JP2010195701A - Living body collagen synthesis promoter - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To provide a living body collagen synthesis promotor which is inexpensive, safe and highly effective. <P>SOLUTION: This living body collagen synthesis promotor has a mixture of a glycerophospholipid and collagen or a hydrolysate thereof as active components, where the glycerophospholipid is preferably one or two or more selected from the group consisting of phosphatidylcholine, lysophosphatidylcholine, phosphatidylserine, lysophosphatidylserine, phosphatidylethanolamine, lysophosphatidylethanolamine, phosphatidylinositol, lysophosphatidylinositol, phosphatidic acid, lysophosphatidic acid, phosphatidylglycerol, and lysophosphatidylglycerol. <P>COPYRIGHT: (C)2010,JPO&INPIT

Description

  The present invention relates to a biological collagen synthesis promoter and a food or drink containing the same.

  Collagen is a fibrous protein present in most tissues such as skin, blood vessels, tendons, and teeth, and occupies about 30% of the total protein constituting the body. 40% of the total amount of collagen is present in the skin, 20% is present in bones and cartilage, and is widely distributed throughout the body including blood vessels and internal organs. Known collagen-producing cells include fibroblasts present in the skin, chondrocytes present in cartilage, and osteoblasts that form bone. Collagen is secreted from these cells, and then sterically fills the space between cells to form an intercellular matrix together with other glycoproteins, which helps to maintain cell and organ morphology. In cartilage and bone, it plays an important role as a component of matrix protein.

  By the way, skin aging (wrinkles, sagging, etc.) and rough skin are major cosmetic concerns. There are various causes of skin aging, rough skin, etc., but the underlying phenomenon is caused by a decrease in collagen production activity of dermal fibroblasts, a decrease in hyaluronic acid synthesis activity, an increase in collagenase activity due to UV rays, UV rays and the environment. It is considered to be deterioration, degeneration, reduction, etc. of skin components due to damage caused by active oxygen generated. If the skin's moisturizing function decreases due to external factors such as the environment, meals, luxury items, etc., and aging, the skin becomes dry and loses its elasticity, causing dry skin and wrinkles. It is thought to lead to the onset of atopic dermatitis.

  The skin is composed of three tissues in order from the surface: epidermis, dermis, and subcutaneous tissue. It is said that the epidermis is mainly related to the moisture and smoothness of the skin. The epidermis is divided into four layers, the basal layer, spiny layer, granule layer, and stratum corneum, from the lowest part, and plays a role of a barrier function to prevent irritation from the outside world, invasion of foreign substances, bacteria, etc. . Cells in the stratum corneum are created in the basal layer at the bottom of the epidermis and accumulate and accumulate in the stratum corneum at the top of the skin, repeating cell division and proliferation over 4 weeks, with the disappearance of intracellular nuclei. And it is known that after two weeks it will become a flake and fall off. This series of cycles is called turnover.

  On the other hand, the dermis is under the epidermis, and collagen, elastic fibers (elastin), etc. are present in a mesh shape, and have a function mainly for maintaining the elasticity and the elasticity of the skin. In addition, collagen and hyaluronic acid are produced in fibroblasts present in the dermis.

  As described above, collagen is most abundant in the skin, but changes in quality and quantity due to active oxygen generated by ultraviolet rays, ionizing radiation, ozone and the like. Moreover, since synthesis by fibroblasts decreases with aging, the amount of degradation exceeds the amount of synthesis, and as a result, wrinkles and blemishes occur and so-called skin aging occurs. Skin aging occurs due to degradation of the stratum corneum and a decrease in the amount of collagen and elastin, which are the extracellular matrix of the dermis, and degradation of the collagen fiber bundle.

  Therefore, many attempts have been made to increase the amount of collagen in the skin by orally ingesting collagen or a hydrolyzate thereof (Patent Documents 1 and 2). In fact, a large number of mainly cosmetic materials including collagen are sold. However, although it is certain that amino acids and peptides that are the raw materials for collagen can be replenished by ingesting collagen, whether or not the collagen content of skin, bone, or cartilage actually increases is weak. For that reason, it is not well-proven scientifically.

  On the other hand, glycerophospholipid exists specifically in a membrane-like structure site of a cell and is known as a main component of a biological membrane together with a protein. It is contained in many parts such as brain, nerves, internal organs, blood, eggs, and seeds, and plays many functions for life support.

  In addition, the functionality of various phospholipids has recently become apparent. For example, phosphatidylcholine (PC), which is a main component of lecithin, has an action of obtaining a whitening effect (Patent Documents 3 and 4), an action of suppressing collagen production induced by inflammatory stimulation (Non-Patent Document 1), and damaged skin. Has been reported to regulate the recovery by inhibiting the contraction of the hair (Non-patent Document 2), and the action of activating protein kinase C (PKC) to phosphatidic acid (PA) to promote hair regeneration (Patent Document 5) An action that improves the membrane fluidity of tumor cells and changes multidrug resistance (Patent Document 6), a cell proliferation action for lysophosphatidic acid (LPA), and a cell growth inhibitory activity for cyclic lysophosphatidic acid (cPA) ( Non-patent document 3) has been reported. In addition, phosphatidylserine (PS) has a brain function improving effect (Non-patent document 4) and neurite outgrowth activity (Non-patent document 5), and phosphatidylethanolamine (PE) has a neurotrophic effect (Non-patent document 6). Has been reported.

  However, it has never been known that the ingestion of glycerophospholipids enhances the action of promoting collagen synthesis by ingesting collagen or a hydrolyzate thereof.

Japanese Patent Laid-Open No. 7-278012 Japanese Patent Laid-Open No. 2001-131084 JP 2004-59496 A JP 2005-272444 A JP 2006-76967 A JP 2006-143744 A Japanese Patent Application No. 2007-221384

J. et al. Lab. Clin. Med. , 139 (2002), 202-210 J. et al. Invest. Surg. , 17 (2004), 15-22 Protein Nucleic Acid Enzyme, Vol. 44, no. 8 (1999), 1118-1125 FOOD Style 21, Vol. 6, no. 11 (2002), 108-116 Japan Agricultural Chemistry 2004 Conference, 3A19p23, “Effects of Egg Yolk-Derived Phosphatidylserine on Neurite Outgrowth” J. et al. Lipid Research, 47 (2006), 1434-1443.

  An object of the present invention is to provide a bio-collagen synthesis promoter that can dramatically enhance the bio-collagen synthesis action by ingesting collagen.

  As a result of intensive studies to solve the above-mentioned problems, the present inventors have unexpectedly ingested a mixture of glycerophospholipid and collagen or a hydrolyzate thereof, thereby promoting the synthesis of biological collagen. It has been found that the collagen content in each tissue increases. Further, the present inventors have found that the mixture promotes skin metabolism, promotes epidermis turnover, promotes collagen production in the dermis, and functions effectively as a skin activator, thereby completing the present invention.

  That is, the first of the present invention is a biocollagen synthesis promoter characterized by comprising a mixture of glycerophospholipid and collagen or a hydrolyzate thereof as an active ingredient. Preferably, glycerophospholipid is Phosphatidylcholine, lysophosphatidylcholine, phosphatidylserine, lysophosphatidylserine, phosphatidylethanolamine, lysophosphatidylethanolamine, phosphatidylinositol, lysophosphatidylinositol, phosphatidic acid, lysophosphatidic acid, phosphatidylglycerol, and lysophosphatidylglycerol It is a biological collagen synthesis promoter that is two or more.

  The second aspect of the present invention is a skin activator characterized in that it contains the above-described biocollagen synthesis promoter.

  The third aspect of the present invention is a food or drink characterized by containing the above-described biocollagen synthesis promoter.

  According to the present invention, it is possible to produce a large amount and a low cost of a biological collagen synthesis promoter or skin activator that is inexpensive and safe and has no side effects. Moreover, the food / beverage products containing these can be provided.

Hereinafter, the present invention will be described in detail.
The biological collagen synthesis promoter of the present invention contains glycerophospholipid alone or in combination of two or more as an essential component. As glycerophospholipids, the presence of ester type (monoacyl type, diacyl type), ether type (alkyl type, alkylacyl type, alkenylacyl type, dialkyl type) and phosphono type (CP compound) are known.

  The glycerophospholipid used in the present invention is preferably an ester glycerophospholipid, and more specifically, phosphatidylcholine, lysophosphatidylcholine, phosphatidylserine, lysophosphatidylserine, phosphatidylethanolamine, lysophosphatidylethanolamine, phosphatidylinositol, lysophosphatidylinositol, phosphatidine Examples include acid, lysophosphatidic acid, phosphatidylglycerol, and lysophosphatidylglycerol. Among these, phosphatidylcholine, lysophosphatidylcholine, phosphatidic acid, and lysophosphatidic acid are highly effective.

  At least one of the fatty acids constituting the ester-type glycerophospholipid used in the present invention is preferably an unsaturated fatty acid, and the unsaturated fatty acid has an unsaturation degree of 1 or more and a carbon number of 4 or more. More desirable. More specifically, butenoic acid (C4: 1, such as crotonic acid and isocrotonic acid), pentenoic acid (C5: 1), hexenoic acid (C6: 1), heptenoic acid (C7: 1), octenoic acid (C8: 1), nonenoic acid (C9: 1), decenoic acid (C10: 1), undecenoic acid (C11: 1), dodecenoic acid (C12: 1 such as lauroleic acid), tridecenoic acid (C13: 1), tetradecenoic acid (C14: 1, such as myristoleic acid, myristaleic acid, etc.), pentadecenoic acid (C15: 1), hexadecenoic acid (C16: 1, such as palmitoleic acid, palmitelaidic acid, etc.), heptadecenoic acid (C17: 1) , Octadecenoic acid (C18: 1, such as petroselinic acid, petroceridic acid, oleic acid, elaidic acid, vaccenic acid, etc.), nonadecenoic acid C19: 1), eicosenoic acid (C20: 1, such as gadoleic acid, gondrenic acid, etc.), docosenoic acid (C22: 1, such as erucic acid, brassicic acid, cetreic acid, etc.), tetracosenoic acid (C24: 1, such as nervonic acid) Hexacosenoic acid (C26: 1), octacosenoic acid (C28: 1), triacontenoic acid (C30: 1), pentadienoic acid (C5: 2), hexadienoic acid (C6: 2, such as sorbic acid), peptadiene Acid (C7: 2), octadienoic acid (C8: 2), nonadienoic acid (C9: 2), decadienoic acid (C10: 2), undecadienoic acid (C11: 2), dodecadienoic acid (C12: 2), tridecadienoic acid ( C13: 2), tetradecadienoic acid (C14: 2), pentadecadienoic acid (C15: 2), hexadecadie Acid (C16: 2), heptadecadienoic acid (C17: 2), octadecadienoic acid (C18: 2, such as linoleic acid, linoelaidic acid, etc.), eicosadienoic acid (C20: 2), docosadienoic acid (C22: 2), Tetracosadenoic acid (C24: 2), Hexacosadienoic acid (C26: 2), Octacosadienoic acid (C28: 2), Triacatadienoic acid (C30: 2), Hexadecatrienoic acid (C16: 3), Octadecatrienoic acid (C18) : 3, for example, α-linolenic acid, γ-linolenic acid, etc.), eicosatrienoic acid (C20: 3, for example, dihomo-γ-linolenic acid, mead acid, etc.), docosatrienoic acid (C22: 3), tetracosatriene Acid (C24: 3), Hexacosatrienoic acid (C26: 3), Octacosatrienoic acid (C28: 3), Triaco Antatrienoic acid (C30: 3), octadecatetraenoic acid (C18: 4, such as stearidonic acid), eicosatetraenoic acid (C20: 4, such as arachidonic acid), docosatetraenoic acid (C22: 4, such as Adrenoic acid, etc.), tetracosatetraenoic acid (C24: 4), hexacosatetraenoic acid (C26: 4), octacosatetraenoic acid (C28: 4), triacontatetraenoic acid (C30: 4), Eicosapentaenoic acid (C20: 5), docosapentaenoic acid (C22: 5, such as crupadnonic acid), tetracosapentaenoic acid (C24: 5), docosahexaenoic acid (C22: 6), tetracosahexaenoic acid (C24: 6, for example, nisic acid).

  In addition to the linear unsaturated fatty acids shown above, lumenic acid (C18: 2), calendic acid (C18: 3), jacaric acid (C18: 3), eleostearic acid (C18: 3), catalpinic acid ( Conjugated fatty acids such as C18: 3), punicic acid (C18: 3), lumenic acid (C18: 3), ricinoleic acid (C18: 1), ricinaleic acid (C18: 1), dimorphecolic acid (C18: 2) Hydroxyl unsaturated fatty acids such as), epoxy fatty acids such as bemolic acid (C18: 1), furanoid fatty acids such as urofuranic acid, high molecular weight branched unsaturated fatty acids such as mycolic acid, and other methoxy unsaturated fatty acids. The structure and type are not particularly limited as long as the degree of unsaturation is 1 or more and the number of carbon atoms is 4 or more.

  The glycerophospholipid as described above can be obtained by extracting with water or an organic solvent from a material containing glycerophospholipid. Examples include glycerophospholipids derived from plant materials such as soybeans and rapeseed, derived from animal materials such as egg yolk, fungi and bacteria, and glycerophospholipids that have been purified, chemically treated, enzymatically treated such as phospholipase, etc. Alternatively, a chemically synthesized product or an enzyme synthesized product can be used.

  As an example of the enzyme treatment, there is a method of reacting natural lecithin with an enzyme. Examples of natural lecithin include lecithin derived from soy, rapeseed, fish and other marine products, egg yolk, and the like. As the enzyme, at least one selected from the group consisting of lipase, phospholipase D, phospholipase A1, and phospholipase A2 is preferably used. The enzyme reaction conditions can be appropriately determined by those skilled in the art depending on the enzyme used.

  The organic solvent used here includes hydrocarbons such as hexane, heptane, octane, cyclohexane, ethanol, acetonitrile, acetate ester, dimethyl sulfoxide (DMSO), dioxane, glycol, petroleum ether, THF, acetone, Examples include methylene chloride and chloroform. These solvents can be used alone or in admixture of two or more for extraction, but ethanol, acetone, heptane and petroleum ether are particularly preferable.

  Although there is no restriction | limiting in particular in the quantity of the solvent used for extraction, It is preferable to use 2-10 times amount with respect to the weight of the raw material containing glycerophospholipid. When the amount is twice or less, the operability is poor, and when the amount is 10 times or more, the work efficiency is poor.

  The extraction can also be performed multiple times using one or more solvents. When performing several times, you may extract from the raw material containing glycerophospholipid, and you may further extract the extraction fraction obtained from the raw material containing glycerophospholipid. Moreover, it can carry out combining them.

  The temperature during the extraction operation is not particularly limited but is preferably 10 to 60 ° C. Extraction efficiency is poor at 10 ° C. or lower, and impurities other than glycerophospholipid are easily extracted at 60 ° C. or higher, resulting in a decrease in purity. Although there is no restriction | limiting in particular also in extraction time, About 1 hour-2 days are preferable. The amount of extraction is less than 1 hour, and the work efficiency is low after 2 days. Extraction can be performed while standing, but the extraction efficiency can be increased by stirring or shaking.

  The glycerophospholipid obtained by the method as described above may be used as it is as a blending component of the biological collagen synthesis promoter of the present invention, and is concentrated, decolored, desalted, as long as the effects of the present invention are not impaired. You may use what gave processing, such as distribution and pulverization. For example, the solvent may be removed by concentration under reduced pressure to increase the solid content, or the colored component may be removed by activated carbon treatment, and water-soluble by liquid / liquid distribution between the aqueous layer and the organic solvent layer. What removed the component may be used. Moreover, you may refine | purify by various chromatography of a normal phase type | system | group or a reverse phase system. Further, those extracts or processed products may be powdered by adding excipients such as dextrin and lactose.

  Examples of collagen used in the present invention include those extracted from connective tissues such as skin, scales, bones and tendons of animals such as cows, pigs, chickens and fish, or gelatin which is a heat-denatured product of collagen. Among them, a solubilized collagen produced by hydrolyzing the telopeptide portion with an enzyme or alkali to remove the cross-link and solubilizing is preferable from the viewpoint of handling.

  The collagen hydrolyzate used in the present invention is a product obtained by hydrolyzing collagen or gelatin. Among them, a peptide having a molecular weight of 400 or less represented by Gly-XY (X and Y are amino acids) is preferable because of its high absorbability. Collagen hydrolysis may be performed by a hydrolase method, or may be performed by acid or alkali hydrolysis. As the hydrolase used for the enzymatic degradation, for example, collagenase enzyme may be derived from bacteria such as Clostridium histoticum and Streptomyces parvulus, actinomycetes or fungi. It is also effective to ferment with these microorganisms. Furthermore, it may be a mixture of other proteolytic enzymes. Preferably, it produces a peptide represented by Gly-XY (where X and Y are amino acids).

  Collagen hydrolysates are already commercially available. Such hydrolysis is carried out by hydrolysis with an enzyme or the like to a molecular weight of about several hundred to several thousand. There is also a product obtained by hydrolyzing gelatin that has been subjected to high-temperature water treatment. Powder and granule products are spray dried.

  The biological collagen synthesis promoter of the present invention comprises a mixture of the above-described glycerophospholipid and collagen or a hydrolyzate thereof as an active ingredient, and the mixing ratio of glycerophospholipid and collagen or a hydrolyzate thereof in this mixture is As long as the expected effect is obtained, there is no limitation, but 20: 1 to 1:20 is preferable, and 1: 1 to 1:20 is particularly preferable.

  The biological collagen synthesis promoter of the present invention may be produced by appropriately mixing glycerophospholipid and collagen or a hydrolyzate thereof in powder form, or may be produced by appropriately mixing respective aqueous solutions. .

  Since the biological collagen synthesis promoter of the present invention exhibits an excellent biological collagen synthesis promoting action, by taking it orally, alleviating symptoms associated with bone and joint diseases, tendon damage healing promoting action, bone formation promoting action, A cosmetic effect, a skin damage and a healing promotion effect of wounds will be seen. Therefore, since the biological collagen synthesis promoter of the present invention has a skin activating effect, it can also be used as a skin activating agent.

  The intake of the biological collagen synthesis promoter or skin activator of the present invention is not particularly limited as long as it is effective, but is preferably 0.1 to 10 g / day. In general, if the amount is less than 0.1 g / day, the effect is not sufficiently obtained, and if it is more than 10 g / day, it is economically disadvantageous. Of course, it can be changed according to the age, weight, symptom, administration period, course of treatment, etc. of the ingested person. The daily dose can be taken in several divided doses.

  In addition to the mixture of the glycerophospholipid and collagen or a hydrolyzate thereof, the skin activator of the present invention may contain components with reported skin beautifying effects such as hyaluronic acid, ceramide, and elastin. it can.

  Further, the biocollagen synthesis promoter of the present invention can be in an orally ingestible form, for example, a powder, powder, granule, tablet, capsule or the like, and can be blended in foods such as beverages. It can also be a food or drink.

  The intake amount of the food or drink of the present invention is not particularly limited, but is usually an amount such that the amount of the biological collagen synthesis promoter is 0.1 to 10 g / day. Furthermore, there is no problem even if it is blended into an ointment or cosmetic as an external preparation.

  EXAMPLES The present invention will be specifically described below with reference to examples, but the present invention is not limited to these examples.

Examples 1 and 2
A mixed solution of heptane and acetone (3: 1 (volume ratio)) was added to 200 g of egg yolk lecithin PL-30S (manufactured by QP Corporation) to dissolve it, and the total amount was made 2 L (to make an egg yolk lecithin solution). Next, 740 mL of an enzyme solution (pH = 8.0) containing 20,000 U of phospholipase D (manufactured by Meito Sangyo Co., Ltd.) was prepared. This enzyme solution was added to the egg yolk lecithin solution and allowed to react for 20 hours at 30 ° C. with stirring. Subsequently, after the liquid separation, the organic solvent layer containing phosphatidic acid (sometimes referred to as PA) was concentrated under reduced pressure (about 3-fold concentration) with an evaporator. After concentration, 5 times the volume of acetone of the concentrate was added, and PA obtained as an insoluble material was dried under reduced pressure to obtain 54 g of a PA crystallized product. The purity was 95%.

  Next, 10 g of the obtained PA crystallized product is dispersed in a buffer solution (0.1 M Tris buffer solution, 50 mM calcium chloride, pH 8) containing 15,000 U phospholipase A2 (PLA2 Nagase: manufactured by Nagase ChemteX Corporation). , And was prepared to be 100 mL. Subsequently, the enzyme reaction was carried out at 30 ° C. for 20 hours with stirring. After completion of the reaction, 1 L of ethanol was added to the reaction solution to extract lysophosphatidic acid (sometimes referred to as LPA), and an LPA extract was obtained by vacuum filtration. This LPA extract was concentrated under reduced pressure (about 3-fold concentration) with an evaporator. After concentration, 5 times the volume of acetone of the concentrate was added, and LPA obtained as an insoluble material was collected by filtration and dried under reduced pressure to obtain 5.5 g of an LPA crystallized product.

  On the other hand, collagen tripeptide HACP-01 (manufactured by Zerais Co., Ltd.) was prepared, and the PA obtained above was mixed at a mass ratio of 9: 1 to obtain the collagen synthesis promoter 1 of the present invention. (Example 1). Similarly, collagen tripeptide HACP-01 (manufactured by Zerais Co., Ltd.) and LPA obtained above were mixed at a mass ratio of 9: 1 to obtain collagen synthesis promoter 2 of the present invention ( Example 2).

Test example (evaluation of skin collagen synthesis promoting action and skin activation action; animal experiment)
Wistar rats (male, 4 weeks old, 5 animals / group) were bred for 3 weeks on a diet containing 6% protein to obtain pseudo-aging model rats. The biological collagen synthesis promoter 1 of Example 1 and the biological collagen synthesis promoter 2 of Example 2 are suspended in tap water so as to be 1 mg / ml, and 1 mL is once a day for 100 g body weight of the pseudo-aged model rat. Orally for 5 consecutive weeks (equivalent to 10 mg / day / kg-BW). Similarly, collagen tripeptide HACP-01 (Comparative Example 1) is suspended in tap water so as to be 0.9 mg / ml, and 1 mL is once a day for 100 g body weight of a pseudo-aged model rat once a day for 5 weeks. Each was ingested continuously (equivalent to 9 mg / day / kg-BW). In addition, the group which orally ingested 1 mL of tap water once a day for 5 weeks continuously with respect to 100 g of body weight of a pseudo-aging model rat was made into the control example.

  The turnover of the epidermis was performed by the dansyl chloride method. Two weeks after the start of administration, the back of the rat was shaved and 5 μL of a 2% dansyl chloride / EtOH solution was applied to the back of the rat (the part that cannot be touched by the rat itself). After application, the fluorescence was observed visually under UV irradiation from the 24th hour, and the disappearance date of the fluorescence was observed. The results are shown in Table 1.

As is clear from Table 1, it can be seen that the biological collagen synthesis promoter of the present invention enhanced the turnover of the epidermis compared to the case of the collagen tripeptide alone of Comparative Example 1.

  After the administration was completed, the hair on the back of the rat was removed, and the skin was excised into a 2 × 2.5 cm rectangle together with the subcutaneous tissue. After weighing, 10 mL of distilled water cooled with ice was added to the extracted skin and homogenized sufficiently, and the precipitate was collected by centrifugation (7000 rpm × 20 min). 10 mL of ice-cooled 0.1N sodium hydroxide was added to the precipitate, shaken overnight under refrigeration (6 ° C.), the precipitate was recovered by centrifugation, and the same operation was performed again. The precipitate recovered by centrifugation is washed with ice-cooled distilled water, and 15 mL of ice-cooled 0.5M acetic acid is added to the precipitate recovered again after centrifugation, followed by collagen extraction overnight under refrigeration (6 ° C), and centrifugation. Extraction supernatant was obtained by separation. Soluble collagen in the extracted solution was quantified using Sircol Collagen Assay Kit (Funakoshi). The results are shown in Table 2.

As is apparent from Table 2, it was found that the biological collagen synthesis promoter of the present invention increased the skin weight and the amount of skin soluble collagen compared to the case of the collagen tripeptide of Comparative Example 1 alone.

Claims (4)

  A biological collagen synthesis promoter comprising a mixture of glycerophospholipid and collagen or a hydrolyzate thereof as an active ingredient.   The glycerophospholipid is selected from the group consisting of phosphatidylcholine, lysophosphatidylcholine, phosphatidylserine, lysophosphatidylserine, phosphatidylethanolamine, lysophosphatidylethanolamine, phosphatidylinositol, lysophosphatidylinositol, phosphatidic acid, lysophosphatidic acid, phosphatidylglycerol, and lysophosphatidylglycerol. The biological collagen synthesis promoter according to claim 1, which is one or more of the above.   A skin activator comprising the biological collagen synthesis promoter according to claim 1 or 2.   A food / beverage product comprising the biological collagen synthesis promoter according to claim 1.