JP4709730B2 - Chewable tablet - Google Patents

Description

  The present invention relates to a chewable tablet. Specifically, the present invention relates to a chewable tablet of a type that contains a high amount of collagen peptide and licks or chews in the oral cavity.

  In recent years, as one of functional foods, gelatin obtained from collagen, collagen or a collagen peptide obtained by hydrolyzing gelatin has attracted attention. Gelatin and collagen peptides are not only a protein source but also expected to have an effect of suppressing or preventing skin and hair aging, bone and joint diseases, etc. Development of foods that can be ingested efficiently is desired. In light of these social demands, beverages, jelly foods, bars, etc. that have been eaten and eaten as traditional foods have recently been explored as functional foods, and various types of gelatin and collagen peptides have been added. Products are being developed and distributed.

However, with regard to conventional chewable tablets, even though gelatin is used as a binder, almost no attempt has been made to blend the gelatin in a high amount. In addition, there is an attempt to add a high amount of collagen peptide in order to give foods nutritional functionality, but when the amount of collagen peptide is increased, specifically, collagen is added to the total amount of the raw material powder mixture. When the peptide was added in an amount of 25% by weight or more, there were many teeth (sticking to the teeth), it was difficult to chew, the mouthfeel was sticky, and it was difficult to make a refreshing tablet.
By the way, in order to improve the texture, generally, the type of sugar (sugar, glucose, lactose, sorbitol, xylitol, palatinit, etc.), the type of binder used for granulation, such as gelatin and gum arabic, The shape of the grain is devised. However, when the collagen peptide is highly blended, the amount of saccharides described above is inevitably small, so it is difficult to improve the texture sufficiently by simply devising the type of saccharides. Moreover, since the influence of the physical properties of the collagen peptide on the texture is very large, it is difficult to sufficiently improve the texture even by means of granulation.

  Therefore, when trying to obtain a chewable tablet having a good texture with the conventional technique, it was not possible to highly blend the collagen peptide. And in such a chewable tablet, if you try to ingest the target amount of collagen peptide, you will also ingest many other ingredients such as sugars at the same time, It was very inefficient.

  Therefore, the problem to be solved by the present invention is to provide a chewable tablet having a good texture without having teeth even though the collagen peptide is highly blended.

  The present inventors have intensively studied to solve the above problems. As a result, among collagen peptides obtained by hydrolyzing collagen or gelatin obtained from the collagen, particularly when a collagen peptide having an average molecular weight of a certain level or less is used, it has been a problem in the past while highly blending the collagen peptide. It was found that adverse effects on food texture can be suppressed. In addition, the proportion of glycine in the N-terminal amino acid of the collagen peptide exceeds 65 mol%, and the content of glutamic acid units and aspartic acid units, particularly the content of aspartic acid units, as the amino acid units constituting the collagen peptide is low. Each composition that the ratio of saccharides contained in the raw material powder mixture is 15 to 75% by weight with respect to the total amount, and that the saccharides are cellulosic polysaccharides. The present inventors have also found that it is effective in suppressing toothing and improving texture. The present invention has been completed based on these ideas.

Hereinafter, in the present specification, in order to simplify the terms, the “unit” is referred to for the amino acid unit and the glutamic acid unit which is a specific example thereof.
That is, chewable tablets according to the present invention is a chewable tablet obtained by tabletting the raw material powder mixture containing 25 wt% or more based on the total amount of the collagen peptide, wherein the collagen peptide has an average molecular weight of its 4000 or less der is, the ratio of glycine in the N-terminal amino acid and wherein der Rukoto, more than 65 mol%.
The total amino acids constituting the front Symbol collagen peptide, the proportion of glutamic acid 4.0 mol% or less, the proportion of the aspartate is less than 4.0 mol%, is preferred.

It is preferable that the ratio of the saccharide contained in the raw material powder mixture is 15 to 75% by weight with respect to the total amount.
It is preferable that the saccharide is a cellulosic polysaccharide.

  According to the present invention, a collagen peptide having an average molecular weight of 4000 or less is used in an amount of 25% by weight or more based on the total amount. Chewable tablets can be obtained, and more efficient intake of highly nutritious collagen peptides becomes possible.

Hereinafter, the chewable tablet according to the present invention will be described in detail. However, the scope of the present invention is not limited to these descriptions, and modifications other than the following examples can be made as appropriate without departing from the spirit of the present invention. .
The chewable tablet according to the present invention contains a collagen peptide having an average molecular weight of 4000 or less.
Preferably, a collagen peptide in which the proportion of glycine in the N-terminal amino acid exceeds 65 mol% is blended. More preferably, it is more than 65 mol% and less than 99 mol%.

The amino acid sequence of collagen or gelatin, which is a collagen peptide raw material, has a repeating structure of Gly-XY, but glycine has hydrophobic and aliphatic properties, and electrostatic interaction with calcium components in hydroxyapatite. Almost no effect. Therefore, when the proportion of glycine in the N-terminal amino acid exceeds 65 mol%, the adsorption of the collagen peptide to hydroxyapatite can be further suppressed, and toothing can be further prevented or suppressed and the texture can be improved.
Here, the “ratio of glycine in the N-terminal amino acid” means the amino acid at the first residue counted from the N-terminal of each collagen peptide, and the percentage of glycine in the total detected N-terminal amino acid is expressed in mole percentage. It is shown by. Among the two ends of the collagen peptide, the ratio of glycine, especially in the “N-terminal amino acid”, is that the C-terminal amino acid always has a carboxyl group, and the carboxyl group electrostatically interacts with the calcium component in hydroxyapatite. This is because, because of the action, adsorption with hydroxyapatite can hardly be suppressed regardless of the type of the C-terminal amino acid.

However, when the proportion of glycine in the N-terminal amino acid is small, for example, even if it is less than 33 mol%, alanine, leucine, isoleucine, valine, phenylalanine, methionine, proline, and hydroxyproline exhibit hydrophobicity in the same manner as glycine. If the total of the amount and the proportion occupied by the amount exceeds 65 mol%, it is possible to prevent or suppress toothing and improve the texture.
Moreover, it is preferable that the ratio of glutamic acid is 4.0 mol% or less and the ratio of aspartic acid is 4.0 mol% or less with respect to all amino acids constituting the collagen peptide. More preferably, the ratio of glutamic acid is 2.5 mol% or less, and the ratio of aspartic acid is 2.0 mol% or less. By reducing the content of these glutamic acid and aspartic acid which have strong interaction with hydroxyapatite among amino acids, it is possible to further prevent or suppress toothing and improve the texture.

The collagen or gelatin used as the raw material for the collagen peptide is not particularly limited, and examples thereof include collagen or gelatin derived from mammals such as cattle and pigs, and collagen or gelatin derived from fish such as sharks and salmon. Collagen can be obtained from the bones, skin parts, fish bones, skins, scale parts, etc. of mammals, and if various known materials such as bones are subjected to conventionally known treatments such as degreasing / decalcification treatment, extraction treatment, etc. Good. Gelatin can be obtained from the collagen by a conventionally known method. Specifically, for example, it can be obtained by hot water extraction from collagen.
A collagen peptide can be obtained by hydrolyzing the collagen or gelatin. The hydrolysis method and its treatment conditions may be any conventionally known one, and are not particularly limited. Specifically, for example, hydrolysis can be performed by a method using an enzyme, a chemical treatment with an acid or an alkali, or the like.

  The enzyme is not particularly limited as long as it is an enzyme capable of cleaving a peptide bond of collagen or gelatin. Usually, an enzyme called a proteolytic enzyme or a protease is used. Specific examples include collagenase, thiol protease, serine protease, acidic protease, alkaline protease, metal protease and the like, and these can be used alone or in combination. Known examples of the thiol protease include plant-derived chymopapain, papain, promelain, ficin, animal-derived cathepsin, and calcium-dependent protease. Moreover, trypsin, cathepsin D, etc. are known as the serine protease, and pepsin, chymosin, etc. are known as the acidic protease. Among them, the proportion of glycine in the N-terminal amino acid exceeds 65 mol%, and the proportion of alanine, glycine, leucine, isoleucine, valine, methionine, proline, and hydroxyproline in the N-terminal amino acid exceeds 65 mol% in total. In order to obtain a collagen peptide, it is particularly preferable to use collagenase, thiol protease, metal protease, acidic protease, or alkaline protease.

Although it does not specifically limit as said acid, For example, hydrochloric acid, a sulfuric acid, nitric acid etc. are mentioned.
Although it does not specifically limit as said alkali, For example, sodium hydroxide, calcium hydroxide, etc. are mentioned.
Hydrolysis is performed so that the average molecular weight of the collagen peptide is 4000 or less. If it exceeds 4000, the problem of toothing cannot be sufficiently prevented. However, if it is less than 500, the hydrolysis is performed excessively, and many components hydrolyzed to amino acids (molecular weight of about 100) are contained, which may deteriorate the taste. Therefore, it is preferably 500 or more. More preferably, it is 1500-3000. The “average molecular weight” in the present invention is a value measured by the “Pagii method” described later in Examples.

In order to obtain a collagen peptide having an average molecular weight of 4000 or less, hydrolysis treatment conditions may be adjusted. Specifically, for example, when using an enzyme, 0.02 to 5 parts by weight with respect to 100 parts by weight of collagen or gelatin is used, and water is added at 30 to 70 ° C. for 0.5 to 24 hours. If the decomposition treatment is performed, a collagen peptide having an average molecular weight of 4000 or less can be obtained. In addition, when acid or alkali is used, a collagen peptide having an average molecular weight of 4000 or less can be obtained by using 0.5 to 5 parts by weight with respect to 100 parts by weight of collagen or gelatin and hydrolyzing at 40 to 80 ° C. for 5 to 10 hours. Obtainable.
When hydrolyzed by an enzyme, it is necessary to deactivate the enzyme. Although the enzyme can be inactivated by heating or the like, in this case, it is sufficient to perform the heat treatment at a minimum necessary temperature for inactivating the enzyme, specifically 70 to 90 ° C. If the temperature is excessively high, the flavor may be deteriorated.

When hydrolyzed with an acid or alkali, a treatment such as neutralizing the acid or alkali with a neutralizing agent or desalting with an ion exchange resin or the like is necessary.
At the stage of finishing the hydrolysis treatment, the collagen peptide is in a state of being dissolved or dispersed in the hydrolysis treatment solution. This solution can be subjected to various purification processes that are usually employed.
Although it does not specifically limit as said refinement | purification process, For example, color tone, flavor improvement, and impurity removal can be performed very simply by adding activated carbon. Also, impurities can be removed by performing a conventionally known solid-liquid separation process such as filtration or centrifugation.

In order to make the ratio of glutamic acid to 4.0 mol% or less and the ratio of aspartic acid to 4.0 mol% or less with respect to all amino acids constituting the collagen peptide, the collagen peptide is dissolved or dispersed as a purification treatment. It is preferable to obtain a mixture by bringing the hydrolysis treatment liquid into contact with synthetic hydroxyapatite to obtain a mixture, and remove the adsorbed fraction from the mixture to obtain a collagen peptide fraction consisting of a non-adsorbed fraction. .
In the case where the hydrolysis treatment solution is contacted and mixed with synthetic hydroxyapatite, the concentration of the collagen peptide is 0.1 to 1% by weight, preferably 0.3 to 0.6% by weight, although not particularly limited. It is preferable to contact and mix the hydrolysis treatment solution in a ratio of 5 to 50 times (weight basis) with respect to the synthetic hydroxyapatite.

A method for removing the adsorbed fraction after the contact / mixing to obtain a collagen peptide fraction comprising a non-adsorbed fraction is not particularly limited. For example, by filtering the mixture, hydroxyapatite as a solid content is obtained. At the same time, the adsorbed fraction can be removed, and the collagen peptide fraction comprising the non-adsorbed fraction obtained as a filtrate can be recovered.
In order to mix | blend a collagen peptide with a chewable tablet, it is preferable to set it as a powder form, Although it does not necessarily limit as a method for pulverizing, For example, spray drying etc. are employable. You may employ | adopt drying methods other than spray drying, such as a drum dryer.

In this invention, the said collagen peptide is contained 25weight% or more with respect to the whole quantity of a raw material powder mixture. Therefore, efficient intake of the collagen peptide is possible.
In the chewable tablet according to the present invention, in addition to the collagen peptide, known materials such as saccharides, dietary fiber, agar, sweetener, acidulant can be used as the material used for ordinary chewable tablets. Is not particularly limited, and may be arbitrarily determined according to the purpose.
Among the materials described above, in particular, by devising the type and content of saccharide, as shown below, the chewable tablet according to the present invention can be further improved in texture, which is preferable.

The saccharides can be classified into monosaccharides, oligosaccharides and polysaccharides, and these can be used alone or in combination.
Examples of the monosaccharide / oligosaccharide include sugar, fructose, glucose, lactose, maltose, syrup, trehalose, xylose, palatinose, mannitol, reduced maltose, reduced syrup, sorbitol, xylitol, palatinit, erythritol, dextrin (cyclic dextrin, Preferred examples include branched cyclic dextrins), oligosaccharides (isomalto-oligosaccharides, fructooligosaccharides, emulsified oligosaccharides, xylooligosaccharides, galactooligosaccharides, etc.). These monosaccharides and oligosaccharides have a good mouthfeel and can be added to chewable tablets to prevent teething.

Moreover, as said polysaccharide, a cellulose polysaccharide etc. are mentioned as a preferable thing, for example. Furthermore, examples of the cellulose-based polysaccharide include cellulose, carboxymethyl cellulose, crystalline cellulose, methyl cellulose, and hydroxymethyl cellulose. Since toothing is due to the high hygroscopicity of the collagen peptide, the use of the cellulose-based polysaccharide having low hygroscopicity prevents the toothing.
The saccharide is preferably contained in a proportion of 15 to 75% by weight with respect to the total amount of the raw material powder mixture. If it is 15% by weight or more, a sufficient texture improvement effect by using each saccharide is obtained, and in combination with the texture improvement effect by using the collagen peptide according to the present invention, both nutrition and texture are very good. An excellent chewable tablet can be obtained. However, if it exceeds 75% by weight, the collagen peptide cannot be contained in an amount of 25% by weight or more, so it becomes 75% by weight or less.

The chewable tablet according to the present invention is produced by tableting a raw material powder mixture comprising the collagen peptide and other optional components. The tableting may be performed in the form of the raw material powder, or may be performed after part or all of the raw material is once granulated. The tableting machine used for tableting is not particularly limited, and for example, a rotary tableting machine, a single tableting machine or the like can be used.
The diameter of the chewable tablet obtained by tableting can be, for example, 5 to 20 mm.

Hereinafter, the present invention will be described more specifically by way of examples. However, the scope of the present invention is not limited to these examples.
A method for measuring the average molecular weight of the collagen peptide and an amino acid analysis method for the collagen peptide are shown below.
<Measurement method of average molecular weight>
The average molecular weight of the collagen peptide was measured by the Paguii method. Here, the “Pagii method” is a method for estimating a molecular weight distribution by obtaining a chromatogram of a sample solution by gel filtration using high-performance liquid chromatography. Specifically, it measured by the following method.

A sample (0.2 g) was placed in a 100 ml volumetric flask, an eluent composed of an equal amount of a mixture of 0.1 M potassium dihydrogen phosphate and 0.1 M disodium hydrogen phosphate was added, and the mixture was expanded for 1 hour. The solution was heated for 60 minutes to dissolve, cooled to room temperature, the eluent was diluted exactly 10 times, and the resulting solution was used as a test solution.
The chromatogram of the test solution was determined by the following gel filtration method.
Column: A column equipped with two Shodex Asahipak GS 620 7G in series was used.
Flow rate: 1.0 ml / min Column temperature: 50 ° C
Measurement wavelength: 230 nm
Under the above conditions, the retention time was taken on the horizontal axis, the corresponding absorbance at 230 nm was made on the vertical axis, a molecular weight distribution curve of the sample was prepared, and the average molecular weight was calculated.

<Analytical method of N-terminal amino acid of collagen peptide>
The proportion of glycine in the N-terminal amino acid of the collagen peptide was analyzed using a protein sequencer (manufactured by Applied Biosystems), which is an amino acid analyzer that automated the Edman method.
<Analysis method of all amino acids constituting collagen peptide>
Analysis was performed according to the following procedure.
(Preparation of test solution for amino acid analysis)
The solution containing the target collagen peptide was diluted with hydrochloric acid so that the concentration of the collagen peptide was 0.1% by weight, placed in a 15 ml test tube with a screw cap, and replaced with nitrogen gas, and the temperature was 105 ° C. In an oven for 24 hours to decompose. The decomposed sample was diluted 100 times with 1/1000 N hydrochloric acid, and this was used as a test solution for amino acid analysis.

(Amino acid analysis)
After the amino acid contained in the test solution for amino acid analysis was reacted with o-phthalaldehyde, it was fractionated with TSKgel Aminopack, and various amino acids were quantified with a fluorescence detector.
[Production Example 1 of Collagen Peptide]
1 kg of acid-treated pork skin gelatin (Nitta Gelatin Co., Ltd.) was dissolved in 2.0 kg of 75 ° C. warm water. To the gelatin solution, 0.6 g of bromelain F (manufactured by Amano Enzyme) as a proteolytic enzyme was added, and the temperature was adjusted to 50 ° C. and pH 7.5 so as to satisfy the optimum hydrolysis conditions of the enzyme. The enzyme treatment was performed for 2 hours until the average molecular weight reached 10,000 to obtain a collagen peptide, and then the enzyme was inactivated by heating to 90 ° C.

After deactivating the enzyme, 20 g of finely powdered activated carbon was added for the purpose of improving color tone and flavor and removing impurities, and after performing microfiltration, a powdered collagen peptide Cpt1 was obtained by spray drying.
About the obtained collagen peptide Cpt1, when the ratio which the glycine accounts for in the N terminal amino acid was analyzed with the analysis method of the N terminal amino acid of the said collagen peptide, it was confirmed that it is the ratio shown in Table 1. Further, when the ratio of glutamic acid and aspartic acid to the total amino acids constituting the collagen peptide was analyzed by the method for analyzing all the amino acids constituting the collagen peptide, the ratio shown in Table 1 was confirmed. The unit of numerical values in Table 1 is “mol%”.

[Production Examples 2 to 6 of collagen peptide]
Collagen peptides Cpt2 to Cpt6 having different average molecular weights were prepared in the same manner as in collagen peptide production example 1 except that the amount of enzyme added was changed. Specifically, Cpt2 having an average molecular weight of 5000 by adding 1.8 g of enzyme, Cpt3 having an average molecular weight of 4000 by adding 2.4 g of enzyme, and Cpt4 having an average molecular weight of 3000 by adding 4.0 g of enzyme, and 5.5 g of enzyme Thus, Cpt5 having an average molecular weight of 2000 and Cpt6 having an average molecular weight of 1000 were prepared by adding 6.0 g of an enzyme.
For each of the obtained collagen peptides Cpt2 to Cpt6, the ratio of glycine in the N-terminal amino acid and the ratio of glutamic acid and aspartic acid to all amino acids constituting the collagen peptide were analyzed, as in the above-mentioned collagen peptide production example 1. The ratios shown in Table 1 were confirmed.

[Production Examples 7 to 12 of collagen peptide]
In addition to the addition of fine activated carbon after enzyme deactivation and microfiltration, the same procedures as in collagen peptide production examples 1 to 6 except that the following operations were performed, Cpt7 having an average molecular weight of 10,000, Cpt8 having 5000, 4000 Cpt9 having 4000 3000 Cpt10, 2000 Cpt11, and 1000 Cpt12 were produced, respectively.
That is, 50 parts by weight of a solution containing each collagen peptide having a different average molecular weight after inactivation of the enzyme was mixed with 1 part by weight of synthetic hydroxyapatite, and after 20 minutes, the mixture was filtered and not adsorbed to hydroxyapatite. The adsorbed fraction was collected as a filtrate.

For each of the obtained collagen peptides Cpt7 to Cpt12, the ratio of glycine in the N-terminal amino acid and the ratio of glutamic acid and aspartic acid to all amino acids constituting the collagen peptide were analyzed as in the above-mentioned Collagen Peptide Production Example 1. The ratios shown in Table 1 were confirmed.
[Production Example 13 of Collagen Peptide]
The enzyme was replaced with 0.6 g of Bromelain F (Amano Enzyme Co.) and 5.5 g of papain (Amano Enzyme Co.) was used. A collagen peptide Cpt13 was produced in the same manner as in Collagen Peptide Production Example 1 except that the pH was adjusted to 60 ° C. and pH 7.5. The average molecular weight of the collagen peptide Cpt13 was 2000.

The obtained collagen peptide Cpt13 was analyzed for the proportion of glycine in the N-terminal amino acid and the proportion of glutamic acid and aspartic acid with respect to all amino acids constituting the collagen peptide, as in Production Example 1 of the collagen peptide. It was confirmed that the ratio was as shown in.
[Production Example 14 of Collagen Peptide]
The enzyme was replaced with 0.6 g of Bromelain F (Amano Enzyme) and 6.0 g of Protease A (Amano Enzyme) was used, and the treatment with the enzyme was performed under the optimum hydrolysis conditions for the enzyme. A collagen peptide Cpt14 was produced in the same manner as in Production Example 1 of collagen peptide except that the temperature was adjusted to 50 ° C. and pH 7.0. The average molecular weight of the collagen peptide Cpt14 was 2000.

  The obtained collagen peptide Cpt14 was analyzed for the proportion of glycine in the N-terminal amino acid and the proportion of glutamic acid and aspartic acid with respect to all amino acids constituting the collagen peptide, as in Production Example 1 of the collagen peptide. It was confirmed that the ratio was as shown in

[Manufacture of chewable tablets]
Using each collagen peptide Cpt1 to Cpt14 obtained by the above operation, each chewable tablet was prepared by the following operation.
Each raw material is powder-mixed at the blending ratio shown in Table 2, granulated using a flow coater (Freund Sangyo Co., Ltd.), and 15 mm in diameter and 1 g / grain using a rotary tableting machine (manufactured by Hata Tekko Co., Ltd.). Each chewable tablet corresponding to Formulation 1-9 was obtained by tableting.

About each chewable tablet corresponding to the mixing | blendings 1-9 obtained as mentioned above, toothedness and food texture were evaluated by the following references | standards. The results are shown in Table 3.
◎ ・ ・ ・ No teeth at all and good texture.
○ ... No teeth and good texture.
Δ: There are some teeth and the texture is slightly inferior.
X: There are teeth and the texture is very bad.

[Evaluation]
(1) Looking at Table 3, regardless of which collagen peptide is used, the higher the amount of collagen peptide added, and the greater the average molecular weight of the collagen peptide, the worse the toothing and texture. It turns out that there is a tendency.
(2) Chewable tablets corresponding to Formulations 1 and 2 in Table 2 have little effect on the toothing and texture of the collagen peptide formulation, and in particular, all chewable tablets with an average molecular weight of 4000 or less are evaluated as ◎. . However, since the blending ratio of the collagen peptide is less than 25% by weight of the total amount, efficient intake of the collagen peptide cannot be realized.

(3) Next, the average molecular weight of chewable tablets containing 25% by weight or more of the total amount of collagen peptides and allowing efficient intake of collagen peptides, ie, each chewable tablet of Formulation 3-9, When it exceeds 4000, all are toothed and have a very bad texture. On the other hand, it can be seen that each chewable tablet according to the present invention having an average molecular weight of 4000 or less is free from toothing and texture and is an excellent food.
(4) Among the chewable tablets of Formulations 3 to 9 according to the present invention, in which collagen peptide is used in an amount of 25% by weight or more based on the total amount as a raw material with an average molecular weight of 4000 or less, in particular, chewables of Formulations 3-8 As for tablets, collagen peptides are contained in 25% by weight or more of the total amount, and sugars (in Table 2, lactitol, reduced maltose starch syrup, crystalline cellulose) are contained in 15% by weight or more, which is insufficient in terms of nutritional function. It turns out that it is a very preferable food without teething and very good texture.

  (5) Furthermore, when Table 3 is seen, the influence which the ratio of glutamic acid and aspartic acid with respect to all the amino acids which comprise a collagen peptide has on the food texture appears remarkably. Specifically, the adsorbed fraction is removed with synthetic hydroxyapatite, and the ratio of glutamic acid to the total amino acids constituting the collagen peptide is 4.0 mol% or less, and the ratio of aspartic acid is 4.0 mol% or less. Each chewable tablet using peptide Cpt7-12 (see Table 1) is markedly evaluated for teething and texture than each chewable tablet using collagen peptide Cpt1-6 (see Table 1) that does not satisfy the above ratio. It turns out that it is excellent.

  (6) Unlike the other collagen peptides Cpt1 to 12, the collagen peptide Cpt13 and 14 has a glycine occupying ratio of 65 mol% or less in the N-terminal amino acid (see Table 1). Therefore, although the average molecular weight is 4000 or less and the collagen peptide is used as a raw material in an amount of 25% by weight or more based on the total amount, the evaluations of the textures of the blends 3 to 9 according to the present invention are all good, but the same average molecular weight Compared with other chewable tablets in terms of blending ratio, other chewable tablets using collagen peptides Cpt1-12 (see Table 1) in which the proportion of glycine in the N-terminal amino acid exceeds 65 mol% are generally toothed. Is suppressed and the texture is good.

  The chewable tablet according to the present invention can be suitably used, for example, as a chewable tablet with nutritional function, which replaces a conventional chewable tablet which has a small amount of collagen peptide or is likely to be toothed.

Claims (4)

The raw material powder mixture containing 25 wt% or more of the collagen peptide based on the total amount a chewable tablet formed by tabletting, the collagen peptide has an average molecular weight of that is Ri der 4000, glycine at its N-terminal amino acid proportion of the Ru der to exceed 65 mol%, characterized in that, chewable tablet. The chewable tablet according to claim 1, wherein the ratio of glutamic acid is 4.0 mol% or less and the ratio of aspartic acid is 4.0 mol% or less with respect to all amino acids constituting the collagen peptide. The chewable tablet according to claim 1 or 2 , wherein a ratio of sugars contained in the raw material powder mixture is 15 to 75% by weight based on the total amount. The chewable tablet according to claim 3 , wherein the saccharide is a cellulosic polysaccharide.