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Collagen peptide composition and food or beverage containing the same

A technology of composition and collagen peptide, applied in the field of collagen peptide composition, can solve problems such as difficult to use, no record, no record of ratio, etc.

Active Publication Date: 2009-10-28
MEIJI CO LTD
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In this publication, an in vivo dynamic test of a tripeptide labeled with a radioactive isotope was carried out, but it is unclear whether the main body of the radioactivity distributed in plasma and in various tissues is the unchanged tripeptide, dipeptide, or free amino acid.
Moreover, since the enzyme used to prepare the tripeptide is also collagenase, it is actually difficult to use it in food in terms of safety
Moreover, the peptides constituting the tripeptide mixture contained in the collagen-promoting active agent disclosed in this publication are all peptides whose N-terminal amino acid is glycine (Gly-X-Y), and the ratio of glycine in the N-terminal amino acid of the tripeptide in the mixture is adjusted. Proportion not recorded
[0008] Furthermore, in Patent Document 8, it is described that a collagen peptide composition containing a large amount of peptides with a molecular weight of 400 to 3,000 exhibits an excellent feeling of use and permeability to the skin when blended into cosmetics and pharmaceuticals for the skin. There is no description of the evaluation of migration in the blood, the adjustment of the proportion of glycine in the N-terminal amino acid of the peptide in the composition

Method used

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  • Collagen peptide composition and food or beverage containing the same

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0062] (Example 1) Preparation of the collagen peptide composition of the present invention

[0063] 1.0 kg of acid-treated fish scale gelatin (manufactured by Nitta Gelatin Inc.) was dissolved in 2.0 kg of warm water at 75°C. 5.5 g of subtilisin (manufactured by Wako Pure Chemical Industries, Ltd.) was added as a protease to the obtained gelatin solution, the pH of the solution was adjusted to 8, and the enzyme reaction was performed at 50° C. for 4 hours. After the reaction, the solution was heated to above 90° C. to inactivate the enzyme, 20 g of micropowder activated carbon was added, finely filtered, and then spray-dried to obtain a powdered collagen peptide composition.

[0064] The average molecular weight of the obtained collagen peptide composition was measured by gel filtration high-performance liquid chromatography (GF-HPLC) under the following conditions, and data processing was performed by MultistationGPC-8020 software Ver4.0 (manufactured by TOSOH). The average...

Embodiment 2

[0071] (Example 2) Comparison test of migration into blood (absorption test (1))

[0072] The blood migration of the collagen peptide composition (average molecular weight: 2000) of the present invention prepared in Example 1 was compared with that of a commercially available collagen peptide composition. As a commercially available collagen peptide composition, fish skin collagen peptide A (manufactured by Nippi, Inc., trade name Nip piPeptide FCP, average molecular weight 5000), fish skin collagen peptide B (manufactured by MARUHA, trade name Fish Collagen WP, average molecular weight 3000) were used. ), fish scale collagen peptide C (manufactured by RABJ, trade name Marine Collagen MS5), pigskin collagen peptide D (manufactured by Nitta Gelatin Inc., trade name Super Collagen PeptideSCP5000, average molecular weight 5000).

[0073] The test was performed based on the report of Iwai et al. (Agric. Food Chem., 2005, Vol. 53, No. 16, p6531-6536). A washout period of more than...

Embodiment 3

[0093] (Example 3) Peptide composition in blood after oral intake of collagen peptide composition

[0094] Among the plasma samples collected in Example 2, the plasma samples after ingestion of the collagen peptide composition of the present invention, commercially available collagen peptide A (derived from fish skin) and collagen peptide D (derived from pig skin) were used as samples. After the ethanol supernatant of each sample was dried to a solid by a vacuum centrifugal dryer, 200 μL of 30% acetonitrile containing 0.1% trifluoroacetic acid was added to dissolve, and fractionation was carried out by HPLC under the following conditions.

[0095] (analysis conditions)

[0096] Column: Superdex peptide HR10 / 30 (Amersham Pharmacia, Piscataway, NJ, USA)

[0097] Eluent: 30% acetonitrile (with 0.1% trifluoroacetic acid)

[0098] Flow rate: 0.5mL / min

[0099] Detection wavelength: 230nm

[0100] Column temperature: room temperature

[0101] Analysis time: 60 minutes

[0102]...

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Abstract

The object is to discover a collagen peptide composed of an oligopeptide having a higher ability of being transported into the blood compared to a conventional collagen peptide, and to provide a food or beverage having the collagen peptide blended therein. Disclosed is a collagen peptide composition produced by digesting a collagen or gelatin with a protease. The collagen peptide composition comprises 70 to 100 wt% of a peptide having a molecular weight of 500 to 3000 inclusive, less than 10 wt% of a peptide having a molecular weight of less than 500, and less than 20 wt% of a peptide having amolecular weight exceeding 3000, wherein the ratio of glycine in the N-terminal amino acid residues of the peptides contained in the composition is 33 to 65 mol% inclusive.

Description

technical field [0001] The present invention relates to a collagen peptide composition, and more specifically, to a collagen peptide composition composed of an oligopeptide excellent in blood migration, and a food or drink containing the collagen peptide composition. Background technique [0002] Collagen is one of the proteins constituting the dermis, ligaments, tendons, bones, cartilage, etc., and is a main component of the extracellular matrix of multicellular animals. Collagen exists in skin, blood vessels, internal organs, bone tissue, etc., and accounts for about 30% of the proteins that make up the body. 70% of the dermis in the skin is composed of collagen, and the fascia (fascia) that wraps various muscles is also composed of collagen. [0003] Collagen aggregates three polypeptide chains (α chains) with a molecular weight of about 100,000 having a repeating structure of Gly-X-Y (X and Y are amino acids other than Gly), forming a helical structure. Collagen has am...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/78A23L1/30A23L1/305A23L2/52A61K35/60A61K38/00A61K38/17A61P3/02A61P17/16A61P19/08A61P19/10A61P43/00C07K2/00A23L29/281
CPCC07K14/78A61K38/014A23V2002/00A23L2/52A23L1/05625A23L1/3053A23J3/06A23J3/341A23L29/284A23L33/18A61P1/04A61P17/00A61P17/02A61P17/04A61P17/14A61P17/16A61P19/02A61P19/08A61P19/10A61P29/00A61P3/02A61P37/08A61P43/00A61P9/10A61P9/12A23V2200/316A23V2250/5422A23L29/281A61K35/60
Inventor 松本均大原浩树中岛孝谦杉原富人高崎一
Owner MEIJI CO LTD
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