin of lactase that can be used in the present technology is not particularly limited as long as it does not impair the action and effect of the present technology. For example, fungal lactases include lactases from the genus Aspergillus such as Aspergillus oryzae, Aspergillus flavus, Aspergillus candidus, and Aspergillus niger, and lactases from the genus Penicillium such as Penicillium multicolor. Yeast lactases include lactases from the genus Cryptococcus such as Cryptococcus terrestris and Cryptococcus laurentii, and lactases from Sporobolomyces singularis. Examples of lactases derived from bacteria include lactases derived from the genus Sporobolomyces such as Kluyveromyces singularis, lactases derived from the genus Kluyveromyces such as Kluyveromyces lactis, lactases derived from Saccharomyces fragilis, Torula cremoris, and Torula utilis, and lactases derived from Escherichia coli, Bacillus subtilis, Bacillus stearothermophilus, Bacillus circulans, Bacillus licheniformis, Bacillus aminoliquefaciens, and the like. Lactase derived from Bacillus bacteria such as Lactobacillus amyloliquefaciens, lactase derived from Lactococcus, and lactase derived from Lactobacillus bulgaricusExamples of lactase include lactase derived from the genus Lactobacillus such as Lactobacillus bulgaricus, and lactase derived from lactic acid bacteria such as Streptococcus and Bifidobacterium.

[0027] The lactase content in the gel composition according to the present technology is not particularly limited as long as it does not impair the action and effect of the present technology. The lower limit of the lactase content can be set to, for example, 0.05 U or more, preferably 0.25 U or more, more preferably 0.5 U or more, 1 U or more, 5 U or more, 10 U or more, 20 U or more, and even more preferably 30 U or more, 40 U or more, or 50 U or more per 1 g of the gel composition. The upper limit of the lactase content can be set to, for example, 60,000 U or less, 50,000 U or less, 40,000 U or less, 30,000 U or less, 20,000 U or less, 15,000 U or less, 10,000 U or less, 5,000 U or less, 4,000 U or less, 3,000 U or less, 2,000 U or less, 1,000 U or less, 500 U or less, 250 U or less, 200 U or less, 150 U or less, 100 U or less, 90 U or less, 80 U or less, or 70 U or less per 1 g of the gel composition.

[0028] In this technology, lactase activity is defined as the amount of enzyme that liberates 1 μmol of o-nitrophenol per minute when reacted for 15 minutes at a reaction temperature of 37°C and a reaction pH of 4.5 using o-nitrophenyl-β-galactopyranoside (ONPG) as a substrate, and one unit (1 U) of the enzyme is used. Details of the method for measuring lactase activity in this technology will be described in the lactase activity measurement method described in the Examples below.

[0029] For each of the enzymes described above, the present technology is not limited to natural (wild-type) enzymes, and recombinant enzymes can also be used. Commercially available enzymes or enzyme preparations can also be used. An example of a commercially available α-amylase or α-amylase preparation is the α-amylase derived from Bacillus amyloliquefaciens manufactured by Amano Enzyme Inc.

[0030] The enzymes used in the present technology can be prepared from the culture medium of the microorganism from which the enzymes are derived. Specific preparation methods include recovering the enzyme from the culture medium or cells of the microorganism. For example, when using enzyme-secreting microorganisms, the cells can be recovered from the culture medium by filtration, centrifugation, or the like, as necessary, and then the enzyme can be separated and / or purified. When using non-enzyme-secreting microorganisms, the cells can be recovered from the culture medium by crushing them by pressure treatment, ultrasonication, or the like, to extract the enzyme, and then the enzyme can be separated and / or purified. Enzyme separation and / or purification methods can be any known protein separation and / or purification method, without particular limitation. Examples include centrifugation, UF concentration, salting out, and various chromatography methods using ion exchange resins. The separated and / or purified enzymes can be powdered by drying methods such as lyophilization and vacuum drying, or by using appropriate excipients and / or drying aids in the drying methods. The separated and / or purified enzymes can also be liquefied by adding appropriate additives and sterilizing by filtration.

[0031] (2) Gelling Agent One or more gelling agents can be freely selected for use in the gel composition of the present technology, as long as they do not impair the action or effect of the present technology. Examples of gelling agents include polysaccharides such as pectin, carrageenan (e.g., kappa carrageenan, iota carrageenan, and lambda carrageenan), locust bean gum, guar gum, gum arabic, tamarind gum, tara gum, konjac mannan, gellan gum, xanthan gum, tragacanth gum, modified starch, curdlan, arabinoxylan, hemicellulose, and cellulose; gelatin; agar; and sodium alginate. Among these, pectin, carrageenan (kappa carrageenan), and locust bean gum are preferably used in the present technology.

[0032] When a polysaccharide is used as a gelling agent, the origin of the polysaccharide is not particularly limited as long as it does not impair the action and effect of the present technology. For example, polysaccharides derived from citrus peels (e.g., lemon, orange, etc.), apples, beets, etc. can be used.

[0033] When gelatin is used as a gelling agent, the method of producing the gelatin is not particularly limited as long as it does not impair the functions and effects of the present technology. For example, gelatin may be extracted and purified from collagen-containing substances (animal skin, bones, connective tissue, etc.). The organism from which the collagen-containing substance is derived is also not particularly limited as long as it does not impair the functions and effects of the present technology. Examples include gelatin derived from the skin and bones of animals such as cows, pigs, and chickens, as well as gelatin derived from aquatic organisms (freshwater and saltwater). Furthermore, gelatin may be subjected to treatments such as acid treatment and alkali treatment. In the present technology, one type of gelatin having the same origin and production method may be used, or two or more types of gelatin having different origins and production methods may be mixed and used.

[0034] The content of the gelling agent in the gel composition according to the present technology is not particularly limited as long as it does not impair the action and effect of the present technology. The lower limit of the gelling agent content can be set to, for example, 0.1 w / v% or more, preferably 0.2 w / v% or more, 0.3 w / v% or more, more preferably 0.4 w / v% or more, 0.5 w / v% or more, even more preferably 0.6 w / v% or more, or 0.7 w / v% or more. The upper limit of the gelling agent content can be set to, for example, 10 w / v% or less, preferably 9 w / v% or less, more preferably 8 w / v% or less, 7 w / v% or less, 6 w / v% or less, even more preferably 5 w / v% or less, 4 w / v% or less, 3 w / v% or less, 2 w / v% or less, or 1 w / v% or less.

[0035] (3) Gelling Aid In the present technology, a gelling aid can be used. As the gelling aid that can be used in the present technology, one or more types can be freely selected and used depending on the type and amount of the gelling agent and solvent, and the type and amount of other components to be contained in the gelling component containing the gelling agent, as long as they can assist the gelation of the liquid gelling component containing the gelling agent.

[0036] Examples of gelling aids include pH adjusters, preferably pH adjusters for foods and beverages, specifically organic acids such as citric acid, malic acid, tartaric acid, acetic acid, fumaric acid, and ascorbic acid; and salts such as calcium chloride.

[0037] The content of the gelling aid in the gel composition according to the present technology is not particularly limited as long as it does not impair the function and effect of the present technology. The lower limit of the content of the gelling aid can be set to, for example, 0.1 w / v% or more, preferably 0.2 w / v% or more, 0.3 w / v% or more, more preferably 0.4 w / v% or more, 0.5 w / v% or more, even more preferably 0.6 w / v% or more, or 0.7 w / v% or more. The upper limit of the content of the gelling aid can be set to, for example, 10 w / v% or less, preferably 9 w / v% or less, more preferably 8 w / v% or less, 7 w / v% or less, 6 w / v% or less, even more preferably 5 w / v% or less, 4 w / v% or less, 3 w / v% or less, or 2 w / v% or less.

[0038] (4) Solvent The solvent used in the gel composition according to the present technology can be one or a combination of two or more solvents that can be used in general gel compositions, as long as the action and effect of the present technology are not impaired. Examples of solvents that can be used in the present technology include water and pH buffer solutions. Fruit juices and vegetable juices, which are exemplified as other components described below, can also be used as solvents.

[0039] (5) Other Components The gel composition according to the present technology can contain one or more materials or additives commonly used in the production of gel compositions, in any combination. For example, fruit juice, dried fruit, vegetable juice, dried vegetables, acidulants, emulsifiers, flavorings, colorings, sweeteners, etc. may be added as appropriate. In addition, inactive enzymes (e.g., enzymes used in the production process) may also be added as long as they do not impair the action or effect of the present technology.

[0040] Examples of fruits that can be used in fruit juices and dried fruits include apples, grapes, strawberries, kiwis, peaches, mandarins, mangoes, and mixtures thereof. Examples of vegetables that can be used in vegetable juices and dried vegetables include carrots, spinach, celery, bell peppers, kale, cabbage, watercress, and mixtures thereof.

[0041] (6) Final Form of Gel Composition The final form of the gel composition according to the present technology is not particularly limited as long as it does not impair the action or effect of the present technology, and the gel composition may be used as a final product in its gel form, or may be hardened to form a final form. Specific examples include candy (soft and hard), gummy candy, chewing gum, caramel, jelly, jam, mousse, pudding, yogurt, tablets, and the like.

[0042] 3. Manufacturing Method of Gel Composition The manufacturing method of the gel composition according to the present technology is a method including an enzyme addition step and a gelation step. Furthermore, if necessary, general manufacturing steps of gel compositions, such as a liquid gelling component preparation step and a recovery step, can be carried out before, after, or simultaneously with each step, as long as the effects of the present technology are not impaired. Each step will be described in detail below.

[0043] (1) Liquid Gelling Component Preparation Step In the step of preparing the liquid gelling component, the above-mentioned gelling agent, and if necessary, a gelling aid and other components, are dissolved and / or dispersed in any solvent to prepare the liquid gelling component. When a gelling aid and other components are used, they can also be added in the enzyme addition step and / or gelling step described below, as long as the action and effect of the present technology are not impaired. In the liquid gelling component preparation step, stirring, heating, etc. can be performed as appropriate depending on the type and amount of the gelling agent, solvent, other components, etc. used, as long as the action and effect of the present technology are not impaired.

[0044] In the liquid gelling component preparation step, it is also possible to subject the raw material to an enzyme treatment depending on the type of solvent and other components used, etc. After the enzyme treatment, an enzyme inactivation step can be carried out as appropriate.

[0045] The gelling agent, gelling aid, solvent, and other components used in the liquid gelling component preparation step are the same as those used in the gel composition described above, and therefore, a description thereof will be omitted here.

[0046] (2) Enzyme Addition Step The enzyme addition step is a step of adding an enzyme to a gelling component. The enzyme addition step is characterized in that the enzyme is added to the gelling component at a temperature below the inactivation temperature of the enzyme. When the liquid gelling component preparation step described above is performed at a temperature below the inactivation temperature of the enzyme, the liquid gelling component preparation step and the enzyme addition step can be performed simultaneously or in any order.

[0047] As described above, when the raw material is subjected to an enzymatic treatment in the liquid gelling component preparation step, the enzyme used in the enzymatic treatment can be allowed to remain active. In this case, the enzyme deactivation step after the enzymatic treatment is not carried out.

[0048] The specific temperature of the enzyme addition step is not particularly limited as long as the enzyme can be added under temperature conditions below the inactivation temperature of the enzyme. The enzyme addition step is preferably carried out at a temperature lower than the inactivation temperature of the enzyme used, for example, −5° C. or lower, preferably −10° C. or lower, more preferably −15° C. or lower, even more preferably −20° C. or lower, and still more preferably −25° C. or lower.

[0049] In the enzyme addition step, gelling aids and other ingredients can be added as needed, as long as they do not impair the action and effect of the present technology.

[0050] (3) Gelation step The gelation step is a step of gelling the gelling component that has been subjected to the enzyme addition step, i.e., the liquid gelling component to which the enzyme has been added. In the present technology, it is preferable that the enzyme is stable in the gelation step. By performing the gelation step under conditions in which the enzyme is stable, the enzyme can remain active in the gel composition.

[0051] The temperature conditions in the gelation step can be freely set as long as they are lower than the inactivation temperature of the enzyme used and do not impair the action and effect of the present technology. The temperature conditions in the gelation step are, for example, −10° C. or lower, preferably −15° C. or lower, more preferably −20° C. or lower, even more preferably −25° C. or lower, and still more preferably −30° C. or lower, −35° C. or lower, or −40° C. or lower relative to the inactivation temperature of the enzyme used.

[0052] The pH conditions in the gelation step can be freely set as long as they are not near the inactivation pH of the enzyme used and do not impair the action and effect of the present technology. The pH conditions in the gelation step are, for example, outside the range of ±0.1, ±0.3, ±0.5, ±1.0, ±1.5, preferably outside the range of ±2.0, more preferably outside the range of ±2.5, even more preferably outside the range of ±3.0, still more preferably outside the range of ±3.5, and particularly preferably outside the range of ±4.0, relative to the inactivation pH of the enzyme used.

[0053] In the gelation step, a gelling aid or other components can be added as needed, as long as the action and effect of the present technology are not impaired. Specific examples include a method in which a gelling aid is added depending on the progress of gelation while gelation is being carried out. In this case, the gelling aid can be added in multiple batches.

[0054] (4) Recovery Step The recovery step is a step of recovering the gel composition obtained through the gelling step. As a specific recovery method, one or a combination of two or more recovery methods generally used in the production of gel compositions can be used depending on the type of gel composition to be produced.

[0055] The present invention will be described in more detail below with reference to examples. Note that the examples described below are representative examples of the present invention and should not be construed as narrowing the scope of the present invention.

[0056] 1. Raw materials and enzymes used The gelling agents and enzymes used in the examples are shown in Table 1 below.

[0057]

[0058] 2. Enzyme Activity Measurement Method [Method for Measuring α-Amylase Activity] (1) Preparation of Substrate Solution: Approximately 1 g of potato starch was precisely weighed out and dried at 105°C for 2 hours, and its weight loss was measured. Potato starch equivalent to 1.000 g of the dried material was accurately weighed and placed in a beaker. 20 mL of water was added. While mixing well, 5 mL of sodium hydroxide solution (2 → 25) was gradually added to form a paste. Next, the solution was heated in a water bath with stirring for 3 minutes, after which 25 mL of water was added. After cooling, the solution was accurately neutralized with 2 mol / L hydrochloric acid test solution, 10 mL of 1 mol / L acetic acid / sodium acetate buffer (pH 5.0) was added, and water was added to make the solution exactly 100 mL.

[0059] (2) Absorbance Measurement: 10 mL of the substrate solution prepared above was accurately measured and heated at 37±0.5°C for 10 minutes. Then, 1 mL of the sample solution was added and immediately shaken. After leaving this solution at 37±0.5°C for exactly 10 minutes, 1 mL of this solution was accurately measured and added to 10 mL of 0.1 mol / L hydrochloric acid test solution, followed by immediate shaking. Next, 0.5 mL of this solution was accurately measured and 10 mL of 0.0002 mol / L iodine test solution (JP) was added. After shaking, the absorbance (AT) at a wavelength of 660 nm was measured using water as a control. The 0.0002 mol / L iodine test solution (JP) was prepared by adding 10 mL of water to 12.7 g of iodine and 25 g of potassium iodide, mixing thoroughly, adding water to make 100 mL, and then diluting 2500 times with water. Separately, 1 mL of water was added exactly in place of the sample solution, and the same procedure was repeated to measure the absorbance (AB).

[0060] (3) Method for calculating activity Under these conditions, the amount of enzyme that reduces the color of potato starch caused by iodine by 10% in 1 minute was defined as 1 unit, and activity was calculated using the following formula: α-amylase activity (U / g, U / mL) = {(AB - AT) / AB} x 1 / W, where AT is the absorbance of the sample solution, AB is the absorbance of the blank solution, and W is the amount of sample (g or mL) in 1 mL of sample solution.

[0061] [Method for Measuring Lactase Activity] 0.370 g of ONPG (o-nitrophenyl-beta-D-galactopyranoside) was weighed out and dissolved in 0.1 mol / L acetic acid / sodium hydroxide buffer (pH 4.5) to make a 100 mL solution. 2 mL of ONPG solution (pH 4.5) was weighed into a 50 mL Nessler tube and allowed to stand at 37±0.1°C for 10 minutes. 0.5 mL of sample solution was then added and immediately shaken. This solution was allowed to stand at 37±0.1°C for exactly 15 minutes, after which 2.5 mL of 10 g / dL sodium carbonate test solution was added and the reaction was stopped by shaking. 20 mL of water was then added and shaken. The absorbance (A1) of this solution was measured at a wavelength of 420 nm using water as a control. Separately, 0.5 mL of water was used as a blank instead of the sample solution, and the absorbance (A2) was measured in the same manner. Lactase activity was calculated using the following formula: The amount of enzyme that liberates o-nitrophenol at a rate of 1 μmol per 1 unit (1 U) was defined as 1 unit. β-Galactosidase activity (U / g, U / mL) = (A1-A2) x 25 / ε x 15 x 1 / w = (A1-A2) x 0.7246 x n A1: absorbance of sample A2: absorbance of blank 25: final volume (mL) ε: extinction coefficient (4.60) 15: reaction time (min) w: amount of enzyme (g, mL) per 0.5 mL of sample solution 1 / w = dilution factor (n) per 1 g or 1 mL of sample x 2

[0062] 3. Experimental Examples <Experimental Example 1> (1) Production of Gel Composition A gelling agent shown in Table 2 below was added to sodium acetate (pH 5.0), and the gelling agent was dissolved by heating at 50°C. The temperature was then lowered to 30°C, and an enzyme shown in Table 2 below was added. The temperature was then lowered to cause gelation. If gelation was not possible even after lowering the temperature to 20°C, a gelling aid shown in Table 2 below was added to cause gelation, thereby producing a gel composition.

[0063] (2) Confirmation of gelation The gel compositions prepared above were visually inspected for the presence or absence of gelation at 20° C. Completely gelled compositions were evaluated as ◯, liquid compositions as ×, and semi-gelled compositions (gelled + liquid) as Δ.

[0064] (3) Confirmation of Enzyme Activity To confirm the enzymatic activity of the produced gel composition, an iodine starch reaction was carried out. The gel composition was placed in a substrate prepared in accordance with the "Starch Refining Test Method, Japanese Pharmacopoeia," and reacted at 37°C for 1 hour. 2 mL of 0.0002 mol / L iodine test solution (Io.37) was then added to confirm the color. If starch remained, the color changed to blue-purple. If the color did not change to blue-purple, this indicates that the starch had been decomposed by α-amylase, i.e., α-amylase activity remained. The remaining enzymatic activity was evaluated as ○, and the absence of enzymatic activity was evaluated as ×.

[0065] (4) Results The results are shown in Table 2.

[0066] (5) Discussion In this experimental example, a gel composition containing an active enzyme was successfully produced. Specifically, it was demonstrated that a gel composition containing an active enzyme can be produced by using an enzyme whose deactivation temperature is higher than the gelation temperature of the gelling component. Furthermore, because the enzyme is stable at the gelation temperature and gelling pH of the gelling component, the enzymatic activity of the enzyme contained in the gel composition can be sufficiently maintained.

[0067] Experimental Example 2 (1) Production of Gel Composition A Glycine and kappa-type carrageenan were added to sodium acetate (pH 6.0) to a concentration of 1% and 0.5%, respectively, and the mixture was dissolved by heating at 60°C. The temperature was then lowered to 30°C, and the enzymes shown in Table 3 below were added. The temperature was then lowered to 20°C, and the mixture was allowed to gel.

[0068] (2) Production of Gel Composition B To sodium acetate (pH 6.0), glycine was added at 1%, kappa-type carrageenan at 0.5%, and locust bean gum at 0.21%, and the mixture was dissolved by heating at 60°C. The temperature was then lowered to 30°C, and the enzymes shown in Table 3 below were added. The temperature was then lowered to 20°C, and the mixture was allowed to gel.

[0069] (3) Measurement of Residual Activity The enzyme-containing gel compositions A and B produced above and the enzyme solutions shown in Table 3 below as Reference Examples 1 and 2 were stored at 4° C., 25° C., and 40° C. for one month for Enzyme 1 (α-amylase) and for three months for Enzyme 2 (lactase). The activity of each enzyme listed in Table 3 below was measured before storage and after 1 to 90 days of storage, and the residual activity was calculated assuming the activity before storage was 100%.

[0070] (4) Results The results are shown in Table 3.

[0071]

[0072] (5) Discussion As shown in Table 3, when α-amylase was used as the enzyme, the decrease in residual activity after storage was suppressed in gelling compositions A and B compared to non-gelling Reference Example 1. In particular, when stored at 40°C, the residual activity of Reference Example 1 fell to 0% after one day of storage, whereas the enzyme in gelling compositions A and B maintained sufficient activity.

[0073] When lactase was used as the enzyme, the enzyme in gelling compositions A and B maintained activity equivalent to that of Reference Example 2 which was not gelled.

Claims

1. A gel composition comprising an active enzyme and a gelling component comprising one or more gelling agents.

2. The gel composition according to claim 1, wherein the deactivation temperature of the enzyme is higher than the gelation temperature of the gelling component.

3. The gel composition according to claim 1, wherein the enzyme is stable at the gelling pH of the gelling component.

4. The gel composition according to claim 1, wherein the enzyme is a bioavailable enzyme.

5. The gel composition according to claim 4, wherein the enzyme is an enzyme that aids digestion.

6. The gel composition according to claim 5, wherein the enzyme is amylase.

7. A method for producing a gel composition, comprising an enzyme addition step of adding an enzyme to a gelling component containing one or more gelling agents, wherein in the enzyme addition step, the enzyme is added to the gelling component under temperature conditions below the inactivation temperature of the enzyme.

8. The method for producing a gel composition according to claim 7, further comprising a gelling step of gelling the gelling component that has undergone the enzyme addition step, wherein the enzyme is stable in the gelling step.

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