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    • 专利摘要:

    公开号:BR112013011894B1
    申请号:R112013011894
    申请日:2011-09-29
    公开日:2018-07-17
    发明作者:Giesen-Wiese Monika；Oesser Steffen；Hausmanns Stephan
    申请人:Gelita Ag；
    IPC主号:
    专利说明:

    (54) Title: COLLAGEN HYDROLYZE TO USE TO IMPROVE HEALTH OF HUMAN SKIN, HAIR AND / OR NAILS (51) Int.CI .: A61K 8/65; A61Q 19/08 (30) Unionist Priority: 11/15/2010 DE 10 2010 060 564.6 (73) Holder (s): GELITA AG (72) Inventor (s): STEPHAN HAUSMANNS; MONIKA GIESEN-WIESE; STEFFEN OESSER
    1/14
    Descriptive Report of the Invention Patent for COLLAGEN HYDROLYSIS TO USE TO IMPROVE HEALTH OF HUMAN SKIN, HAIR AND / OR NAILS.
    The present invention relates to a collagen hydrolyzate for use to improve the health of human skin, hair and / or nails.
    It has long been known that, through oral absorption of collagen hydrolyzate, advantageous effects can be obtained in relation to the health of the skin, but also of the human hair and / or nails (see, for example, Vivian Zague: A new view concerning the effects of collagen hydrolysate intake on skin properties in Arch. Dermatol. Res. 2008 (9) 479483). By improving the health of the skin in this context, any positive influence of the natural properties and functions of the skin is understood, and these properties and functions can be considered both as a result of aging, and also in addition to several negative environmental influences. The absorption of collagen hydrolyzate also has an advantage on the properties of the skin and / or nails.
    The aim of the invention is to further increase the positive effects of collagen hydrolyzate on the health of the skin, hair and / or nails and to propose a collagen hydrolyzate particularly effective for this use.
    This objective is solved in the case of the collagen hydrolyzate of the type mentioned above according to the invention by the fact that at least 90% by weight of the collagen hydrolyzate has a molecular weight of less than 3,500 Da and that the collagen hydrolyzate comprises at least at least four characteristic peptides with a molecular weight between 600 and 1,200 Da.
    Collagen hydrolysates contain peptides with different chain lengths or molecular weights, which are formed in the dissociation of collagen protein chains, in which the molecular weight distributions of these peptides, depending on the hydrolyzate production conditions, can be clearly distinguished. It has now surprisingly been shown that a collagen hydrolyzate with the above properties
    2/14 mentioned in different aspects acts in a particularly advantageous way on the health of the skin, that is, it shows markedly better results than the collagen hydrolysates used so far, which contain a substantially smaller portion of low molecular weight peptides and / or not contain the characteristic peptides.
    The molecular weight distribution of the collagen hydrolyzate, which serves as a basis for the limit value of at least 90% by weight, below 3,500 Da can be determined in a very precise and reproducible way, for example, by means of permeation chromatography in gel using a calibration standard for defined collagen fragments.
    Preferably, at least 45% by weight of the collagen hydrolyzate has a molecular weight of less than 1,500 Da, that is, a certain portion of the peptides of the collagen hydrolyzate is particularly short-chain. It has been shown that through these portions of particularly low molecular weight, which are contained only in substantially less quantity in the collagen hydrolyzates currently used, it is possible to obtain pronounced effects on the health of the skin.
    The average molecular weight (average weight M w ) of the collagen hydrolyzate used according to the invention, is typically in the range of about 1,700 to about 2,300 Da.
    The presence of the characteristic peptides of the collagen hydrolyzate, which interestingly contribute substantially to its effectiveness, can be determined, in particular, through MALDI mass spectroscopy, in which the characteristic peptides appear in the mass spectrum as peaks. Preferably, the at least four characteristic peptides in a molecular weight distribution determined by means of MALDI mass spectroscopy have an intensity at least double, more preferably an intensity at least quadruple compared to their medium.
    In a preferred embodiment of the invention, the collagen hydrolyzate comprises a peptide between 620 and 690 Da, a peptide between 790 and 860 Da, a peptide between 980 and 1,050 Da and a peptide
    3/14 between 1,175 and 1,245 Da. These peptides distinguish the collagen hydrolyzate according to the invention in a characteristic manner from known collagen hydrolysates.
    The collagen hydrolyzate can additionally also present characteristic peptides between 1,500 and 3,500 Da, which also represent a distinctive feature in relation to collagen hydrolyzates according to the state of the art.
    Preferably, the collagen hydrolyzate has a hydroxyproline portion of 12% by weight or more. The hydroxyproline amino acid formed through post-translational hydroxylation of proline occurs exclusively in collagens, so that a high portion of hydroxyproline in the collagen hydrolyzate represents a measure for the wide absence of other connective tissue proteins (for example, elastin and proteoglycans) , whose fragments, depending on the production process, may also be present in certain amounts in collagen hydrolysates.
    It is advantageous that the collagen hydrolyzate is produced through enzymatic hydrolysis of gelatin. Gelatine comprises denatured collagen and is obtained through various processes known to the specialist from connective tissue or from the bones of different animal species. In the context of the present invention, gelatine used as a starting material for collagen hydrolyzate is preferably obtained from mammalian skin, in particular pig skin or bovine connective tissue, but, where also, the use is not excluded wings gelatin.
    The enzymatic hydrolysis of gelatine is usually carried out using at least one endoprotease, and in the context of the invention it is preferable to use several endoproteases (that is, at least two different endoproteases) to thereby influence them in a corresponding way the amino acid profile of the resulting collagen hydrolyzate and increase the positive effect of collagen hydrolyzate on the health of the skin, hair and / or nails.
    According to a preferred embodiment of the invention, collagen hydrolyzate is produced through the successive action of
    4/14 at least two endoproteases with a different specificity, in particular, by at least two different metalloproteases and / or serinaproteases, that is, by proteases, which dissociate the amino acid sequence from the collagen molecules in each case before, respectively, after certain amino acids. Advantageously, in the case of metalloproteases and / or serine proteases, these are enzymes from the microorganisms Bacillus subtilis, Bacillus licheniformis, Bacillus amyloliquefaciens, Aspergillus oryzae and Aspergillus melleus.
    Through the selection of suitable endoproteases, it is possible to obtain not only the characteristic molecular weight distribution of the collagen hydrolyzate, but also the type of amino acids at the ends of the peptides obtained in the hydrolyzate is also influenced. In this regard, it is preferable, for example, if at least 50% of the N-terminal amino acids of the collagen hydrolyzate are hydrophobic amino acids, in particular, alanine, leucine and isoleucine.
    The invention also relates, in particular, to the use of collagen hydrolyzate to stimulate the biosynthesis of extracellular matrix proteins through skin cells. Skin cells comprise, in particular, fibroblasts that, among others, synthesize collagen (mainly type I), elastin, as well as proteoglycans. The formation of these proteins in sufficient quantity is decisive for the structuring or regeneration of the extracellular matrix of the skin, which in turn, is essentially determinant for the properties of the skin, such as tonicity and elasticity, as well as its moisture.
    The skin cells also include keratocytes, which are responsible for both the keratinization of the outer layer of the skin and the formation of hair and nails. Thus, a stimulation of these cells by the collagen hydrolyzate used according to the invention, can cause an improvement in the skin barrier function, as well as in the health of the hair and / or nails.
    An essential aspect of the invention concerns the use of collagen hydrolyzate to increase the skin's tensile strength and / or decrease
    5/14 formation of wrinkles. These skin properties worsen, as a rule, conditioned by age, as well as as a result of environmental influences, such as, for example, UV radiation or toxic substances. Since collagen and elastin matrix proteins are especially responsible for skin tonicity and elasticity, through their multiple synthesis, which is particularly stimulated by the collagen hydrolyzate used according to the invention, they can react against these effects and improve markedly skin health.
    Another important aspect of the invention concerns the use of collagen hydrolyzate to increase the skin's moisture content. An essential contribution to the skin's ability to form sufficient amounts of moisture is provided by the proteoglycans contained in the extracellular matrix (for example, versican, biglican and decorin), whose synthesis is also proven to be stimulated by the collagen hydrolyzate used according to invention. The skin's moisture content can also be reduced through harmful environmental influences, such as UV radiation, where moisture loss often occurs with less elasticity, cracking and excessive keratinization of the skin.
    Another important aspect of the invention concerns the use of collagen hydrolyzate to improve the skin's barrier function. An essential role for this barrier function are the aforementioned CE proteins (cornified envelope proteins), among others, involucrin, loricrin and filagrin, whose biosynthesis is proven to be stimulated by low molecular weight collagen hydrolyzate. Thus, through the use according to the invention of collagen hydrolyzate, the reduction of moisture loss, the barrier function, as well as, the natural protection of the skin against pathogenic germs and toxic substances, improves.
    The use according to the invention of collagen hydrolyzate additionally also leads to an antioxidant effect on the skin region, with which the frequency of DNA damage (mutations) can be reduced, for example, through UV radiation or mutagenic substances . Such mutations represent one of the origins for the premature aging of
    6/14 cells and thereby promote signs of skin aging (decreased tone, wrinkle formation and so on), so that this procedure can be inhibited by use according to the invention.
    According to a preferred embodiment of the invention, the collagen hydrolyzate is intended for oral ingestion. Oral intake often results in more efficient transport of collagen hydrolyzate through the bloodstream to the site of action, that is, in particular, to the skin cells, than to a topical application. In addition, this form of application for the user is usually associated with substantially less expense.
    Preferably, collagen hydrolyzate is used as a food supplement. In this case, collagen hydrolyzate serves, as a rule, to improve skin health in the sense of general health prevention or also as a cosmetic application; such food supplements can be referred to as nutraceuticals or nutricosmetics. But the use of collagen hydrolyzate for the treatment of a clinical condition in the context of the present invention is also possible, for example, in the presence of atopic dermatitis, in which patients have a high tendency to dry, cracked skin.
    The food supplement can be offered in almost arbitrary form, for example, in the form of tablets, capsules, pills, lozenges or also a solution (for example, in individual ampoules or in drinks).
    Collagen hydrolyzate can also alternatively be contained in a food or related products, for example, in sweets or in an instant powder for the preparation of drinks. In this way, the hydrolyzate can be taken by the consumer without additional expense within the scope of a normal diet (the so-called functional food). In this context, it is particularly advantageous that the collagen hydrolyzate has an essentially neutral flavor.
    It is advantageous to have a daily intake of about 1.5 to 5 g, preferably about 2 to 3 g, more preferably
    7/14 about 2.3 to 2.7 g of collagen hydrolyzate. It has been shown that through oral intake of this amount of hydrolyzate, the skin's health can be noticeably improved within a few weeks.
    Another embodiment of the invention relates to the topical application of collagen hydrolyzate, that is, to the application in the form of cosmetic products to be applied to the skin, hair and / or nails. The collagen hydrolyzate, in this case, can be contained, in particular, in a cream, an ointment, a lotion or a gel. It is also advantageous that the collagen hydrolyzate is added to a body care product, such as, for example, in a shower gel or hair shampoo, for example, in an amount of about 5 to 10 % by weight.
    This and other advantages of the invention are described in detail based on the following examples with reference to the figures. Individually show:
    Figures 1A through 1C: diagrams that refer to the stimulation of type I, biglican or versican collagen synthesis;
    Figures 2A and 2B: diagrams referring to the increase in skin moisture in bald mice;
    Figure 3: a diagram referring to the stimulation of EC protein synthesis;
    Figure 4A to 4C: MALDI mass spectra of several collagen hydrolysates; and Figure 5A and 5B: diagrams that refer to stimulation of type I, decorin and versican collagen synthesis.
    Examples
    1. Production and properties of collagen hydrolyzate
    To produce a collagen hydrolyzate according to the invention, an aqueous solution of a pigskin gelatine (type A, 200 to 250 g Bloom) is used with a concentration of 20 to 40% by weight (dry substance). Gelatin is enzymatically hydrolyzed through the successive action of two different endoproteases from
    8/14 microbial origin at 50 to 60 ° C for 120 to 180 minutes, in which, as a first enzyme, a Bacillus subtilis or Bacillus amyloliquefaciens endoprotease is used and as a second enzyme, a Bacillus licheniformis endoprotease. Then, the enzymes are thermally inactivated and the solution is spray dried.
    The molecular weight distribution of the resulting collagen hydrolyzate can be determined by means of gel permeation chromatography using the following parameters:
    stationary phase: TSK 2000 SW XL (Tosoh Bioscience GmbH) mobile phase: 0.4 mol / l dihydrogen phosphate pH 5.3 flow rate: 0.5 ml / min calibration standard: defined type I collagen fragments (FILK, Freiberb) detection: UV detector Knauer K-2501 at 214 nm.
    The determination provided a molecular weight distribution of the collagen hydrolyzate according to the invention (hereinafter referred to as low molecular weight hydrolyzate) according to the following Table 1. For comparison, Table 1 also indicates the weight distribution molecular structure of a commercially available collagen hydrolyzate, which was terminated with the same method (hereinafter referred to as high molecular weight hydrolyzate):
    Table 1
    molecular weight range low molecular weight hydrolyzate high molecular weight hydrolyzate > 7,500 Da <5% by weight <10% by weight 3,500 - 7,500 Da about 12-18% inWeight about 25-35% inWeight 1,500-3,500 Da about 25-31% by weight about 29-35% inWeight 500-1,500 Da about 40-46% inWeight about 24-30% inWeight <500 Da about 5.10% by weight about 2-5% inWeight
    The hydroxyproline content of this low molecular weight hydrolyzate is about 12 to 13% by weight and can be photometrically determined after oxidation with chloramine-T and reaction with pdimethylamino-benzaldehyde. More than 50% of the hydrolyzate's N-terminal amino acids are hydrophobic amino acids, in particular, alanine, leucine and isoleucine.
    2. Stimulation of extracellular matrix protein synthesis
    The stimulation of collagen synthesis (type I) as well as biglican and versican proteoglycans was investigated in vitro in human dermal fibroblasts (skin cells). For that purpose, the cells were incubated for 24 hours with 0.5 mg / ml each of the low molecular weight or high molecular weight hydrolyzate, and then the expression of collagen RNA, biglican-RNA and versican-RNA was determined by Realtime-PCR and evaluated semi-quantitatively (based on a control without hydrolyzate).
    The results are represented as column diagrams for type-l collagen in figure 1A, for biglican in figure 1B and for versican in figure 1C, with the diagrams showing in each case the average value of at least 18 measurements. In the abscissa, the expression RNA is registered in relation to the control (= 1). The filled left column represents in each case the control, the shaded middle column represents the high molecular weight hydrolyzate (as a comparison) and the dotted right column, the low molecular weight hydrolyzate (according to the invention).
    It was found that the synthesis of all three matrix proteins is stimulated by the two collagen hydrolysates, and the positive effect of the low molecular weight hydrolyzate is in each case more pronounced than that of the high molecular weight hydrolyzate. In collagen, which in addition to elastin, is mainly responsible for skin tonicity and elasticity, as well as in versican, it has an important role in maintaining skin moisture, the pronounced effect of low molecular weight hydrolyzate is particularly clear.
    3. Increased skin moisture content
    The influence of skin moisture through the colá10 / 14 geno hydrolyzate was investigated directly in bald mice. Hairless mice represent an established model system, which is often used in dermatological matters and the knowledge obtained from these can be transmitted, in principle, to human skin (see, for example, T. Fujimura etal .; J. Dermatol. Sei. 2000 (24) 105-111 and Y. Nishimori et al .; J. Invest. Dermatol. 2001 (117) 1458-1463).
    The animals were fed for a period of three weeks daily with 150 pg of collagen hydrolyzate per kg of body weight, the control group, instead, received BSA. At the same time, all animals received a weekly dose of UV-B radiation of 18 mJ / cm 2 on the skin surface, so the skin moisture is negatively influenced.
    The moisture content of the skin was measured after one week and after three weeks with a CM 825 corneometer (manufacturer: Courage & Khazaka). The measurement principle is based here on changing the capacity of a measurement capacitor through the dielectricity constant of the water bound in the upper layers of the skin, which differs from the dielectricity constants of most other substances.
    The results are shown in Figure 2A as column charts for the measurement after one week and in Figure 2B for the measurement after three weeks, where the graphs show in each case the mean value and standard error of 7 measurements. In abscissa, skin moisture is plotted relative to the control (= 1). The filled left column represents in each case the control, the shaded middle column represents the high molecular weight hydrolyzate (as a comparison) and the dotted right column, the low molecular weight hydrolyzate (according to the invention).
    It can be seen that the increase in skin moisture by the low molecular weight hydrolyzate both after one week and also after three weeks is in each case greater than the high molecular weight hydrolyzate. This is another result for the particular effectiveness of the hydrolyzate used according to the invention in improving skin health.
    11/14
    4. Stimulation of EC protein synthesis
    The so-called Cornified Envelope proteins ”play an important role in the skin's barrier function against the penetration of pathogenic germs and toxic substances. The synthesis of CE proteins involucrin, loricrin and filaggrin was determined in hairless mice, which were previously fed for five weeks daily with 150 pg of collagen hydrolyzate per kg of body weight (as described above). The quantification of proteins in relation to a control group (feeding with BSA) was performed by electrophoresis in SDSpolycrylamide gel and Western-Blot with specific antibodies after the extraction of proteins from the skin.
    The results are shown in Figure 3 as column graphs, where the graph shows in each case the average value and the standard error of 7 measurements. In abscissa, the amount of CE proteins after feeding with the low molecular weight hydrolyzate is plotted relative to the control (= 1). The left column represents Involucrin, the middle column, Loricrin and the right column represents Filaggrin.
    It appears that the synthesis of all three EC proteins investigated is stimulated by the oral absorption of the collagen hydrolyzate used according to the invention, in the case of Involucrin, even in more than triple.
    5. Antioxidant effect of collagen hydrolyzate
    The antioxidant effect of low molecular weight collagen hydrolyzate was determined in a cell-free system using a malondiaideide assay.
    In this case, it appears that the formation of reactive oxygen species is reduced by collagen hydrolyzate by an average of about 7%. In the skin region, the frequency of DNA damage can thus be reduced, so that it is possible to react against the signs of aging through use according to the invention.
    6. Analysis of molecular weight distribution using MSMALDI
    12/14
    The low molecular weight collagen hydrolyzate according to the invention, produced according to example 1, which has an average molecular weight of about 2,000 Da (hereinafter, hydrolyzate A), was confronted with two commercially available collagen hydrolysates with a average molecular weight of about 2,100 Da (hereinafter, hydrolyzate B) and about 2,900 Da (hereinafter, hydrolyzate C).
    The exact molecular weight distributions of these three hydrolysates were analyzed using MALDI mass spectroscopy (MSMALDI). For this purpose, the samples were adjusted in 0.1% trifluoroacetic acid to a final concentration of 10 pg / μΙ and then purified using pCi 8 material. The samples were prepared with an HCCA matrix on a MALDI target and the mass spectra were determined using an Ultraflex-lll-TOF / TOF mass spectrometer (manufacturer: Bruker Daltonics).
    Figures 4A through 4C show the corresponding mass spectra or molecular weight distributions of collagen hydrolysates A, B or C, with the molecular weight or mass index being plotted in the ordinate and in the abscissa, the intensity. A comparison of the three spectra shows that the hydrolyzate A according to the invention comprises the following characteristic peptides according to Table 2, with the corresponding peaks having a double to quadruple intensity compared to their medium:
    Table 2
    In particular, the four peptides between 600 and 1,500 Da have no correspondence in the two commercial hydrolysates B and C,
    13/14 way, are particularly characteristic for hydrolyzate A.
    7. Stimulation of extracellular matrix protein synthesis
    The stimulation of collagen synthesis (type I), as well as decorin and versican proteoglycans, was investigated in vitro in human dermal fibroblasts (skin cells). For this, the cells were incubated for 24 hours in each case with 0.5 mg / ml of hydrolysates A, B or C, and then the expression of collagen-RNA, decorin-RNA and versican-RNA was determined by means of of realtime-PCR and evaluated semi-quantitatively. Decorin plays an important role in the formation of collagen fibers in the skin.
    The results are represented as column graphs for hydrolyzate B in figure 5A and for hydrolyzate C in figure 5B, and in the abscissa the RNA expression in commercial hydrolysates B or C is plotted in each case relative to the expression RNA in hydrolyzate A of according to the invention (= 1). The left column in each case represents type I collagen, the middle column, decorin and the right column represents versican. The average value of at least 7 measurements is represented in each case, as well as standard error.
    Interestingly, the data show that in all three matrix proteins there is markedly less stimulation of RNA synthesis compared to hydrolyzate A by the two hydrolysates B and C, whose average molecular weight is only negligibly higher. The peptides characteristic of hydrolyzate A thus seem to play a decisive role in this advantageous effect.
    8. Sample recipes for food and cosmetics (supplements)
    The following are some exemplary recipes for using the collagen hydrolyzate according to the invention, which of course can be modified in several ways:
    Capsules_ (Food supplements) glycerin 53.67% by weight hydrolyzed collagen 21.95% by weight
    14/14
    gelatine 10.08% by weight6.00% by weight5.00% by weight2.00% by weight0.50% by weight0.50% by weight0.30% by weight51.0% by weight 5 guar seed flourlecithinCitric acidaroma (cassis)orange essenceacesulfam-KChocolatecocoa mass 10 sucrose 22.4% by weight cocoa butter 16.6% by weight collagen hydrolyzateBeverage 10.0% by weight Water 63.00% by weight 15 aloe-vera concentrate 31.00% by weight collagen hydrolyzate 4.00% by weightsucrose 1.50% by weight Citric acid 0.26% by weight flavors and dyes 0.24% by weight 20 sucraloseXamou 0.0031% by weight Water 58.8% by weight sodium laureth-11-carboxylate 18.0% by weight cocoamidopropyl-betaine 9.0% by weight 25 collagen hydrolyzate 6.0% by weight PEG-6 capril / caproil-glyceride 3.0% by weight PEG-150 distearate 2.5% by weight laureth-7 2.0% by weight potassium sorbate 0.5% by weight 30 fragrance 0.2% by weight
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    权利要求:
    Claims (17)
    [1]
    1. Collagen hydrolyzate for use to improve the health of human hair, nails and / or skin, characterized by the fact that collagen hydrolyzate is produced through enzymatic hydrolysis of gel5 derived from mammals or birds by the consecutive action of at least two endoproteases with a different specificity at 50 to 60 ° C for 120 to 180 min, where a Bacillus subtilis or Bacillus amyloliquefaciens endoprotease is used as the first enzyme and a Bacillus licheniformis endoprotease is used as the second enzyme,
    10 where at least 90% by weight of the collagen hydrolyzate has a molecular weight of less than 3,500 Da, and where the collagen hydrolyzate comprises at least four characteristic peptides with a molecular weight between 600 and 1,200 Da having at least double intensity compared to your
    15 medium in a molecular weight distribution determined by MALDI mass spectroscopy, where the mass spectrum was determined using a TOF / TOF mass spectrometer with a sample of the collagen hydrolyzate having been adjusted in 0.1% trifluoroacetic acid to a final concentration of 10 pg / pl, purified using pCi 8 material and prepared with an HCCA matrix on a MALDI target.
    [2]
    2. Collagen hydrolyzate according to claim 1, characterized by the fact that at least 45% by weight of the collagen hydrolyzate has a molecular weight of less than 1,500 Da.
    [3]
    Collagen hydrolyzate according to claim 1 or
    25 2, characterized by the fact that the at least four characteristic peptides in a molecular weight distribution determined by means of MALDI mass spectroscopy have at least a quadruple intensity compared to their medium.
    [4]
    4. Collagen hydrolyzate according to any one of claims 1 to 3, characterized by the fact that the collagen hydrolyzate comprises a peptide between 620 and 690 Da, a peptide between 790 and 860 Da, a peptide between 980 and 1,050 Da and a peptide between 1,175 and
    Petition 870180030033, of 04/13/2018, p. 15/38
    2/3
    1,245 Da.
    [5]
    Collagen hydrolyzate according to any one of claims 1 to 4, characterized in that the collagen hydrolyzate comprises other characteristic peptides with a molecular weight
    5 between 1,500 and 3,500 Da showing an at least double intensity compared to its medium in a molecular weight distribution determined through MALDI mass spectroscopy.
    [6]
    Collagen hydrolyzate according to any one of claims 1 to 5, characterized in that the collagen hydrolyzate 10 does not have a hydroxyproline portion of 12% or more.
    [7]
    Collagen hydrolyzate according to any one of claims 1 to 6, characterized in that at least 50% of the N-terminal amino acids of the collagen hydrolyzate are hydrophobic amino acids, in particular, alanine, leucine and isoleucine.
    15
    [8]
    Collagen hydrolyzate according to any one of claims 1 to 7, characterized by the fact that it is to be used for the stimulation of the extracellular matrix protein biosynthesis through the skin cells.
    [9]
    9. Collagen hydrolyzate according to any of the
    Claims 1 to 8, characterized by the fact that it is to be used to increase skin tone and / or to decrease the formation of wrinkles.
    [10]
    10. Collagen hydrolyzate according to any of claims 1 to 9, characterized by the fact that it is to be used to increase the moisture content of the skin.
    25
    [11]
    Collagen hydrolyzate according to any one of claims 1 to 10, characterized in that it is to be used to improve the skin's barrier function.
    [12]
    Collagen hydrolyzate according to any one of claims 1 to 11, characterized in that the cholesterol hydrolyzate is intended for oral ingestion.
    [13]
    13. Collagen hydrolyzate according to claim 12, characterized by the fact that collagen hydrolyzate is a supplement
    Petition 870180030033, of 04/13/2018, p. 16/38
    3/3 food.
    [14]
    14. Collagen hydrolyzate according to claim 12, characterized in that the collagen hydrolyzate is contained in a food or related product.
    [15]
    Collagen hydrolyzate according to any one of claims 12 to 14, characterized in that a daily intake of about 1.5 to 5 g, preferably about 2 to 3 g, more preferably about 2, 3 to 2.7 g of collagen hydrolyzate.
    [16]
    16. Collagen hydrolyzate according to any of claims 1 to 11, characterized in that the collagen hydrolyzate is intended for topical application.
    [17]
    17. Collagen hydrolyzate according to claim 16, characterized in that the collagen hydrolyzate is contained in a cream, ointment, lotion, gel or shampoo.
    Petition 870180030033, of 04/13/2018, p. 17/38
    1/6
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    法律状态:
    2017-08-15| B07A| Technical examination (opinion): publication of technical examination (opinion) [chapter 7.1 patent gazette]|
    2018-01-16| B07A| Technical examination (opinion): publication of technical examination (opinion) [chapter 7.1 patent gazette]|
    2018-06-19| B09A| Decision: intention to grant [chapter 9.1 patent gazette]|
    2018-07-17| B16A| Patent or certificate of addition of invention granted|
    优先权:
    申请号 | 申请日 | 专利标题
    DE201010060564|DE102010060564A1|2010-11-15|2010-11-15|Use of collagen hydrolyzate to improve the health of human skin, hair and / or nails|
    PCT/EP2011/067028|WO2012065782A2|2010-11-15|2011-09-29|Collagen hydrolysate used to improve the health of human skin, hair and/or nails|
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