Peptide composition and method for producing the same

Abstract

This peptide composition contains: a collagen peptide; and at least three types of first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenyl acetaldehyde, and methional.

Description

Technical Field

[0001] The present invention relates to a peptide composition and a method for producing the same.

Background Art

[0002] Gelatin and collagen peptides obtained by hydrolyzing the above gelatin are made from collagen extracted from animals typified by cows, pigs, sheep, chickens, ostriches, etc., or fish. Therefore, it is known that they can make people feel a so-called collagen odor such as a raw smell and an animal smell. In applications where the above gelatin and collagen peptides (hereinafter also referred to as "gelatins") are required to be odorless, the above collagen odor may be an obstacle. On the other hand, Japanese Patent Application Laid-Open No. 2007-159557 (Patent Document 1) and Japanese Patent Application Laid-Open No. 2013-236550 (Patent Document 2) disclose techniques for reducing the above collagen odor.

Prior Art Documents

Patent Documents

[0003]

Patent Document 1

Patent Document 2

Summary of the Invention

Problems to be Solved by the Invention

[0004] The above Patent Document 1 and Patent Document 2 disclose a technique for reducing the collagen odor based on capturing odor components causing the collagen odor with a specific compound or chemically reacting the odor components with a specific compound. However, the above Patent Document 1 and Patent Document 2 do not disclose a technique for reducing the molecular weight of the above gelatins. That is, the reduction of the collagen odor and the reduction of the molecular weight of the gelatins have not been achieved simultaneously yet, and the development thereof is eagerly desired.

[0005] In view of the above circumstances, an object of the present invention is to provide a peptide composition in which the collagen odor of collagen peptides obtained by reducing the molecular weight of gelatin or the like is reduced, and a method for producing the same.

Means for Solving the Problems

[0006] The present inventors have found that when gelatin is fermented with koji, the reduction of the molecular weight of the gelatin and the reduction of the collagen odor are achieved simultaneously, and have completed the present invention.

[0007] That is, the present invention has the following features. 〔1〕The peptide composition according to the present invention contains a collagen peptide and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional. 〔2〕Preferably, the peptide composition contains four of the above first compounds. 〔3〕Preferably, the peptide composition contains 0.05 ppm or more of the first compound. 〔4〕Preferably, the peptide composition contains 0.4 ppm or more of the first compound. 〔5〕Preferably, the collagen peptide has a weight average molecular weight of 20,000 or less. 〔6〕Preferably, the peptide composition is a food or a cosmetic. 〔7〕The method for producing a peptide composition according to the present invention includes a step of preparing koji containing koji mold and a collagen raw material, and a step of obtaining a peptide composition by fermenting the collagen raw material with the koji. 〔8〕Preferably, the strain of the koji mold belongs to the genus Aspergillus. 〔9〕Preferably, the strain of the koji mold is at least one selected from the group consisting of Aspergillus sojae, Aspergillus oryzae, and Aspergillus luchuensis. 〔10〕The above-mentioned collagen raw material is preferably at least one selected from the group consisting of the following Group 1 to Group 6, collagen extracted from at least one selected from the above group, gelatin obtained by treating the above collagen, and at least any one of gelatin hydrolyzates obtained by hydrolyzing the above gelatin. Group 1: The group consisting of cowhide, skin, bone, cartilage, and tendon Group 2: The group consisting of pigskin, skin, bone, cartilage, and tendon Group 3: The group consisting of sheepskin, skin, bone, cartilage, and tendon Group 4: The group consisting of chicken skin, skin, bone, cartilage, and tendon Group 5: The group consisting of ostrich skin, skin, bone, cartilage, and tendon Group 6: The group consisting of fish bones, skin, and scales 〔11〕The peptide composition according to the present invention contains collagen peptides produced by fermenting a collagen raw material with koji.

Advantages of the Invention

[0008] According to the above, it is possible to provide a peptide composition in which the collagen odor of collagen peptides reduced in molecular weight from gelatin or the like is reduced, and a method for producing the same.

Embodiments for Carrying Out the Invention

[0009] Hereinafter, embodiments according to the present invention (hereinafter also referred to as "the present embodiments") will be described in more detail. Here, in this specification, the notation in the form of "A to B" means the upper and lower limits of the range (that is, A or more and B or less). When there is no unit description for A and there is a unit description only for B, the units of A and B are the same.

[0010] In this specification, the "peptide composition" may be in a solid state such as powder, or may be in a liquid state such as an aqueous solution dissolved in water. In this specification, "fermentation" means the entire process in which beneficial organic substances are produced from raw materials by the activity of koji mold contained in koji, and is distinguished from "decay" in which non-beneficial organic substances are produced from raw materials by the activity of microorganisms.

[0011] In this specification, the term "gelatin" may be used when referring to the substance name, gelatin gel, and gelatin solution, respectively. Also, for the term "collagen peptide", similar to the above gelatin, it may be used when referring to the substance name and collagen peptide solution, respectively.

[0012] In this specification, the "collagen raw material" refers to at least one "itself" selected from the group consisting of the following Group 1 to Group 6, "collagen" extracted from at least one selected from the group consisting of the following Group 1 to Group 6, "gelatin" obtained by treating the above collagen using a known method such as hot water extraction, and "gelatin hydrolyzate" obtained by hydrolyzing the above gelatin. Furthermore, the "hydrolysis" of the above gelatin includes all of hydrolysis using an acid, hydrolysis using a base, hydrolysis using an enzyme, and hydrolysis using heating. Group 1: The group consisting of cowhide, skin, bone, cartilage, and tendon Group 2: The group consisting of pigskin, skin, bone, cartilage, and tendon Group 3: The group consisting of sheepskin, skin, bone, cartilage, and tendon Group 4: The group consisting of chicken skin, skin, bone, cartilage, and tendon Group 5: The group consisting of ostrich skin, skin, bone, cartilage, and tendon Group 6: The group consisting of fish bones, skin, and scales.

[0013] In this specification, the "collagen odor" means an odor that gives people a feeling of discomfort, such as a raw smell or an animal smell, which is the gelatin or gelatin hydrolyzate obtained from collagen derived from at least one selected from the group consisting of the above-mentioned Group 1 to Group 6. The above-mentioned collagen odor is also felt by people as the odor of the collagen peptide when the collagen peptide is obtained from the above-mentioned collagen raw material. Generally, Orientals are considered to be more sensitive to the above-mentioned collagen odor than Westerners.

[0014] [Peptide Composition] The peptide composition according to this embodiment includes a collagen peptide and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional. The above peptide composition preferably contains the four above-mentioned first compounds. By having such characteristics, this embodiment can provide a peptide composition with reduced collagen odor possessed by the collagen peptide. In particular, the above peptide composition can be obtained by fermenting a collagen raw material with koji.

[0015] [Collagen Peptide] The peptide composition according to this embodiment contains a collagen peptide as described above. The collagen peptide is a conventionally known collagen peptide. That is, the collagen peptide means a peptide mixture that can contain various peptides such as dipeptides, tripeptides, oligopeptides, and polypeptides obtained by performing conventionally known treatments on collagen or gelatin. In the above peptide composition, the collagen peptide is preferably obtained by fermenting a collagen raw material with koji. In this case, the collagen peptide is obtained by reducing the molecular weight from the collagen raw material, and the collagen odor is reduced by being masked by the first compound described below.

[0016] (Weight-average molecular weight) The above-mentioned collagen peptide preferably has a weight average molecular weight of 20,000 or less. When the weight average molecular weight of the above-mentioned collagen peptide is 20,000 or less, the peptide composition can be easily applied to food or cosmetic uses without additional treatment. The above-mentioned collagen peptide more preferably has a weight average molecular weight of 10,000 or less, and even more preferably 6,000 or less. The lower limit of the weight average molecular weight of the above-mentioned collagen peptide is 76. When the weight average molecular weight of the above-mentioned collagen peptide exceeds 20,000, it cannot be said to be sufficiently low molecular weight, and thus may be unsuitable for, for example, food or cosmetic uses.

[0017] Here, the weight average molecular weight of the above-mentioned collagen peptide contained in the above-mentioned peptide composition can be determined by performing size exclusion chromatography (SEC) under the following measurement conditions. The inventors have confirmed that this measurement method is also valid for measuring molecular weights exceeding 12,000. Equipment: High Performance Liquid Chromatography (HPLC) (manufactured by Tosoh Corporation) Column: TSKGel (registered trademark) G2000SW XL Column temperature: 40 °C Eluent: 45 mass% acetonitrile (containing 0.1 mass% TFA) Flow rate: 1.0 mL / min Injection volume: 10 μL Detection: UV214 nm Molecular weight markers: The following 5 types are used Cytochrom C Mw: 12,000 Aprotinin Mw: 6,500 Bacitracin Mw: 1,450 Gly-Gly-Tyr-Arg Mw: 451 Gly-Gly-Gly Mw: 189.

[0018] <First compound> The peptide composition according to this embodiment contains at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as described above. The first compound has an effect of masking the odor components that cause the collagen odor of the above-mentioned collagen peptide. In the above peptide composition, the first compound is considered to be produced together with the collagen peptide by fermenting the collagen raw material with koji as described later.

[0019] The above peptide composition may contain isovaleraldehyde, 1-octen-3-ol, and phenylacetaldehyde as the first compound, may contain isovaleraldehyde, 1-octen-3-ol, and methional, may contain isovaleraldehyde, phenylacetaldehyde, and methional, or may contain 1-octen-3-ol, phenylacetaldehyde, and methional. In particular, it is preferable that the above peptide composition contains the four (isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional) first compounds.

[0020] (Isovaleraldehyde) Isovaleraldehyde is a compound also known as isovaleric aldehyde, 3-methylbutanal, or 3-methylbutyl aldehyde, and is a compound that has been conventionally used as a fragrance (food additive) and the like.

[0021] (1-Octen-3-ol) 1-Octen-3-ol is a kind of unsaturated alcohol and is a compound known to conventionally contribute to the aroma of matsutake mushrooms.

[0022] (Phenylacetaldehyde) Phenylacetaldehyde is a kind of aromatic aldehyde and is a compound that has been conventionally used as a raw material for formulating fragrances and flavors.

[0023] (Methional) Methional is a kind of organic sulfur compound and is also a compound called 3-methylthio-1-propanol. Methional is a compound that has been conventionally known to be contained in soy sauce. Furthermore, methional is also known to have an effect of weakening the fishy smell of meat and fish. Na

[0024] (Content) The first compound is preferably contained in the above peptide composition at 0.05 ppm or more as its total amount (total of at least three or four kinds). That is, the above peptide composition preferably contains the first compound at 0.05 ppm or more. Thereby, the above peptide composition can sufficiently reduce the collagen smell.

[0025] More preferably, the first compound is contained in the above peptide composition at 0.4 ppm or more as its total amount. That is, the above peptide composition more preferably contains the first compound at 0.4 ppm or more. In this case, the above peptide composition can more sufficiently reduce the collagen smell.

[0026] More preferably, the above peptide composition contains the first compound at 0.45 ppm or more as its total amount. Thereby, the collagen smell can be more sufficiently reduced. On the other hand, it is necessary for the above peptide composition to contain the first compound at 0.01 ppm or more as its total amount. When the content of the first compound is less than 0.01 ppm, the masking effect on the above collagen peptide tends to be insufficient. The upper limit value of the content of the first compound is not particularly limited, but in order not to have an adverse effect on the above peptide composition due to the smell of the first compound, it is preferably 5 ppm or less as its total amount.

[0027] ​The qualitative and quantitative determination of the above first compound contained in the above peptide composition can be determined by the following procedure. First, a dry powder of the peptide composition is obtained by the production method described later. Further, a measurement sample is obtained by dissolving 0.5 g of the above dry powder in 4.5 mL of RO water. Next, the above measurement sample is introduced into a gas chromatograph mass spectrometer (trade name: "7890A GC System", manufactured by Agilent Technologies, Inc., and trade name: "JMS-Q1050GC", manufactured by JEOL Ltd.), vaporized, and then moved to a column provided in the above analyzer using ultra-high purity helium as a carrier gas to separate the components contained in the above measurement sample for each compound. Further, the above compound is detected by a detector provided in the above analyzer, and the qualitative determination of the above first compound can be performed by comparing the data (spectrum data) obtained from the above detector with the standard data. At the same time, the above first compound can be quantified based on the above spectrum data (peak area) obtained from the above detector.

[0028] <Food or Cosmetic> The peptide composition according to the present embodiment is preferably a food or a cosmetic. When the peptide composition is a food, it is possible to provide the above peptide composition as a food with a reduced fishy smell of collagen, although it contains collagen peptides. In this case, the above peptide composition can impart an added value of reducing the fishy smell of collagen in various applications of both foodstuffs and beverages containing collagen peptides. In particular, the above peptide composition is useful in food applications and the like where it is required to be odorless.

[0029] Furthermore, when the above peptide composition is a cosmetic, it is possible to provide the above peptide composition as a cosmetic with a reduced collagen odor despite containing collagen peptides. In this case, the above peptide composition can impart added values such as reducing the collagen odor and suppressing the amount of perfume used in various applications of cosmetics containing collagen peptides. In particular, the above peptide composition is useful in cosmetic applications where it is required to be odorless.

[0030] Here, in this specification, "when the peptide composition is a food" means a food containing collagen peptides and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional. Also, "when the peptide composition is a cosmetic" means a cosmetic containing collagen peptides and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional.

[0031] (Food) When the above peptide composition is a food, the above peptide composition may be, for example, a food for specified health use or a food with functional claims. The concentration of the peptide composition in the above food for specified health use or food with functional claims can be 0.01 to 100% by mass. Note that since the content of the first compound in the above food is very small, the concentration of the collagen peptides in the above peptide composition is meant. Therefore, the concentration of the peptide composition in the above food can be determined by a conventionally known method for measuring the concentration of collagen peptides. For example, the concentration of the peptide composition in the above food can be determined by measuring the mass percentage of hydroxyproline in the collagen peptides by the chloramine T method. Furthermore, it is also possible to determine it by measuring the mass percentage of hydroxyproline in the collagen peptides using an amino acid analyzer.

[0032] Cosmetic When the peptide composition is a cosmetic, the concentration of the peptide composition in the cosmetic can be 0.01 to 100% by mass. Note that, similar to the above food, since the content of the first compound is extremely small, the concentration of the collagen peptide in the peptide composition is meant. Therefore, the concentration of the peptide composition contained in the cosmetic can be the same as the method for measuring the concentration of the peptide composition in the above food described above.

[0033] 〔Method for producing peptide composition〕 The method for producing the peptide composition according to this embodiment includes a step of preparing koji containing Aspergillus oryzae and a collagen raw material (first step), and a step of obtaining a peptide composition by fermenting the collagen raw material with the koji (second step). The method for producing a peptide composition having such characteristics can produce a peptide composition in which low-molecular-weight collagen peptides are obtained and the collagen odor of the collagen peptides is reduced at the same time.

[0034] In the peptide composition produced by the above manufacturing method, the reason why low-molecular-weight collagen peptides can be obtained and the collagen odor can be reduced simultaneously is not clear in detail, but it is considered to be due to the following mechanism. That is, the above manufacturing method includes a step (second step) of obtaining a peptide composition by fermenting a collagen raw material with koji. The above koji is known to contain a variety of enzymes produced by the propagation of koji mold. Therefore, in the second step, these various enzymes may act to decompose or redox polypeptides in the collagen raw material and carbohydrates in the koji. Therefore, in the second step, it is presumed that the above-mentioned various enzymes act to reduce the molecular weight of the above polypeptide and produce a first compound that masks the odor component causing the above collagen odor. Thus, it is considered that the above manufacturing method can produce a peptide composition in which low-molecular-weight collagen peptides are obtained and the collagen odor of the above collagen peptides is reduced simultaneously. Hereinafter, each step in the manufacturing method of the peptide composition according to the present embodiment will be described.

[0035] <First Step> The first step is a step of preparing koji containing koji mold and a collagen raw material. The first step is carried out for the purpose of preparing each material (koji containing koji mold and collagen raw material) required for producing the above peptide composition.

[0036] (Collagen Raw Material) The collagen raw material may be at least any one of at least one "itself" selected from the group consisting of the following first group to sixth group as described above, "collagen" extracted from at least one selected from the group consisting of the following first group to sixth group, "gelatin" obtained by treating the above collagen using a known method such as hot water extraction, and "gelatin degradation product" obtained by hydrolyzing the above gelatin. First Group: The group consisting of cowhide, skin, bone, cartilage and tendon Group 2: A group consisting of pig skin, skin, bone, cartilage and tendon Group 3: A group consisting of sheep skin, skin, bone, cartilage and tendon Group 4: A group consisting of chicken skin, skin, bone, cartilage and tendon Group 5: A group consisting of ostrich skin, skin, bone, cartilage and tendon Group 6: A group consisting of fish bone, skin and scale.

[0037] That is, in the first step, it is preferable that at least one selected from the group consisting of the above-mentioned Group 1 to Group 6 is prepared as the above-mentioned collagen raw material, and at least one selected from the group consisting of the above-mentioned collagen, the above-mentioned gelatin and the above-mentioned gelatin degradation product. In the first step, one kind of collagen raw material selected from these may be prepared, or two or more kinds of collagen raw materials may be prepared in combination. The above-mentioned Group 1 to Group 6, the above-mentioned collagen, the above-mentioned gelatin and the above-mentioned gelatin degradation product can all be prepared by conventionally known methods.

[0038] Here, the above-mentioned gelatin is more preferably obtained by performing pretreatment by acid treatment or alkali treatment, hot water extraction, purification treatment and sterilization treatment in this order on collagen extracted from at least one selected from the group consisting of the above-mentioned Group 1 to Group 6. Thereby, gelatin with high safety for the human body and the like can be prepared, and thus the peptide composition to be produced in this embodiment can be applied to the uses of the above-mentioned food or cosmetic. Furthermore, such gelatin is also excellent in economy. The above-mentioned pretreatment by acid treatment or alkali treatment, hot water extraction, purification treatment and sterilization treatment can all be performed by conventionally known methods.

[0039] The above gelatin hydrolyzate can be obtained by performing any one of hydrolysis using a conventionally known acid, hydrolysis using a base, hydrolysis using an enzyme, and hydrolysis using heat on the above gelatin. The weight average molecular weight of the gelatin hydrolyzate is not particularly limited, but is preferably, for example, 20,000 or less, and more preferably 10,000 or less. The lower limit of the weight average molecular weight of the above gelatin hydrolyzate is 76. The weight average molecular weight of the above gelatin hydrolyzate can be determined by the same measurement method as the weight average molecular weight of the collagen peptide described above.

[0040] (Koji containing Aspergillus oryzae) Koji containing Aspergillus oryzae can be prepared by a conventionally known method as long as koji that can obtain the effects of the present embodiment is selected by performing the second step described below. That is, it can be obtained by inoculating Aspergillus oryzae as the mother koji on miscellaneous grains such as rice, barley, wheat, or soybeans, and then propagating it in the above rice, barley, wheat, or miscellaneous grains. It is preferable to inoculate the above Aspergillus oryzae in an amount of 0.01 to 1% by mass based on the above rice, barley, wheat, or miscellaneous grains. In this specification, the category of "miscellaneous grains" includes all of the above-mentioned soybeans, bran, rice bran, okara, and defatted soybeans. In the preparation of koji containing Aspergillus oryzae, it is preferable to prepare an environment in which Aspergillus oryzae easily propagates by providing a koji room for preventing the contamination of other bacteria, and perform necessary operations in the above koji room.

[0041] The bacterial species of the above Aspergillus oryzae is preferably a bacterial species belonging to the genus Aspergillus. The bacterial species of the above Aspergillus oryzae is more preferably at least one selected from the group consisting of Aspergillus sojae, Aspergillus oryzae, and Aspergillus luchuensis. Since these bacterial species have been confirmed to be safe for the human body and the like, the peptide composition produced in the present embodiment can be easily applied to the above-mentioned food or cosmetic uses. In the first step, koji containing one kind selected from the group of these bacterial species may be prepared, or koji containing two or more kinds selected from the group of the above bacterial species may be prepared.

[0042] <Second Step> The second step is a step of obtaining a peptide composition by fermenting the above collagen raw material with the above koji. The second step is carried out for the purpose of obtaining collagen peptides by reducing the molecular weight of the above collagen raw material and reducing the collagen odor of the above collagen peptides. In the second step, for example, the above collagen raw material and the above koji are put into warm water, and these are cultured in warm water for a predetermined time to ferment the above collagen raw material with the above koji, whereby a fermented product containing the above peptide composition can be obtained.

[0043] Specifically, a dispersion is prepared from 0.1 to 75% by mass of the above collagen raw material, 0.1 to 20% by mass of the above koji as dry mass (dry weight), and 5 to 99.8% by mass of water, with the total of these being 100% by mass. After further adjusting the pH of the above dispersion to 2 to 10, it is preferable to culture for 1 to 24 hours while maintaining the temperature of the above dispersion at 10 to 65°C. Thereby, a fermented product containing a peptide composition containing collagen peptides and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional can be obtained.

[0044] It is also preferable to obtain the above-mentioned fermented product by the following method. That is, first, a dispersion in which the total of the above koji at 0.1 to 40% by mass (dry weight) and water at 60 to 99.9% by mass is 100% by mass is prepared, and the temperature of the above dispersion is maintained at 10 to 65°C while culturing for 1 to 24 hours, followed by rough filtration through a nylon mesh and filtration with diatomaceous earth and cellulose to obtain a koji extract. Next, a dispersion in which the total of the above collagen raw material at 0.1 to 75% by mass and the above koji extract at 0.1 to 99.9% by mass is 100% by mass is prepared, and after adjusting the pH of the above dispersion to 2 to 10, the temperature of the above dispersion is maintained at 10 to 65°C while culturing for 1 to 24 hours. By this method as well, a fermented product containing a peptide composition can be obtained. When a fermented product is obtained by applying this method, a peptide composition can be obtained without performing the separation treatment step described later on the fermented product. However, it does not exclude performing at least one of the purification step and the deodorization step described later on the fermented product.

[0045] The temperature of the warm water during culturing is preferably 15 to 60°C, more preferably 20 to 50°C. When the temperature of the warm water during culturing is below 10°C or exceeds 65°C, the efficiency of fermentation by koji may decrease, resulting in insufficient low-molecular-weight conversion of the collagen raw material and reduction of the collagen odor.

[0046] Furthermore, the culturing time is preferably 2 to 18 hours, more preferably 4 to 8 hours. When the culturing time exceeds 24 hours, it may be economically inefficient. When the culturing time is less than 1 hour, the fermentation by koji may be insufficient.

[0047] The content of the collagen raw material in the warm water during culturing is preferably 10 to 45% by mass, more preferably 20 to 40% by mass. When the content of the collagen raw material in the warm water during culturing is less than 0.1% by mass, it may be economically inefficient. When the content of the collagen raw material in the warm water during culturing exceeds 75% by mass, the operation may be inefficient.

[0048] The content of koji in the dispersion liquid composed of the above koji, the above collagen raw material and water is preferably 1 to 15% by mass, more preferably 5 to 10% by mass, as the dry mass (dry weight). When the content of koji in the warm water during cultivation is less than 0.1% by mass as the dry mass (dry weight), the fermentation by koji may be insufficient. When the content of koji in the warm water during cultivation exceeds 20% by mass as the dry mass (dry weight), it may be economically inefficient. The content of koji in the above koji extract is preferably 2 to 25% by mass, more preferably 8 to 16% by mass. When the content of koji in the koji extract is less than 0.1% by mass as the dry mass (dry weight), the fermentation by koji may be insufficient. When the content of koji in the koji extract exceeds 40% by mass as the dry mass (dry weight), it may be economically inefficient.

[0049] The pH value during the cultivation of the above dispersion liquid is preferably 2 to 10, more preferably 5 to 8. When the pH value during the cultivation of the above dispersion liquid is less than 2 or exceeds 10, there is a risk that the low molecular weight of the collagen raw material and the reduction of the collagen odor may be insufficient.

[0050] Here, in the second step, after obtaining a fermented product containing a peptide composition by the above steps, the temperature is set to 75 °C or higher according to the purpose to inactivate the action (activity) of Aspergillus oryzae, thereby stopping the progress of the fermentation of the collagen raw material by koji. Specifically, the weight average molecular weight of the collagen peptide in the above fermented product is measured, and it is confirmed that it has a lower molecular weight compared to the collagen raw material, or when the cultivation time has elapsed for a predetermined time, for example, 24 hours, the temperature of the above fermented product is set to 75 °C or higher to stop the progress of the fermentation of the collagen raw material by koji. The weight average molecular weight of the collagen peptide in the fermented product can be, for example, the same as the measurement method of the weight average molecular weight of the collagen peptide described above.

[0051] (Other steps) The second step preferably includes a separation treatment step to obtain a peptide composition from the above-mentioned fermented product. For this separation treatment step, conventionally known separation treatments can be applied. For example, a peptide composition can be separated from the above-mentioned fermented product by separation treatments such as rough filtration using a nylon mesh, centrifugation, and filter paper filtration using commercially available filter paper. Thereby, a peptide composition containing collagen peptide and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional can be obtained.

[0052] Furthermore, it is also preferable that the second step includes a purification step (purification process) for purifying the peptide composition obtained by applying the above-mentioned separation treatment step or the above-mentioned fermented product for the purpose of increasing its transparency. In this purification step, conventionally known purification treatments can be applied. For example, a purification treatment using diatomaceous earth or a purification treatment by microfiltration can be performed. Furthermore, depending on the need, deodorization treatment (deodorization process) is not excluded by using activated carbon or the like.

[0053] The peptide composition obtained as described above can be stored as it is in a solution state. Furthermore, for the peptide composition in a solution state, a dry powder of the peptide composition can be obtained by using conventionally known methods such as spraying or drum drying, and it can also be stored in that state.

[0054] <Function and effect> From the above, the method for producing a peptide composition according to this embodiment can obtain a peptide composition containing collagen peptide and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional.

Example

[0055] Hereinafter, the present invention will be described in more detail with reference to examples, but the present invention is not limited thereto. In the following description, Sample 1 to Sample 11 and Sample 12 are the peptide compositions of the examples, and Sample 101 to Sample 103 are the peptide compositions of the comparative examples.

[0056] 〔Preparation of Samples〕 <Sample 1> (First Step) Aspergillus oryzae-containing koji and a collagen raw material were prepared according to the following procedure.

[0057] 〈Preparation of Aspergillus oryzae-containing koji〉 As the Aspergillus oryzae-containing koji, barley bran koji inoculated with Aspergillus sojae (manufactured by Higuchi Matsunosuke Shoten Co., Ltd.) was prepared.

[0058] 〈Preparation of collagen raw material〉 As the collagen raw material, a gelatin hydrolyzate having a weight average molecular weight of about 4000 derived from tilapia scales (trade name: "HDL-50SP", manufactured by Nitta Gelatin Inc.) was prepared.

[0059] (Second Step) The above collagen raw material was fermented with the above koji to obtain a peptide composition according to the following procedure. First, a dispersion consisting of 40% by mass of the above collagen raw material, 8% by mass (dry weight) of the above barley bran koji, and 52% by mass of RO water was prepared, and the dispersion was cultured for 6 hours while maintaining the temperature at 40°C. Then, the temperature of the dispersion was raised to 75°C, and the dispersion was maintained at a temperature near 75°C for 60 minutes to inactivate the koji mold in the above barley bran koji, thereby obtaining a fermented product containing the peptide composition.

[0060] Next, the above fermented product was centrifuged at a centrifugal acceleration of 1610G for 30 minutes, and the supernatant was obtained to obtain the peptide composition of Sample 1.

[0061] The peptide composition of Sample 1 is an aqueous solution. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above-mentioned collagen raw material. Also, from the analysis using the above-mentioned gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 1 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0062] <Sample 2> As koji containing koji mold, except for preparing barley bran koji inoculated with Aspergillus oryzae (manufactured by Higuchi Matsunosuke Shoten Co., Ltd.), the peptide composition of Sample 2 was obtained by the same method as obtaining Sample 1.

[0063] The peptide composition of Sample 2 is an aqueous solution. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above-mentioned collagen raw material. Also, from the analysis using the above-mentioned gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 2 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0064] <Sample 3> As koji containing koji mold, except for preparing barley bran koji inoculated with Aspergillus luchuensis (manufactured by Higuchi Matsunosuke Shoten Co., Ltd.), the peptide composition of Sample 3 was obtained by the same method as obtaining Sample 1.

[0065] The peptide composition of Sample 3 is an aqueous solution. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above-mentioned collagen raw material. Also, from the analysis using the above-mentioned gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 3 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0066] <Sample 4> Except for preparing gelatin derived from porcine skin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc., weight average molecular weight: about 65,000) as the collagen raw material, a peptide composition of Sample 4 was obtained by the same method as obtaining Sample 1.

[0067] The peptide composition of Sample 4 was an aqueous solution. When its weight average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight average molecular weight of the above collagen raw material. Also, from the analysis using the above-described gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 4 contained isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0068] <Sample 5> Except for preparing gelatin derived from porcine skin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc., weight average molecular weight: about 65,000) as the collagen raw material, a peptide composition of Sample 5 was obtained by the same method as obtaining Sample 2.

[0069] The peptide composition of Sample 5 was an aqueous solution. When its weight average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight average molecular weight of the above collagen raw material. Also, from the analysis using the above-described gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 5 contained isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0070] <Sample 6> Except for preparing gelatin derived from porcine skin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc., weight average molecular weight: about 65,000) as the collagen raw material, a peptide composition of Sample 6 was obtained by the same method as obtaining Sample 3.

[0071] The peptide composition of Sample 6 is an aqueous solution. When measuring its weight-average molecular weight, it was confirmed that the weight-average molecular weight was lower compared to that of the above collagen raw material. Also, from the analysis using the above gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 6 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0072] <Sample 7> (First step) According to the following procedure, koji containing Aspergillus oryzae and a collagen raw material were prepared.

[0073] 〈Preparation of koji containing Aspergillus oryzae〉 As koji containing Aspergillus oryzae, barley bran koji inoculated with Aspergillus sojae (manufactured by Higuchi Matsunosuke Shoten Co., Ltd.) was prepared.

[0074] 〈Preparation of collagen raw material〉 As the collagen raw material, gelatin derived from bovine bone (trade name: "♯250", manufactured by Nitta Gelatin Inc., weight-average molecular weight: approximately 190,000) was prepared.

[0075] (Second step) According to the following procedure, the above collagen raw material was fermented with the above koji to obtain a peptide composition. First, a dispersion consisting of 10% by mass of the above collagen raw material, 2% by mass (dry weight) of the above barley bran koji, and 88% by mass of RO water was prepared, and the dispersion was cultured for 6 hours while maintaining the temperature of the dispersion at 40°C. Then, the temperature of the dispersion was set to 75°C, and the koji in the above barley bran koji was inactivated by maintaining the dispersion at a temperature near 75°C for 60 minutes, thereby obtaining a fermented product containing a peptide composition.

[0076] Next, the above fermented product was centrifuged at a centrifugal acceleration of 1610G for 30 minutes, and the supernatant was obtained to obtain the peptide composition of Sample 7.

[0077] The peptide composition of Sample 7 is an aqueous solution. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above-mentioned collagen raw material. Also, from the analysis using the above-mentioned gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 7 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0078] <Sample 8> A peptide composition of Sample 8 was obtained by the same method as for obtaining Sample 7, except that gelatin derived from porcine skin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc., weight-average molecular weight: about 65,000) was prepared as the collagen raw material.

[0079] The peptide composition of Sample 8 is an aqueous solution. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above-mentioned collagen raw material. Also, from the analysis using the above-mentioned gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 8 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0080] <Sample 9> A peptide composition of Sample 9 was obtained by the same method as for obtaining Sample 7, except that gelatin derived from tilapia scales (manufactured by Nitta Gelatin Inc., weight-average molecular weight: about 150,000) was prepared as the collagen raw material.

[0081] The peptide composition of Sample 9 is an aqueous solution. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above-mentioned collagen raw material. Also, from the analysis using the above-mentioned gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 9 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compounds.

[0082] <Sample 10> After obtaining the supernatant by centrifugation in the second step, the supernatant was filtered through filter paper and diatomaceous earth filtration, and a peptide composition was obtained as a dry powder by using a spray dryer (manufactured by Okawara Seisakusho Co., Ltd.). A peptide composition of Sample 10 was obtained in the same manner as Sample 4, except for the above operations.

[0083] The peptide composition of Sample 10 was a dry powder. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was lower compared to the weight-average molecular weight of the above collagen raw material. Also, from the analysis using the above gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 10 contained isovaleraldehyde, phenylacetaldehyde, and methional as the first compound.

[0084] <Sample 11> (First step) Koji containing Aspergillus oryzae and a collagen raw material were prepared by the following procedure.

[0085] <Preparation of koji containing Aspergillus oryzae> As koji containing Aspergillus oryzae, barley bran koji inoculated with Aspergillus sojae (manufactured by Higuchi Matsunosuke Shoten Co., Ltd.) was prepared.

[0086] <Preparation of collagen raw material> After washing the dehaired cowhide (produced in the United States) with running water, it was mechanically refined by using a commercially available meat grinder equipped with a plate having pores with a diameter of 6 mm and a stone mortar type ultra-fine grinding machine (manufactured by Masayuki Sangyo Co., Ltd.) to obtain paste-like cowhide collagen. Thereby, a collagen raw material was prepared. Although it is difficult to accurately calculate the weight-average molecular weight of the above collagen raw material, it is considered to be 300,000 or more.

[0087] (Second step) A peptide composition was obtained by fermenting the above collagen raw material with the above koji according to the following procedure. First, a dispersion consisting of 2.5% by mass of the above collagen raw material (cowhide collagen), 0.5% by mass of the above barley bran koji (dry weight), and 97% by mass of RO water was prepared, and cultured for 24 hours while maintaining the temperature of the dispersion at 40°C. Then, the temperature of the dispersion was raised to 75°C, and the koji mold in the above barley bran koji was inactivated by maintaining the dispersion at a temperature near 75°C for 60 minutes, thereby obtaining a fermented product containing a peptide composition. This fermented product was used as the peptide composition of Sample 11.

[0088] The peptide composition of Sample 11 is a dispersion (suspension). When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above collagen raw material. Also, from the analysis using the above gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 11 contains isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compound.

[0089] <Sample 12> (Step 1) The koji containing koji mold and the collagen raw material were prepared according to the following procedure.

[0090] <Preparation of Koji Containing Koji Mold> As the koji containing koji mold, barley bran koji inoculated with Aspergillus sojae (manufactured by Higuchi Matsunosuke Shoten Co., Ltd.) was prepared.

[0091] <Preparation of Collagen Raw Material> As the collagen raw material, gelatin derived from pigskin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc., weight-average molecular weight: about 65,000) was prepared.

[0092] (Step 2) The following procedure was used to obtain a peptide composition by fermenting the above collagen raw material with the above koji. First, a dispersion consisting of 6% by mass of the above barley bran koji (dry weight) and 94% by mass of RO water was prepared and stirred for 1 hour while maintaining the temperature of the dispersion at 40°C. Then, a koji extract was obtained by performing rough filtration through a nylon mesh and filtration with diatomaceous earth and cellulose. Next, a dispersion consisting of 40% by mass of the above collagen raw material and 60% by mass of the above koji extract was prepared and cultured for 6 hours while maintaining the temperature of the dispersion at 40°C. Then, the temperature of the dispersion was set to 60°C, and pasteurization was performed by maintaining the dispersion at a temperature near 60°C for 60 minutes. Moreover, a peptide composition of Sample 12 was obtained as a dry powder by using a spray dryer (manufactured by Okawara Seisakusho Co., Ltd.).

[0093] The peptide composition of Sample 12 was a dry powder. When its weight-average molecular weight was measured, it was confirmed that the molecular weight was reduced compared to the weight-average molecular weight of the above collagen raw material. Also, from the analysis using the above gas chromatograph mass spectrometer, it was confirmed that the peptide composition of Sample 12 contained isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional as the first compound.

[0094] <Sample 101> A dispersion consisting of 40% by mass of gelatin (manufactured by Nitta Gelatin Inc.) with a weight-average molecular weight of approximately 150,000 derived from tilapia scales, 0.4% by mass of alcalase 2.4LFG, an enzyme derived from Bacillus licheniformis (manufactured by Novozymes Japan), and 59.6% by mass of RO water was prepared. Then, the dispersion was cultured for 2 hours while maintaining the temperature at 60°C. Then, the temperature of the dispersion was set to 75°C, and the enzyme was inactivated by maintaining the dispersion at a temperature near 75°C for 60 minutes, and a deodorization step using activated carbon was performed to obtain the peptide composition of Sample 101.

[0095] <Sample 102> A dispersion was prepared from 40% by mass of gelatin with a weight average molecular weight of approximately 65,000 derived from porcine skin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc.), 0.4% by mass of papain W-40, an enzyme derived from papaya (manufactured by Amano Enzyme Inc.), and 59.6% by mass of RO water. The dispersion was cultured for 2 hours while maintaining the temperature of the dispersion at 60°C. Then, the temperature of the dispersion was set to 75°C, and the enzyme was inactivated by maintaining the dispersion at a temperature near 75°C for 60 minutes, thereby obtaining the peptide composition of Sample 102.

[0096] <Sample 103> A dispersion was prepared from 10% by mass of gelatin with a weight average molecular weight of approximately 65,000 derived from porcine skin (trade name: "BCN-HL", manufactured by Nitta Gelatin Inc.), 0.5% by mass of flavorzyme, an enzyme derived from Aspergillus oryzae (manufactured by Novozymes Japan), and 89.5% by mass of RO water. The dispersion was cultured for 6 hours while maintaining the temperature of the dispersion at 55°C. Then, the temperature of the dispersion was set to 75°C, and the enzyme was inactivated by maintaining the dispersion at a temperature near 75°C for 60 minutes, thereby obtaining the peptide composition of Sample 103.

[0097] 〔First Test〕 <Odor Sensory Test> Regarding Samples 1 to 6 and Samples 101 to 103, after adjusting the concentration of their collagen peptides to 10% by mass using RO water, 20 mL of each was prepared. Further, for Sample 10, a solution (20 mL) obtained by dissolving 2 g of the above dry powder in 18 mL of RO water was prepared. An odor sensory test regarding how much collagen odor was felt for each of the above samples was performed by 5 evaluators. In the above odor sensory test, as shown in Table 1, scores of 1 to 4 were assigned to each sample. It can be evaluated that the higher the score, the more the so-called collagen odor such as raw odor and animal odor is reduced. The results are shown in Table 2.

[0098]

Table 1

[0099]

Table 2

[0100] <Investigation> According to Table 2, the peptide compositions of Sample 1 to Sample 6 and Sample 10 were evaluated to have a reduced collagen odor compared to the peptide compositions of Sample 101 to Sample 103.

[0101] 〔Second Test〕 <Qualitative and Quantitative Tests> Five milliliters of a solution in which the collagen peptide concentrations of Sample 4, Sample 5, and Sample 102 were adjusted to 10% by mass were each prepared. Further, for Sample 10, a solution (5 mL) obtained by dissolving 0.5 g of the above dry powder in 4.5 mL of RO water was prepared. For each of the above samples, components in each sample were identified using a gas chromatograph mass spectrometer (trade names: "7890A GC System", manufactured by Agilent Technologies, Inc., and "JMS-Q1050GC", manufactured by JEOL Ltd.), and qualitative and quantitative tests of the first compound in each sample were performed. The methods of the above qualitative and quantitative tests were as described above. The results are shown in Table 3. The units of the numerical values shown in Table 3 are ppm, and "N.D" indicates that it was not detected.

[0102]

Table 3

[0103] <Investigation> According to Table 3, the peptide compositions of Sample 4, Sample 5, and Sample 10 all had at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional. On the other hand, the peptide composition of Sample 102 had only methional.

[0104] 〔Third Test〕 <Weight-Average Molecular Weight of Collagen Peptide> Regarding Samples 1 to 3, it was investigated to what extent the collagen raw material was converted into collagen peptides with a lower molecular weight through the second step. Specifically, regarding Samples 1 to 3, the weight-average molecular weight of the collagen peptides contained in the above peptide composition after fermentation for 6 hours in the second step was determined according to the measurement method described above. The results are shown in Table 4.

[0105]

Table 4

[0106] <Discussion> According to Table 4, it is understood that the peptide compositions of Samples 1 to 3 had their collagen raw materials reduced in molecular weight through the second step.

[0107] 〔Fourth Test〕 <Weight-Average Molecular Weight of Collagen Peptides> Regarding Samples 4 to 6, it was investigated to what extent the collagen raw material was converted into collagen peptides with a lower molecular weight through the second step. Specifically, regarding Samples 4 to 6, the weight-average molecular weight of the collagen peptides contained in the above peptide composition after fermentation for 6 hours in the second step was determined according to the measurement method described above. The results are shown in Table 5.

[0108]

Table 5

[0109] <Discussion> According to Table 5, it is understood that the peptide compositions of Samples 4 to 6 had their collagen raw materials reduced in molecular weight through the second step.

[0110] 〔Fifth Test〕 <Weight-Average Molecular Weight of Collagen Peptides> Regarding Samples 7 to 9, it was investigated to what extent the collagen raw material was converted into low-molecular-weight collagen peptides by undergoing the second step. Specifically, regarding Samples 7 to 9, the weight-average molecular weight of the collagen peptides contained in the above peptide composition after fermentation for 8 hours in the second step was determined according to the measurement method described above. The results are shown in Table 6.

[0111]

Table 6

[0112] <Discussion> According to Table 6, it is understood that the peptide compositions of Samples 7 to 9 had their collagen raw materials reduced in molecular weight by undergoing the second step.

[0113] 〔Sixth Test〕 <Weight-Average Molecular Weight of Collagen Peptides> Regarding Sample 10, it was investigated to what extent the collagen raw material was converted into low-molecular-weight collagen peptides by undergoing the second step. Specifically, regarding Sample 10, the weight-average molecular weight of the collagen peptides contained in the above peptide composition after fermentation for 6 hours in the second step was determined according to the measurement method described above. The results are shown in Table 7.

[0114]

Table 7

[0115] <Discussion> According to Table 7, it is understood that the peptide composition of Sample 10 had its collagen raw material reduced in molecular weight by undergoing the second step.

[0116] 〔Seventh Test〕 <Weight-Average Molecular Weight of Collagen Peptides> Regarding Sample 11, it was investigated to what extent the collagen raw material was converted into low-molecular-weight collagen peptides through the second step. Specifically, regarding Sample 11, the weight-average molecular weight of the collagen peptides contained in the above peptide composition after fermentation for 24 hours in the second step was determined according to the measurement method described above. The results are shown in Table 8.

[0117]

Table 8

[0118] <Discussion> According to Table 8, it is understood that the peptide composition of Sample 11 had its collagen raw material reduced in molecular weight through the second step.

[0119] 〔Test 8〕 <Weight-average Molecular Weight of Collagen Peptides> Regarding Sample 12, it was investigated to what extent the collagen raw material was converted into low-molecular-weight collagen peptides through the second step. Specifically, regarding Sample 12, the weight-average molecular weight of the collagen peptides contained in the above peptide composition after fermentation for 6 hours in the second step was determined according to the measurement method described above. The results are shown in Table 9.

[0120]

Table 9

[0121] <Discussion> According to Table 9, it is understood that the peptide composition of Sample 12 had its collagen raw material reduced in molecular weight through the second step.

[0122] 〔Test 9〕 <Taste Sensory Test> Regarding Samples 1 to 6 and Samples 101 to 103, after adjusting the concentration of the collagen peptide to 10% by mass using RO water, 20 mL of each was prepared. Further, for Sample 10, a solution (20 mL) obtained by dissolving 2 g of the above dry powder in 18 mL of RO water was prepared. For each of the above samples, a taste sensory test regarding how much the taste peculiar to collagen was felt was carried out by 5 evaluators. In the above taste sensory test, as shown in Table 10, scores from 1 to 4 were given to each sample. It can be evaluated that the higher the above score, the more the taste peculiar to collagen is reduced. The results are shown in Table 11.

[0123]

Table 10

[0124]

Table 11

[0125] <Consideration> According to Table 2, the peptide compositions of Samples 1 to 6 and Sample 10 were evaluated to have a reduced taste peculiar to collagen compared to the peptide compositions of Samples 101 to 103.

[0126] 〔Summary〕 From the above, it is suggested that the peptide compositions of Samples 1 to 12 contain low-molecular-weight collagen peptides and can reduce the collagen odor and the taste peculiar to collagen. In particular, based on the results regarding Samples 4, 5, and 10 in the above Second Test, it is suggested that the peptide compositions of Samples 1 to 12 can reduce the collagen odor and the taste peculiar to collagen by containing at least three types of the first compounds. Thus, the peptide compositions of Samples 1 to 12 are considered to be particularly suitable for food uses or cosmetic uses, etc.

[0127] The embodiments and examples disclosed herein should be considered illustrative in all respects and not restrictive. The scope of the present invention is shown not by the above description but by the claims, and it is intended that all modifications within the meaning and scope equivalent to the claims be included.

Claims

1. A peptide composition produced by fermenting a collagen raw material with koji, wherein the fungal species of koji mold contained in the koji is at least one selected from the group consisting of Aspergillus sojae, Aspergillus oryzae, and Aspergillus luchuensis, the collagen raw material is at least one selected from the group consisting of the following Group 1 to Group 5, collagen extracted from at least one selected from the group, gelatin obtained by treating the collagen, and at least any one of gelatin degradation products obtained by hydrolyzing the gelatin, the peptide composition contains collagen peptides and at least three first compounds selected from the group consisting of isovaleraldehyde, 1-octen-3-ol, phenylacetaldehyde, and methional, the peptide composition contains 0.4 ppm or more of the first compound. Group 1: The group consisting of cowhide, skin, bone, cartilage, and tendon Group 2: The group consisting of pigskin, skin, bone, cartilage, and tendon Group 3: The group consisting of sheepskin, skin, bone, cartilage, and tendon Group 4: The group consisting of chicken skin, skin, bone, cartilage, and tendon Group 5: The group consisting of ostrich skin, skin, bone, cartilage, and tendon

2. The peptide composition according to claim 1, wherein the peptide composition contains four of the first compounds.

3. The peptide composition according to claim 1 or claim 2, wherein the collagen peptide has a weight average molecular weight of 20,000 or less.

4. The peptide composition according to any one of claims 1 to 3, wherein the peptide composition is a food or a cosmetic.

5. A method for producing a peptide composition produced by fermenting a collagen raw material according to any one of claims 1 to 4 with koji, comprising: a step of preparing the koji and the collagen raw material; and a step of obtaining a peptide composition by fermenting the collagen raw material with the koji, in the step of obtaining the peptide composition, the content of the collagen raw material in the dispersion containing the collagen raw material and the koji is 20 to 75% by mass, in the step of obtaining the peptide composition, the time condition and temperature condition for fermenting the collagen raw material with the koji are 1 to 24 hours and 10 to 65 °C, respectively. The method for producing a peptide composition, wherein the collagen raw material is at least one selected from the group consisting of the following Group 1 to Group 5, collagen extracted from at least one selected from the group, gelatin obtained by treating the collagen, and at least any one of gelatin hydrolysates obtained by hydrolyzing the gelatin. Group 1: The group consisting of cowhide, skin, bone, cartilage, and tendon Group 2: The group consisting of pigskin, skin, bone, cartilage, and tendon Group 3: The group consisting of sheepskin, skin, bone, cartilage, and tendon Group 4: The group consisting of chicken skin, skin, bone, cartilage, and tendon Group 5: The group consisting of ostrich skin, skin, bone, cartilage, and tendon

6. The method for producing a peptide composition according to claim 5, wherein the fungal species of the Aspergillus is a fungal species belonging to the genus Aspergillus.

7. The method for producing a peptide composition according to claim 5 or claim 6, wherein the fungal species of the Aspergillus is at least one selected from the group consisting of Aspergillus sojae, Aspergillus oryzae, and Aspergillus luchuensis.

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