RECOMBINANT PRODUCTION OF A COLLAGEN PEPTIDE PREPARATION AND USE THEREOF

Abstract

The present invention relates to a method for producing a collagen peptide preparation containing recombinant collagen peptides. The method is characterized in that it comprises the following steps: a) providing an in vitro expression system including at least one expression cassette, the expression cassette including at least one nucleotide sequence encoding a collagen peptide having a molecular weight in the range of 8 to 100 kDa; b) incubating the expression system under conditions that allow expression of the collagen peptide; c) obtaining the collagen peptide; d) hydrolyzing the collagen peptide under conditions that result in the production of a collagen peptide preparation including collagen peptides having an average molecular weight of 1 to 5 kDa and a molecular weight in the range of 0.1 to 12 kDa; wherein no more than 5.5% by weight of the hydrolyzed collagen peptides have a molecular weight of less than 500 Da, no more than 2.8% by weight of the hydrolyzed collagen peptides have a molecular weight between 7500 Da and 13500 Da, and between 35% and 60% by weight of the hydrolyzed collagen peptides have a molecular weight between 1500 Da and 3500 Da; e) obtain the collagen peptide preparation.

Description

RECOMBINANT PRODUCTION OF A COLLAGEN PEPTIDE PREPARATION AND USE THEREOF FIELD OF INVENTION The present invention relates to methods for producing collagen peptide preparations containing recombinant collagen peptide, to collagen peptide preparations produced by these methods, to products containing the collagen peptide preparations, and to the use of the aforementioned preparations and products. BACKGROUND OF THE INVENTION Collagen is an extracellular structural protein found in some animals, such as mammals, birds, and fish. It is typically found in connective tissue, specifically as a component of the extracellular matrix. Collagen is particularly abundant in tendons, ligaments, cartilage, and bones. However, collagen is not found in plants or single-celled organisms. Collagens come in different types, structurally and functionally distinct, and are distinguished, among other aspects, by their structure, function, and origin. The polypeptide chains that make up collagen are synthesized one by one in the cell at the ribosomes of the endoplasmic reticulum as larger precursor molecules and have bulky (gli-XY)n repeating sequences, where X and Y can be any amino acid, although most often they are proline and 4-hydroxyproline. These precursor polypeptide chains are hydroxylated in the endoplasmic reticulum, forming post-translational hydroxyproline and hydroxyl residues on proline and lysine residues of the polypeptide chain. Hydroxylation serves to stabilize adjacent collagen polypeptide chains of the right-handed triple helix of three of the precursor polypeptide chains (procollagen). The procollagen thus formed is glycosylated intracellularly, secreted by the cell in the form of a glycosylated triple helix (tropocollagen), and then collagen is formed by peptide-mediated separation of the terminal residues. Collagen is also frequently used in its denatured form and is then designated as gelatin or in the form of hydrolysates. If gelatin and collagen are subjected to hydrolytic processes, particularly enzymatic hydrolysis, collagen hydrolysates with different compositions and application profiles can be produced, depending on the type and origin of the collagen used, as well as the enzymatic conditions. Collagen hydrolysates represent a mixture of peptides whose molecular weights are distributed within specific size ranges. The use of such collagen hydrolysates, for example, as a dietary supplement or as a cosmetic additive, has been known for some time, among other uses, for the prevention and / or treatment of conditions related to bones, joints, or connective tissue. Document WO 2012 / 065782, for example, describes collagen hydrolysates obtained from pigskin gelatin that serve to stimulate the biological synthesis of extracellular matrix proteins by skin cells and are suitable, in particular, for cosmetic purposes. Document WO 2012 / 117012 states an enzymatically hydrolyzed collagen from bovine hide with an average molecular weight of 1500 to 8000 Da that can be used together with a prebiotic for the prevention and / or treatment of osteoporosis. Although the use of collagen hydrolysates derived from animal sources offers advantages for many applications and consumer groups, for certain consumer groups and application profiles, their use may be less desirable. Some consumer groups have a critical or rejecting attitude toward raw materials derived from animal sources, either due to concerns about contamination with microorganisms or agents hazardous to health (such as behavioral aids) or undesirable immunological reactions, or for religious or ethical reasons. Furthermore, the production methods used to obtain collagen hydrolysates from animal sources often involve complex and expensive decomposition, purification, and processing steps.It may also be convenient for certain applications to offer a standardized collagen hydrolysate, precisely and reliably defined, that can be advantageously and economically produced also on an industrial scale. Given this background, it is not surprising that methods were developed to produce gelatin and collagen, as well as hydrolysates of these, using recombinant genetic technology. Document WO 2006 / 052451 A2, for example, shows the production of recombinant type III collagen in strains of Pichia pastoris that also express human prolyl hydroxylases. Document WO 2005 / 012356 A2 states the production of human type I collagen gelatin and individual collagen peptide species with sizes of 50 kDa, 65 kDa and 100 kDa, in each case in fully hydroxylated, partially or non-hydroxylated form. Document WO 01 / 34646 A2 also states the production of individual recombinant gelatin species with a defined molecular weight resulting from the recombinant production route, which may be present in non-hydroxylated, partially or totally hydroxylated form. The production of recombinant collagen or collagen hydrolysates that possess structural and functional properties identical or at least similar to those of collagen or collagen hydrolysates obtained from natural sources is, however, problematic. This is due, among other reasons, to the fact that natural collagen formation is a comparatively complex physiological process, influenced by a series of intra- and extracellular factors, including post-translational synthesis steps such as glycosylation and hydroxylation. These post-translational synthesis steps, particularly the specific positioning and degree of hydroxylation of proline and lysine, ensure the formation of stable tropocollagen, which ultimately associates to form fibrils and fibers.It is known, for example, from Wang et al. (Engineering Biology, 2017 (1), 18-23) that current recombinant collagen production is characterized by low yields, high costs, and, in particular, absent or deviant post-translational synthesis steps. It is also known that these post-translational modifications are essential for both the natural structure and function of collagen and for applications that utilize collagen or collagen hydrolysates. frczcnn / Lznz / B / Yi To date, there is correspondingly no recombinantly produced collagen or collagen hydrolysate that has a structure, in particular, the quality and quantity of post-translational modifications, in particular, the degrees of hydroxylation and glycosylation and the positions of hydroxylation and glycosylation that are identical to natural collagens or collagen hydrolysates obtained from them. The preparation of recombinantly produced collagen and collagen hydrolysates with the potential properties derived from collagen, or of conventionally produced collagen hydrolysates, is not straightforward, due, among other reasons, to the circumstances described above, particularly the differences in raw materials and production methods. In particular, in prokaryotic organisms, which are inherently suitable for the industrial production of recombinant proteins, the production of recombinant collagen is problematic. This is partly because post-translational synthesis steps must usually be introduced into the cell using recombinant technologies, resulting in an additional metabolic burden that hinders or prevents the expression and production of the desired collagen peptides.Furthermore, the expression of foreign proteins can be toxic to the host cell, obtaining recombinantly produced proteins in or from host cells may not be technically or economically feasible, the stability of the expression product may be very low, or other effects such as growth and reproduction failures may occur. Therefore, there is still a great demand for a proposal of recombinantly produced collagen hydrolysates for application in the most diverse fields, in particular also for therapeutic purposes, in particular for the prevention or treatment of conditions or diseases related to the muscles, joints, bones and skin of man and animal. BRIEF DESCRIPTION OF THE INVENTION The present invention is therefore based on the technological problem of providing methods for the production of collagen peptide preparations and the recombinant collagen peptide preparations thus obtained that overcome the disadvantages mentioned above, and that, in particular, can be recombinantly produced in a standardized, reliable, and precisely defined manner, even on a larger industrial and economical scale, and that have comparable properties, in particular, optimized properties, with respect to collagen hydrolysates obtained from animal-derived materials, and that have, in particular, greater activity, in particular, that develop biological activity with respect to the preservation of the health of muscles, joints, bones, and skin, as well as the prevention or treatment of diseases related to the muscles, joints, bones, and skin of humans and animals. The present invention solves the technological problem on which it is based by offering the lessons of the independent claims, in particular, also the lessons of the preferred modalities in the description and in the dependent claims. The present invention relates, in particular, to a method for the production of a collagen peptide preparation comprising recombinant collagen peptides comprising the following method steps: frczcnn / ίζηζ / Β / γι a) providing an expression system comprising at least one expression cassette, the expression cassette comprising at least one nucleotide sequence encoding a collagen peptide with a molecular weight in the range of 8 to 100 kDa, b) incubate the expression system under conditions that allow the expression of the collagen peptide, c) obtain the collagen peptide, d) hydrolyzing the collagen peptide under conditions conducive to the production of a collagen peptide preparation comprising collagen peptides with an average molecular weight of 1 to 7 kDa and having a molecular weight in the range of 0.1 to 13.5 kDa and e) obtain the collagen peptide preparation. The method provided by the invention for the production of collagen peptide preparations is distinguished, above all, in that it is prepared from at least one, preferably from exactly one precisely defined, recombinantly produced collagen peptide, with a specific size of 8 to 100 kDa, a recombinantly produced collagen peptide preparation having a molecular weight distribution and structure advantageously resulting from the specific recombinant collagen peptide species used for hydrolysis, and the subsequent method steps, in particular the hydrolysis step, in particular the hydroxylation profile, and which are distinguished, their recombinant production notwithstanding, directly and without additional processing steps by advantageous biological activity. Inventively prepared collagen peptide preparations exhibit notable structural differences, particularly regarding modifications introduced by post-translational synthesis steps such as hydroxylation and glycosylation, due to their recombinant production method, compared to collagen hydrolysates obtained from natural sources. Remarkably, they can be prepared in a wide variety of expression systems, even on an industrial scale, without undesirable contamination, while simultaneously possessing advantageous biological activity, especially for applications in maintaining and improving the health of bones, cartilage, skin, hair, and nails. The inventively discovered biological activity of recombinantly prepared collagen peptide preparations is already present in preparations obtained directly from hydrolysis without requiring additional processing steps. The biological activity of the inventively discovered and recombinantly produced collagen peptide preparations of the present invention can be verified, in particular, with the help of in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts and chondrocytes, preferably with the help of in vitro assays for the stimulation of extracellular matrix protein synthesis or of the mRNA encoding these proteins in osteoblasts, fibroblasts and chondrocytes, in particular, with the help of the in vitro assays represented in Examples 3 to 7, in particular, in Examples 3 to 5, for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts and chondrocytes. In a particularly preferred embodiment, the collagen peptide preparations containing inventively produced recombinant collagen peptides of the present invention have biological activity in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The collagen peptide preparations comprising recombinant collagen peptides, inventively produced according to the present invention, preferably have, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5, the same biological activity as collagen peptide preparations isolated from natural sources, in particular, as collagen peptide preparations produced in a non-recombinant manner. The collagen peptide preparations comprising recombinant collagen peptides, inventively produced according to the present invention, preferably have, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5, better biological activity than collagen peptide preparations isolated from natural sources, in particular, than collagen peptide preparations produced in a non-recombinant manner. In a preferred embodiment of the present invention, the expression system prepared in step a) is a cell-based or cell-free expression system. The expression system prepared in step a), in particular, the cell-based expression system is a host cell, in particular, a prokaryotic or eukaryotic cell. The expression system, in particular the cell-based expression system, is preferably a host cell selected from the group of bacterial cells, yeast cells, fungal cells, mammalian cells, insect cells, and plant cells. The expression system, in particular the cell-based expression system, is preferably a bacterial cell, particularly of the species Escherichia coli or Bacillus subtilis. In another preferred embodiment of the present invention, the expression system, in particular the cell-based expression system, is preferably a yeast cell, in particular, of the species Saccharomyces cerevisiae, Pichia pastoris or Ogataea angusta (Hansenula polymorpha). The expression system, in particular the cell-based expression system, is preferably a fungal cell, in particular, of the species Aspergillus niger. In another preferred embodiment of the present invention, the expression system, in particular the cell-based expression system, is a mammalian cell, in particular a CHO cell, a HeLa cell, or a HEK293 cell. The expression system, in particular the cell-based expression system, is preferably an insect cell, in particular an Sf-9, Sf-21 or Tn-5 cell. The expression system, in particular the cell-based expression system, is preferably a plant cell, in particular a maize or tobacco cell. In another preferred embodiment of the present invention, the expression system prepared in step a) is an expression system, in particular a cell-based expression system, capable of hydroxylating proline, lysine, or proline and lysine residues of the expressed collagen peptide. The expression system prepared in step a) is preferably a host cell capable of hydroxylating proline, lysine, or proline and lysine residues of the expressed collagen peptide. The expression system prepared in step a) is preferably an expression system, in particular a cell-based expression system exhibiting prolyl hydroxylase and / or lysyl hydroxylase activity. The expression system prepared in step a) is preferably a host cell exhibiting prolyl hydroxylase and / or lysyl hydroxylase activity. In a preferred embodiment, the expression system prepared in step a) is a cell-based expression system comprising at least one expression cassette comprising a polynucleotide sequence encoding prolyl-4-hydroxylase. Particularly preferably, the expression system prepared in step a) is a cell-based expression system comprising at least one expression cassette comprising a polynucleotide sequence encoding prolyl-4-hydroxylase, such that a hydroxylated collagen peptide preparation is obtained in vivo in step e) of the method. In a preferred embodiment, the expression system prepared in step a) is a cell-based expression system comprising at least one expression cassette comprising a polynucleotide sequence encoding lysyl hydroxylase. Particularly preferably, the expression system prepared in step a) is a cell-based expression system comprising at least one expression cassette comprising a polynucleotide sequence encoding lysyl hydroxylase, such that in step e) of the method, a hydroxylated collagen peptide preparation is obtained in vivo. In a preferred embodiment, the expression system prepared in step a) is a cell-based expression system comprising at least one expression cassette comprising a polynucleotide sequence encoding prolyl-4-hydroxylase and at least one expression cassette comprising a polynucleotide sequence encoding lysyl hydroxylase. Particularly preferentially, the expression system prepared in step a) is a cell-based expression system comprising at least one expression cassette comprising a polynucleotide sequence encoding prolyl-4-hydroxylase and at least one expression cassette comprising a polynucleotide sequence encoding lysyl hydroxylase, such that a hydroxylated collagen peptide preparation is obtained in vivo in step e) of the method. The present invention therefore also comprises a method for the production of a collagen peptide preparation comprising recombinant collagen peptides, in particular, an in vivo hydroxylated collagen peptide preparation comprising the method steps a) providing a cell-based expression system comprising at least one expression cassette, the expression cassette comprising at least one nucleotide sequence encoding a collagen peptide with a molecular weight in the range of 8 to 100 kDa and wherein the cell-based expression system is capable of hydroxylating proline, lysine or proline and lysine residues of the expressed collagen peptide, b) incubate the cell-based expression system under conditions that enable the expression and hydroxylation of the collagen peptide, c) obtaining the collagen peptide, in particular, the in vivo hydroxylated collagen peptide, d) hydrolyzing the collagen peptide, in particular the in vivo hydroxylated collagen peptide under conditions conducive to the production of a collagen peptide preparation, in particular, in vivo hydroxylated collagen peptides comprising collagen peptides with an average molecular weight of 1 to 7 kDa and having a molecular weight in the range of 0.1 to 13.5 kDa and e) obtaining the collagen peptide preparation, in particular, from the in vivo hydroxylated collagen peptide preparation which, hereinafter, is also referred to as collagen peptide preparations A. With the aid of the aforementioned method, it is advantageously possible to obtain a collagen preparation with recombinantly produced in vivo collagen peptides that have a specific molecular weight and a specific median molecular weight, which are distinguished, depending on the cell-based expression system used in each case, by a specific pattern of post-translational modifications, in particular, hydroxylations and glycosylations. It is particularly advantageous to obtain a biologically active collagen peptide preparation directly, i.e., without the need for further modification of the collagen peptides in the collagen peptide preparation. In a preferred embodiment, the in vivo hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., collagen peptide preparation A, shows biological activity in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The in vivo hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., collagen peptide preparation A, preferably exhibits the same biological activity as collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The in vivo hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., collagen peptide preparation A, shows, in particular preference, better biological activity than collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. According to another embodiment of the present invention, the expression system prepared in step a) is an expression system that is not capable of causing hydroxylation of proline, lysine or proline and lysine residues of the collagen peptide; in particular, the expression system prepared in step a) does not exhibit any prolylhydroxylase or lysylhydroxylase activity. The present invention therefore comprises a method for the production of a collagen peptide preparation comprising recombinant collagen peptides, in particular, a non-hydroxylated collagen peptide preparation comprising the method steps a) providing an expression system comprising at least one expression cassette, the expression cassette comprising at least one nucleotide sequence encoding a collagen peptide with a molecular weight in the range of 8 to 100 kDa and wherein the expression system is not capable of hydroxylating proline, lysine or proline and lysine residues of the expressed collagen peptide, b) incubate the expression system under conditions that allow the expression of the collagen peptide, c) obtaining the collagen peptide, in particular, from the non-hydroxylated collagen peptide, d) hydrolyzing the collagen peptide, in particular the non-hydroxylated collagen peptide, under conditions conducive to the production of a collagen peptide preparation comprising collagen peptides with an average molecular weight of 1 to 7 kDa and having a molecular weight in the range of 0.1 to 13.5 kDa and e) obtaining the collagen peptide preparation, in particular, the non-hydroxylated collagen peptide which, in what follows, is also referred to as collagen peptide preparations B. In a preferred embodiment, the non-hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide B preparation, shows biological activity in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The non-hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide B preparation, preferably exhibits the same biological activity as collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The non-hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide B preparation, shows, in particular preference, better biological activity than collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. In a preferred embodiment of the present invention, the collagen peptide obtained in step c) of the method is hydroxylated before the execution of step d) of the method in a step x1) of the method and is obtained in step e) of the method in pre-lysal form, i.e., before hydrolysis, a pre-lysal ex vivo hydroxylated collagen peptide preparation. The present invention therefore further comprises a method for the production of a collagen peptide preparation comprising recombinant collagen peptides, in particular, a pre-lysal ex vivo hydroxylated collagen peptide preparation comprising the method steps a) providing an expression system comprising at least one expression cassette, the expression cassette comprising at least one nucleotide sequence encoding a collagen peptide with a molecular weight in the range of 8 to 100 kDa and wherein the expression system is not capable of hydroxylating proline, lysine or proline and lysine residues of the expressed collagen peptide, b) incubate the expression system under conditions that allow the expression of the collagen peptide, c) obtain the collagen peptide, x1) hydroxylate ex vivo the collagen peptide obtained in step c) d) hydrolyzing the collagen peptide, in particular the hydroxylated collagen peptide ex vivo under conditions conducive to the production of a collagen peptide preparation comprising collagen peptides with an average molecular weight of 1 to 7 kDa and having a molecular weight in the range of 0.1 to 13.5 kDa and e) obtaining the collagen peptide preparation, in particular the ex vivo pre-lysal hydroxylated collagen peptide which, hereinafter, is also referred to as collagen peptide C preparations. In a preferred embodiment, the ex vivo prelyal hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide C preparation, shows biological activity in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The ex vivo pre-lysal hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide C preparation, preferably exhibits the same biological activity as collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The ex vivo pre-lysal hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide C preparation, shows, in particular preference, better biological activity than collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes represented in Examples 3 to 7, in particular, in Examples 3 to 5. In another preferred embodiment of the present invention, the collagen peptide obtained in step c) is hydroxylated after the execution of step d) of the method in a step x2) of the method and is obtained in step e) of the method in post-lysal form, i.e., after hydrolysis, a preparation of hydrolyzed collagen peptide hydroxylated in post-lysal form ex vivo. The present invention therefore further comprises a method for the production of a collagen peptide preparation comprising recombinant collagen peptides, in particular, a pre-lysal ex vivo hydroxylated collagen peptide preparation comprising the method steps a) providing an expression system comprising at least one expression cassette, the expression cassette comprising at least one nucleotide sequence encoding a collagen peptide with a molecular weight in the range of 8 to 100 kDa and wherein the expression system is not capable of hydroxylating proline, lysine or proline and lysine residues of the expressed collagen peptide, b) incubate the expression system under conditions that allow the expression of the collagen peptide, c) obtain the collagen peptide, d) hydrolyzing the collagen peptide under conditions conducive to the production of a collagen peptide preparation comprising collagen peptides with an average molecular weight of 1 to 7 kDa and having a molecular weight in the range of 0.1 to 13.5 kDa and x2) hydroxylating ex vivo the collagen peptide from the collagen preparation obtained in step d) e) obtaining the collagen peptide preparation, in particular the ex vivo post-lysal hydroxylated collagen peptide preparation which, hereinafter, is also referred to as collagen peptide preparations D. In a preferred embodiment, the ex vivo post-lysal hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide D preparation, shows biological activity in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The ex vivo pre-lysal hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide D preparation, preferably exhibits the same biological activity as collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. The ex vivo post-lysal hydroxylated collagen peptide preparation containing inventively produced recombinant collagen peptides, i.e., the collagen peptide D preparation, shows, in particular preference, better biological activity than collagen peptide preparations isolated from natural sources, in particular, collagen peptide preparations not recombinantly produced, in at least one of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably, in at least two, preferably, in all of the in vitro assays for the stimulation of extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes depicted in Examples 3 to 7, in particular, in Examples 3 to 5. According to a preferred embodiment of the present invention, the at least single nucleotide sequence of the at least single expression cassette was subjected to codon optimization, i.e., those codons in the nucleotide sequence that are not used or that are preferably not used by the translation system of the prepared expression system, in particular, by the prepared cell-based expression system, in particular, in the prepared host cell, are replaced by others that are preferably used by the translation system of the prepared expression system, in particular, by the prepared cell-based expression system, in particular, in the prepared host cell, without thereby changing the amino acid sequence of the encoded peptide or protein. In a preferred embodiment of the present invention, the collagen peptide encoded by the frczcnn / Lznz / B / Yi nucleotide sequence is a collagen peptide from a vertebrate, in particular, from a mammal, for example, man, or from a non-human mammal, for example, horse, donkey, kangaroo, sheep, rodent, pig or cattle, from a bird, for example, chicken, from a fish, from an amphibian, from a reptile, or from a non-vertebrate animal, for example, jellyfish. The collagen peptide encoded by the nucleotide sequence preferably comprises an amino acid sequence present in collagen of types I, II, III, IV, V, VI, VII, VIII, IX, X, XI, XII, XIII, XIV, XV, XVI, XVII, XVIII, XIX, XX, XXI, XXII, XXIII, XXIV, XXV, XXVI, XXVII, preferably of type I, II or III, preferably of type I, preferably of type II, preferably of type III. The collagen peptide encoded by the nucleotide sequence is preferably of type I, II or III, preferably of type I or II, with particular preference for type I. The collagen peptide encoded by the nucleotide sequence preferably comprises an amino acid sequence present in vertebrate collagen, in particular fish, amphibians, reptiles, birds and mammals, in particular human, bovine, porcine, equine or avian collagen of types I, II or III, preferably of type I, preferably of type II, preferably of type III. The collagen peptide encoded by the nucleotide sequence has, in particular preference, an amino acid sequence present in human collagen, in particular, in human type I collagen, preferentially in the a1 chain of human type I collagen. The collagen peptide encoded by the nucleotide sequence has, in particular preference, an amino acid sequence present in a non-human collagen, in particular, in a non-human type I collagen, preferably in the a1 chain of the non-human type I collagen, in particular, an amino acid sequence present in bovine, equine, or avian collagen. The collagen peptide encoded by the nucleotide sequence is, preferably, a naturally occurring collagen peptide. In another preferred embodiment of the present invention, the collagen peptide encoded by the nucleotide sequence is not a naturally occurring collagen peptide. The collagen peptide encoded by the nucleotide sequence is, preferably, a genetically modified collagen peptide.In a particularly preferred embodiment of the present invention, the collagen peptide encoded by the nucleotide sequence is a genetically modified collagen peptide in which at least one amino acid of the amino acid sequence of a naturally occurring collagen peptide, preferably at least one non-essential amino acid, in particular Ala, Asn, Asp, Glu, Ser of the amino acid sequence of a naturally occurring collagen peptide, was substituted by at least one fully determined amino acid, in particular, by at least one essential amino acid, in particular, Ie, Leu, Lys, Met, Phe, Thr, Trp, Val, His, Cys, Tyr, particularly preferably Trp. The collagen peptide encoded by the nucleotide sequence is, inventively preferred, a genetically modified collagen peptide in which at least one amino acid, preferably at least one non-essential amino acid, in particular, Ie, Leu, Lys, Met, Phe, Thr, Trp, Val, His, Cys, Tyr, particularly Trp, has been added to the amino acid sequence of a naturally occurring collagen peptide. It can be inventively provided that the at least one essential amino acid, preferably, in particular, Ie, Leu, Lys, Met, Phe, Thr, Trp, Val, His, frczcnn / ίζηζ / B / γι Cys, Tyr, of particular preference, Trp was added at the N term, at the C term and / or within the amino acid sequence of a naturally occurring collagen peptide. According to a preferred embodiment of the present invention, the at least single nucleotide sequence encodes a collagen peptide with a molecular weight in the range of, preferably, 8 to 95 kDa, preferably, 8 to 90 kDa, preferably, 8 to 85 kDa, preferably, 8 to 80 kDa, preferably, 9 to 95 kDa, preferably, 7 to 90 kDa, preferably, 9 to 85 kDa, preferably, 9 to 80 kDa, preferably, 10 to 95 kDa, preferably, 10 to 90 kDa, preferably, 10 to 85 kDa, preferably, 10 to 80 kDa. In a particularly preferred embodiment of the present invention, the hydrolysis is enzymatic or acid-catalyzed hydrolysis, preferably enzymatic hydrolysis, preferably acid-catalyzed hydrolysis. The hydrolysis of the collagen peptide obtained in step c) is preferably carried out by the addition of at least one bacterial or microbial protease, in particular, a serine, cysteine, aspartate protease and / or metalloprotease, preferably at least one bacterial and / or microbial endoprotease, preferably at least one bacterial and / or microbial exoprotease. In another preferred embodiment of the present invention, the collagen peptide is hydrolyzed in step d) under conditions conducive to the production of a collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 3 kDa and a molecular weight in the range of 0.1 to 10 kDa, preferably 0.18 to 10 kDa, preferably 0.2 to 10 kDa. In a preferred embodiment of the present invention, the collagen peptide is hydrolyzed in step d) under conditions conducive to the production of a collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 5 kDa and a molecular weight in the range of 0.1 to 12 kDa, preferably 0.18 to 12 kDa, preferably 0.2 to 12 kDa. The present invention relates further to a collagen peptide preparation produced by one of the inventive methods mentioned above, in particular to a collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, preferably 0.18 to 13.5 kDa, preferably 0.2 to 13.5 kDa. In a preferred embodiment of the present invention, the collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is a non-hydroxylated, partially hydroxylated, or fully hydroxylated collagen peptide preparation, preferably a non-hydroxylated collagen peptide preparation, preferably a partially hydroxylated collagen peptide preparation, preferably a fully hydroxylated collagen peptide preparation. Preferably, the collagen peptide preparation produced by one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa is a collagen peptide preparation in which at least 1%, preferably at least 2%, preferably at least 3%, preferably at least 4%, preferably at least 5%, of the prolyl residues, preferably of the lysyl residues, particularly of the prolyl and lysyl residues of the collagen peptides are hydroxylated, preferably in vivo, preferably ex vivo, particularly ex vivo hydroxylated in a pre-lysal form or ex vivo hydroxylated I live in post-lysal form. Preferably, the collagen peptide preparation produced by one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is a collagen peptide preparation in which at most 95%, preferably, at most 90%, preferably, at most 85%, preferably, at most 80%, preferably, at most 75%, preferably, at most 70%, preferably, at most 65%, preferably, at most 60%, preferably, at most 55%, preferably, at most 50%, preferably, at most 45%, preferably, at most 40%, preferably, at most 35%, preferably, at most 30%, preferably, at most 25%, preferably, at most 20%, Preferably, a maximum of 15%, preferably, a maximum of 10%, preferably,at most 5% of the prolyl residues, preferably of the lysyl residues, particularly of the prolyl and lysyl residues of collagen peptides are hydroxylated, preferably hydroxylated in vivo, preferably hydroxylated ex vivo, particularly hydroxylated ex vivo in a pre-lysal form or hydroxylated ex vivo in a post-lysal form. In another preferred embodiment of the present invention, the collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is a collagen peptide preparation in which 0.5 to 80%, preferably, 1 to 75%, preferably, 5 to 70%, preferably, 5 to 65%, preferably, 10 to 60%, preferably, 15 to 55%, preferably, 20 to 50%, preferably, 25 to 50%, preferably, 30 to 50%, preferably, 35 to 50%, preferably, 40 to 50% of the prolyl residues, preferably, of the lysyl residues, particularly of the prolyl and lysyl residues of collagen peptides are hydroxylated, preferably, hydroxylated in vivo, preferably, hydroxylated ex vivo, particularly hydroxylated ex vivo in pre-lysal form or hydroxylated ex vivo in post-lysal form. In a preferred embodiment of the present invention, the collagen peptide preparation produced by one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is a collagen peptide preparation in which the collagen peptides are glycosylated. Preferably, the collagen peptides are glycosylated in vivo, or preferably, glycosylated ex vivo.Preferably at least 1%, preferably at least 2%, preferably at least 3%, preferably at least 4%, preferably at least 5%, preferably at least 6%, preferably at least 7%, preferably at least 8%, preferably at least 9%, preferably at least 10%, preferably at least 15%, preferably at least 20% of the hydroxyl residues are glycosylated, preferably glycosylated in vivo, preferably glycosylated ex vivo. In another preferred embodiment of the present invention, the collagen peptide preparation produced by one of the inventive methods is a collagen peptide preparation in which the collagen peptides are not glycosylated. In a preferred embodiment of the present invention, the collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is an in vivo hydroxylated collagen peptide preparation, i.e., a collagen A preparation. In a preferred embodiment of the present invention, the collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is a non-hydroxylated collagen peptide preparation, i.e., a collagen B preparation. In another preferred embodiment of the present invention, the collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is an ex vivo hydroxylated collagen peptide preparation, i.e., a collagen C or D preparation. The collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa is, preferably, a hydroxylated collagen peptide preparation in a pre-lysal ex vivo form, i.e., before hydrolysis, i.e., a collagen C preparation. According to another preferred embodiment of the present invention, the collagen peptide preparation produced by means of one of the inventive methods mentioned above, in particular, the collagen peptide preparation containing collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa, is a post-lysal ex vivo hydroxylated collagen peptide preparation, i.e., after hydrolysis, i.e., a collagen D preparation. The present invention relates, in particular, also to a collagen peptide preparation, in particular, to a hydroxylated or non-hydroxylated collagen peptide preparation, which was produced by hydrolysis of recombinantly produced collagen peptide in a host cell having a molecular weight in the range of 8 to 100 kDa, the collagen peptide preparation comprising collagen peptides with an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa. The presence of characteristic peptides in the collagen peptide preparation that contribute to its activity can be determined, in particular, by mass spectrometry, preferably by ESI (electrospray ionization) or MALDI (matrix-assisted laser desorption / ionization) mass spectrometry, with the characteristic peptides appearing as peaks in the mass spectrum. In a molecular weight distribution determined by MALDI mass spectrometry, the characteristic peptides have an intensity at least twice, and preferably at least four times, that of their surroundings. Inventive collagen peptide preparations, in particular collagen peptide preparation A, collagen peptide preparation B, collagen peptide preparation C and collagen peptide preparation D, may also additionally comprise characteristic peptides in a size of 1,500 to 3,500 Da. In another preferred embodiment of the invention, the inventive collagen peptide preparations, in particular collagen peptide preparation A, collagen peptide preparation B, collagen peptide preparation C, and collagen peptide preparation D, have at most 5.5%, preferably at most 5%, preferably at most 4.5%, preferably at most 4%, preferably at most 3.5% of collagen peptides with a size of < 500 Da. According to this method, there is advantageously an improvement in the taste of peptide preparations compared to preparations known in the state of the art, thanks to the particularly low proportion of peptides with a size of less than 500 Da, in particular a less bitter taste of collagen peptide preparations. Preferably 35 to 60%, preferably 35 to 55%, preferably 35 to 50%, preferably 36 to 48%, preferably 36 to 46%, preferably 37 to 45%, preferably 38 to 44% of the collagen peptides in the inventive collagen peptide preparations, in particular, collagen peptide preparation A, collagen peptide preparation B, collagen peptide preparation C, and collagen peptide preparation D have a size in the range of 1500 Da to 3500 Da. The inventive collagen preparations, in particular collagen peptide preparation A, collagen peptide preparation B, collagen peptide preparation C and collagen peptide preparation D, preferably comprise a maximum of 2.8%, preferably a maximum of 2.75%, preferably a maximum of 2.7%, preferably a maximum of 2.65%, preferably a maximum of 2.6%, preferably a maximum of 2.55%, preferably a maximum of 2.5%, preferably a maximum of 2.45%, preferably a maximum of 2.4%, preferably a maximum of 2.35%, preferably a maximum of 2.3% of collagen peptides with a size in the range of 7500 Da to 13500 Da. According to a particularly preferred embodiment of the present invention, at least 93%, preferably at least 93.5%, preferably at least 94%, preferably at least 94.5%, preferably at least 95% of the collagen peptides in the inventive collagen peptide preparations, in particular collagen peptide preparation A, collagen peptide preparation B, collagen peptide preparation C, and collagen peptide preparation D, have a size in the range of 500 Da to 7500 Da. frczcnn / Lznz / E / Yi Preferably at least 94.5%, preferably at least 95%, preferably at least 95.5%, preferably at least 95.6%, preferably at least 95.7%, preferably at least 95.8%, preferably at least 95.9%, preferably at least 96%, preferably at least 96.1%, preferably at least 96.2%, preferably at least 96.3%, preferably at least 96.4%, preferably at least 96.5% of the collagen peptides in the inventive collagen peptide preparations, in particular collagen peptide preparation A, collagen peptide preparation B, collagen peptide preparation C, and collagen peptide preparation D, have a size in the range of 500 Da to 13500 Da. In a preferred embodiment, the collagen peptide preparation according to the present invention is administered locally, in particular topically, or systemically, in particular enterally, preferably orally. According to a preferred embodiment of the invention, the collagen peptide preparation is administered as a food supplement. The food supplement is particularly advantageously presented as a solution, suspension, or gel, for example, in an ampoule, or as granules or powder. Thanks to its good solubility, the collagen peptide preparation can be added to various beverages without causing cloudiness. The inventively prepared food supplement, according to a preferred embodiment of the present invention, does not contain, in addition to the collagen peptide preparation, any other proteins or protein hydrolysates. According to one embodiment of the invention, the inventive food supplement does not contain, in addition to the collagen peptide preparation, any other physiologically active components, in particular, no proteins or protein hydrolysates. The invention further relates to a product comprising an inventive collagen peptide preparation and at least one additive. The object of the invention is also a food supplement comprising a collagen peptide preparation and at least one further component, in particular, at least one food-acceptable additive. The collagen peptide preparation can be added, in one modality, to a food or stimulant, for example, a chocolate bar, a protein bar, a cereal bar, milk, dairy products, for example, yogurt, whey or cottage cheese and milk substitute, for example, soy milk, rice milk, almond milk and coconut milk (so called, functional food). The object of the invention is, therefore, also a food or stimulant comprising an inventive collagen peptide preparation. It may also be inventively provided that the collagen peptide preparation is administered in the form of a pharmaceutical composition. The inventive pharmaceutical composition is particularly advantageously administered in the form of tablets, orally dissolving tablets, chewable tablets, capsules, bite-sized capsules, dragees, lozenges, juices, gels, or ointments. The present invention also relates to a pharmaceutical composition comprising an inventive collagen peptide preparation and at least one pharmaceutically permissible additive. In another embodiment, the collagen peptide preparation can be administered in the form of a cosmetic composition. The inventive cosmetic composition is particularly advantageously administered in the form of lotions, ointments, creams, gels, powders, injections, or sprays. The present invention also relates to a cosmetic composition comprising an inventive collagen peptide preparation and at least one skin-compatible additive. Provided that the collagen peptide preparation according to a preferred embodiment of the invention is not used as the sole physiologically active component of a product, in particular a food supplement, food or stimulant, pharmaceutical composition or cosmetic composition, it may be combined with one or more other components that have a favorable effect on general health, in particular on prolonged endurance strength.Such components are preferably selected from the group consisting of vitamin C, B vitamins, D, E, and K, omega-3 fatty acids, omega-6 fatty acids, conjugated linolenic acids, caffeine and its derivatives, guarana extract, green tea extract, epigallocatechin gallate, creatine, L-carnitine, alpha-liponic acid, N-acetylcysteine, NADH, D-ribose, magnesium aspartate, antioxidants such as anthocyanins, carotenoids, flavonoids, resveratrol, glutathione, and superoxide dismutase (SOD), cannabinoids such as cannabidiol (CBD), adaptogens such as Phlodiola rosea, Panax ginseng, Withania somnifera, shiitake, Ganoderma lucidum, and Lepidium meyenii, minerals such as iron, magnesium, calcium, zinc, selenium, and phosphorus, as well as other proteins, hydrolysates, and peptides such as soy protein, wheat and whey protein. In a preferred embodiment of the invention, the collagen peptide preparation is administered in an amount of 1 to 40 g per day, preferably, 1 to 30 g per day, preferably, 1 to 20 g per day, preferably, 1 to 15 g per day, preferably, 2.5 to 30 g per day, preferably, 2.5 to 20 g per day, preferably, 2.5 to 15 g per day, preferably, 2.5 to 10 g per day, preferably, 4 to 15 g per day, preferably, 4 to 12 g per day, more preferably, 5 to 25 g per day, preferably, 5 to 15 g per day, more preferably, 10 to 25 g per day, preferably, 12 to 22 g per day, and, in particular, 12.5 to 20 g per day, most preferably 6 to 15 g per day, in particular 2.5 to 7.5 g per day, preferably 2.5 to 5 g per day. The present invention also relates to an inventive collagen peptide preparation for application in a therapeutic method for preserving and improving bone health, for the prevention and / or treatment of osteoporosis, for the prevention and / or treatment of sarcopenia, for the prevention and / or treatment of degenerative loss of muscle mass, for improving muscle strength, for stimulating fat reduction, and for reducing body weight. The present invention relates in a preferred embodiment, moreover, to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of bone diseases, in particular, osteoporosis. The present invention relates in a preferred embodiment, furthermore, to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of sarcopenia. The present invention relates in a preferred embodiment, moreover, to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of degenerative loss of muscle mass. frczcnn / Lznz / E / Yi The present invention relates in a preferred embodiment, moreover, to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of cartilage diseases, in particular osteoarthritis or arthritis. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for improving muscle strength. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of a pathological condition characterized by reduced mitochondrial activity, in particular, for the prevention and / or treatment of a pathological condition characterized by a decrease in prolonged resistance power. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for stimulating fat reduction. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for reducing body weight. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of degenerative joint diseases, in particular osteoarthritis, rheumatoid arthritis, rheumatic diseases, spondylitis and / or fibromyalgia. In a preferred embodiment, the present invention relates to the preparation of inventive collagen peptide for application in a method for the prevention and / or treatment of tendon or ligament diseases. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of skin diseases, in particular, common psoriasis, acne, atopic dermatitis, chronic pruritus and / or rosacea. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the treatment of injuries, in particular, chronic injuries, acute injuries and / or burn injuries. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of degenerative nerve diseases. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of dementia. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of Alzheimer's disease. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of a pathological condition characterized by a decrease in cognitive ability. In a preferred embodiment, the present invention relates to the preparation of inventive collagen peptide for application in a method for the prevention and / or treatment of diseases related to inadequate functions of the blood-brain barrier, in particular, of the structure and / or function of the cerebral cortex. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of intestinal diseases, in particular, chronic inflammatory bowel diseases. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of diseases of the cardiovascular system, in particular, of the structure and / or function of blood vessels, in particular, the vessel wall, in particular, the prevention and / or treatment of hypertension and / or blood irrigation dysfunctions. In a preferred embodiment, the present invention relates to the preparation of an inventive collagen peptide for application in a method for the prevention and / or treatment of diseases of the dental support structures. The present invention also relates to an inventive collagen peptide preparation for application in a non-therapeutic method for preserving and improving bone health, for preventing osteoporosis, for preventing and / or treating sarcopenia, for preventing degenerative loss of muscle mass, for improving muscle strength, for stimulating fat reduction, for reducing body weight, and / or for preventing degenerative joint diseases. The present invention also relates to an inventive collagen peptide preparation for application in a non-therapeutic method for the optical or structural improvement of the skin, in particular for the reduction of wrinkle formation, improvement of skin elasticity, increase of skin tensile strength, increase of skin moisture content, reduction of cellulite and / or reduction of stretch marks, in particular, pregnancy stretch marks. In another preferred embodiment, the present invention relates to the non-therapeutic use of the inventive collagen peptide preparation to accelerate nail growth and / or reduce nail brittleness. In a preferred embodiment, the present invention further relates to the non-therapeutic use of the inventive collagen peptide preparation for the optical and structural improvement of hair, in particular for improving hair quality, reducing splitting and / or reducing / delaying hair loss. In another preferred embodiment, the present invention relates to the non-therapeutic use of the inventive collagen peptide preparation to increase the number of mitochondria and / or mitochondrial activity. In another preferred embodiment, the present invention relates to the non-therapeutic use of the inventive collagen peptide preparation to enhance long-lasting strength. In another preferred embodiment, the present invention relates to the non-therapeutic use of the inventive collagen peptide preparation to enhance cognitive ability. frczcnn / ίζηζ / Β / γι In a preferred embodiment of the present invention, the inventive collagen peptide preparation is used alone, i.e., without other substances, for application in one of the inventively provided applications. In another embodiment of the present invention, the inventive collagen peptide preparation is used as the sole agent exhibiting biological activity in an inventively provided application. In another preferred embodiment of the present invention, the inventive collagen peptide preparation is used as an agent together with at least one other agent, in particular another biologically active agent, in an inventively provided application. The present invention also relates to a method for the prevention and / or treatment of the indications mentioned above, in particular the therapeutic indications mentioned above, according to which a quantity sufficient for therapeutic purposes of the inventive collagen peptide preparation is administered to the human or animal body, possibly together with an additive. The present invention also relates to a non-therapeutic method for improving muscle strength, increasing muscle mass, stimulating fat reduction, reducing body weight, preserving and / or improving bone health, preserving and / or improving skin health, preserving and / or improving bowel health, preserving and / or improving blood vessel structure, preserving and / or improving the health of the cardiac circulatory system, preserving and / or improving the dental support structure, preserving and / or improving the health of the nails and hair of a human or animal body, preserving and / or increasing the number of mitochondria and / or mitochondrial activity, preserving and / or improving prolonged endurance power, or preserving and / or improving cognitive ability, by administering to the human or animal body at least one inventive collagen peptide preparation. The present invention also relates to an inventive collagen peptide preparation for use in a method for producing films, sheets, and coatings. The coatings may be, for example, paints and varnishes, in particular, paints and varnishes with special optical effects or coatings for producing self-cleaning surfaces. In a preferred embodiment, the term collagen, in the context of the present invention, is understood in the manner customary in the field, as defined, for example, in WO 01 / 34646. In a preferred embodiment, the term collagen refers to collagen types I to XXVII. In another preferred embodiment, the term collagen is understood to mean a peptide comprising the sequence glycineproline, glycine-4-hydroxyproline, or glycine-X-4-hydroxyproline, preferably the peptide comprising the repeating motif (Gly-XY)n, X and Y being any amino acid, preferably proline and 4-hydroxyproline. Particularly preferred, the term collagen is understood to mean a peptide comprising the repeating motif (Gly-Pro-Y)ny / or (Gly-X-Hyp)m, X and Y being any amino acid. The term gelatin, in the context of the present invention, is understood, preferably, in the manner usual in the field, in particular, as defined in document WO 01 / 34646.In the context of the present invention, the term "collagen peptide" preferably means a peptide comprising an amino acid sequence occurring in collagen as defined above. A collagen peptide preferably also means a genetically modified collagen peptide obtained by modifying the amino acid sequence of a naturally occurring collagen peptide. The collagen peptide preparation obtained from the collagen peptide in step (e) of the inventive method preferably demonstrates, in at least one of the in vitro assays for stimulating extracellular matrix protein synthesis in osteoblasts, fibroblasts, and chondrocytes, in particular, at least one, preferably at least two, preferably all of the in vitro assays for stimulating extracellular matrix protein synthesis in osteoblasts.fibroblasts and chondrocytes represented in Examples 3 to 7, in particular, in Examples 3 to 5, a biological activity, preferably the same biological activity as collagen peptide preparations isolated from natural sources, in particular, as collagen peptide preparations produced in a non-recombinant manner, preferably a better biological activity than collagen peptide preparations isolated from natural sources, in particular, as collagen peptide preparations produced in a non-recombinant manner. In the context of the present invention, the term recombinant DNA refers to an artificially produced or manipulated DNA molecule that was produced in vitro using genetic engineering methods. In a preferred embodiment, the recombinant DNA is composed of components from different organisms of origin. In the context of the present invention, the term recombinant collagen peptide or recombinantly produced collagen peptide means a collagen peptide encoded by recombinant DNA. In the context of the present invention, the term expression cassette means a segment of DNA that is responsible for the transcription of the information encoded in this segment into an RNA, in particular an mRNA, and that contains at least one promoter and a protein-coding nucleotide sequence, usually at least one promoter, at least one protein-coding nucleotide sequence and, optionally, a terminator. In the context of the present invention, the term "nucleotide sequence" refers to the nucleotide sequence of a nucleic acid, in particular, a nucleic acid strand, specifically a strand of DNA or RNA. Therefore, a nucleotide sequence should be understood to mean both a unit of information and the DNA or RNA strand that physically embodies this information. In the context of the present invention, an expression system is understood to be a system in which a focused and controlled biological synthesis of proteins can be carried out. The term "expression system" herein inventively comprises both cell-free expression systems, in which the components necessary for the biological synthesis of proteins are not present within a cell (i.e., the biological synthesis of proteins takes place outside a cell), and cell-based expression systems, in which the biological synthesis of proteins takes place within a living cell. A cell-free expression system, in the context of the present invention, is preferably a lysate or an extract of E.cali, insect cells, wheat germ cells, tobacco cells or mammalian cells, in particular CHO cells or rabbit reticulocytes containing the components necessary for the biological synthesis of proteins, in particular, a translation system and a transcription system. In the context of the present invention, a host cell is understood to be a living cell that is capable of expressing peptides or proteins encoded in foreign DNA, in particular, in recombinant DNA. In the context of the present invention, the terms pre-lysal and post-lysal designate a temporal point before and after, respectively, hydrolysis, in particular, before and after, respectively, enzymatic or acid-catalyzed hydrolysis. In the context of the present invention, the term "incubate" refers both to the cultivation of a cell-based expression system, in particular a host cell, and to the action of certain conditions on a cell-free expression system. The terms "obtain the collagen peptide according to step c) of the method" and "obtain from the collagen peptide preparation according to step e) of the method" are inventively understood to mean a method, known to the skillful, for isolating the collagen peptide and the collagen peptide preparation, respectively, from a composition containing several components by means of known isolation methods such as, for example, centrifugation methods, in particular, differential centrifugation and / or density gradient centrifugation, chromatographic methods, in particular, gel filtration chromatography, ion exchange, affinity and / or high-performance liquid chromatography, electrophoresis methods, filtration methods and / or extraction methods, enrichment and purification of the components in question from the composition containing several components being achievable, preferably by the sequential application of several isolation methods. Conditions enabling collagen peptide expression are understood to include, in particular, temperature, pressure, time, light, and the presence or absence of inducers and / or repressors that activate or enhance collagen peptide expression. In a preferred embodiment, collagen peptide expression is carried out within the framework of high-density cell fermentation, particularly under high pressure, preferably high air pressure. The specific conditions enabling collagen peptide expression are familiar to the specialist and depend on the expression system and expression cassette used, particularly the promoter contained therein. Depending on the construction of the expression cassette, collagen peptide expression can be constitutive or inducible. In the context of the present invention, the term "hydrolyzing the collagen peptide under conditions conducive to the production of a collagen peptide preparation" means those conditions, in particular, the type of hydrolysis, optionally the type and quantity of at least the single enzyme used for hydrolysis, pH value, duration of hydrolysis, and temperature of hydrolysis, that are conducive to obtaining collagen peptides with an average molecular weight of 1 to 7 kDa and with a molecular weight in the range of 0.1 to 13.5 kDa of a recombinantly produced collagen peptide with a molecular weight in the range of 8 to 100 kDa. Appropriate conditions for obtaining collagen peptides with an average molecular weight of 1 to 7 kDa and with a molecular weight in the range of 0.1 to 13.5 kDa from a recombinantly produced collagen peptide with a molecular weight in the range of 8 to 100 kDa are indicated, for example, in Example 1. The % indications mentioned in the context of the molecular weight distribution of collagen peptides in inventive collagen peptide preparations refer in each case to % by weight with respect to all collagen peptides contained in the collagen peptide preparation. In the context of the present invention, the expressions "comprising" and "having" are understood to mean that, in addition to the elements explicitly designated by these expressions, there may be other elements not explicitly mentioned. In the context of the present invention, these expressions are also understood to mean that only the explicitly mentioned elements are designated and that there are no additional elements. In this particular embodiment, the meaning of the expression "comprising" and "having" is synonymous with the expression "consisting of." The expressions "comprising" and "having" also include compositions that contain, in addition to the explicitly mentioned elements, other unmentioned elements, which, however, are subordinate in a functional and qualitative sense. In this embodiment, the expressions "comprising" and "having" are synonymous with the expression "essentially consisting of." The expression "and / or" in the context of the present invention means that all members of a group connected by the expression "and / or" manifest themselves both alternatively and cumulatively, in each case, in any arbitrary combination. For the expression "A, B and / or C", this means the following manifestations: a) A or B or C, b) (A and B), c) (A and C), d) (B and C), e) (A and B and C). Additional preferred modalities result from the subordinate claims. BRIEF DESCRIPTION OF THE FIGURES The invention is described below with the help of figures, tables and relevant embodiment examples without restricting the general inventive idea. It is shown in the Figure 1 shows the percent proportions of some collagen peptides from comparative products 1 and 2, as well as from collagen peptide preparations according to examples 1.3, 1.4 and 1.5 in defined molecular weight ranges. Figure 2A is a chromatogram of a 1% solution of comparator product 1. The molecular weight is marked on the abscissa on a logarithmic scale. Figure 2B is a chromatogram of a 1% solution of comparator product 2. The molecular weight is marked on the abscissa on a logarithmic scale. Figure 3A is a chromatogram of a 1% solution of the collagen peptide preparation according to Example 1.3. The molecular weight is marked on the abscissa on a logarithmic scale. Figure 3B is a chromatogram of a 1% solution of the collagen peptide preparation according to Example 1.4. The molecular weight is marked on the abscissa on a logarithmic scale. Figure 4 is a chromatogram of a 1% solution of the collagen peptide preparation according to Example 1.5. The molecular weight is marked on the abscissa on a logarithmic scale. Figure 5 shows a comparison of the stimulation of collagen synthesis in primary human fibroblasts in the absence of a collagen peptide (control 1), in the presence of 0.5 mg / ml of a 100 kDa collagen peptide (control 2), from a non-hydroxylated inventive collagen peptide preparation with an average molecular weight of 1.8 kDa (sample 1), from a non-hydroxylated inventive collagen peptide preparation frczcnn / Lznz / B / Yi with an average molecular weight of 2.4 kDa (sample 2), or from a non-hydroxylated inventive collagen peptide preparation with an average molecular weight of 3.4 kDa (sample 3). Error bars show the standard deviation. Figure 6 shows a comparison of the stimulation of elastin synthesis in primary human fibroblasts in the absence of a collagen peptide (control 1), in the presence of 0.5 mg / ml of a 100 kDa collagen peptide (control 2), an inventive non-hydroxylated collagen peptide preparation with an average molecular weight of 1.8 kDa (sample 1), an inventive non-hydroxylated collagen peptide preparation with an average molecular weight of 2.4 kDa (sample 2), or an inventive non-hydroxylated collagen peptide preparation with an average molecular weight of 3.4 kDa (sample 3). Error bars show the standard deviation. Figure 7 shows a comparison of the stimulation of proteoglycan synthesis in primary human fibroblasts in the absence of a collagen peptide (control 1), in the presence of 0.5 mg / ml of a 100 kDa collagen peptide (control 2), an inventive non-hydroxylated collagen peptide preparation with an average molecular weight of 1.8 kDa (sample 1), an inventive non-hydroxylated collagen peptide preparation with an average molecular weight of 2.4 kDa (sample 2), or an inventive non-hydroxylated collagen peptide preparation with an average molecular weight of 3.4 kDa (sample 3). Error bars show the standard deviation. Figure 8 shows a comparison of the stimulation of collagen synthesis in primary human fibroblasts in the absence of a collagen peptide (control 1), in the presence of 0.5 mg / ml of a hydroxylated inventive collagen peptide with an average molecular weight of 7 kDa (sample 4), a hydroxylated inventive collagen peptide preparation with an average molecular weight of 5.6 kDa (sample 5), or a hydroxylated inventive collagen peptide preparation with an average molecular weight of 1.3 kDa (sample 6). Error bars show the standard deviation. Figure 9 shows a comparison of the stimulation of elastin synthesis in primary human fibroblasts in the absence of a collagen peptide (control 1), in the presence of 0.5 mg / ml of a hydroxylated inventive collagen peptide with an average molecular weight of 7 kDa (sample 4), a hydroxylated inventive collagen peptide preparation with an average molecular weight of 5.6 kDa (sample 5), or a hydroxylated inventive collagen peptide preparation with an average molecular weight of 1.3 kDa (sample 6). Error bars show the standard deviation. Figure 10 shows a comparison of the stimulation of proteoglycan synthesis in primary human fibroblasts in the absence of a collagen peptide (control 1), in the presence of 0.5 mg / ml of a hydroxylated inventive collagen peptide with an average molecular weight of 7 kDa (sample 4), a hydroxylated inventive collagen peptide preparation with an average molecular weight of 5.6 kDa (sample 5), or a hydroxylated inventive collagen peptide preparation with an average molecular weight of 1.3 kDa (sample 6). Error bars show the standard deviation. DETAILED DESCRIPTION OF THE INVENTION Examples: Example 1 - the production of collagen peptides: 1.1 Hydrolysis of a non-hydroxylated bovine collagen peptide, produced recombinantly in Pichia pastoris with a size of 45 kDa using neutral protease A 0.789% collagen solution was tempered in a 50 ml bottle in a cryostat, initially at a temperature of 50°C. Then, 200 ppm of CaCl₂x2H₂O (relative to the dry matter (DM) of the collagen) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 6.2 with a 10% NaOH solution. In the next step, 0.8% Sumizyme BNP-L (relative to the DM of the collagen) was added to the collagen solution. The average molecular weight of collagen peptides after a hydrolysis duration of 180 min was determined to be 5.04 kDa. 1.2 Hydrolysis of a non-hydroxylated bovine collagen peptide, recombinantly produced in Pichia pastoris with a size of 45 kDa, using alkaline protease A 0.792% collagen solution was tempered in a 50 ml bottle in a cryostat, initially at a temperature of 63°C. Then, 200 ppm of CaCl₂x·2H₂O (relative to the collagen solution) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.75 with a 10% NaOH solution. In the next step, 0.3% Alcalase (relative to the collagen solution) was added to the collagen solution at 2.4 L. The average molecular weight of collagen peptides after a hydrolysis duration of 180 min was determined to be 3.01 kDa. 1.3 Hydrolysis of a recombinantly produced, non-hydroxylated human collagen peptide of 25 kDa size in Pichia pastoris with alkaline protease A 2.85% collagen solution was tempered in a 50 ml bottle in a cryostat, initially at a temperature of 63°C. Then, 200 ppm of CaCl₂x2H₂O (relative to the dry matter (DM) of the collagen) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.6 with a 10% NaOH solution. In the next step, 0.3% Alcalase (relative to the DM of the collagen) was added to the collagen solution. The average molecular weight of collagen peptides after a hydrolysis duration of 45 min was determined to be 1.8 kDa. 1.4 Hydrolysis of a recombinantly produced, non-hydroxylated human collagen peptide of 100 kDa size in Pichia pastoris with alkaline protease A 2.85% collagen solution was tempered in a 50 ml bottle in a cryostat, initially at a temperature of 63°C. Then, 200 ppm of CaCl₂x2H₂O (relative to the collagen solution) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.6 with a 10% NaOH solution. In the next step, 0.4% Alcalase (relative to the collagen solution) was added to the collagen solution. The solution, after a hydrolysis time of 45 min, contained collagen peptides with an average molecular weight of 2.4 kDa. The inventive collagen peptide preparation obtained was used in Example 6 as Sample 2. 1.5 Hydrolysis of a recombinantly produced, non-hydroxylated human collagen peptide of 100 kDa size in Pichia pastoris with alkaline protease A 1.5% collagen solution was tempered in a 50 ml bottle in a cryostat at a temperature of 63°C. Then, 200 ppm of CaCl₂·2H₂O (relative to the collagen solution) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.6 with a 10% NaOH solution. In the next step, 0.3% Alcalase (relative to the collagen solution) was added to the collagen solution. The average molecular weight of the collagen peptides after a hydrolysis time of 60 min was determined to be 1.8 kDa. The inventive collagen peptide preparation obtained was used in Example 6 as Sample 1. 1.6 Hydrolysis of a recombinantly produced, non-hydroxylated human collagen peptide of 25 kDa size in Pichia pastoris with alkaline protease A 2.85% collagen solution was tempered in a 50 ml bottle in a cryostat, initially at a temperature of 63°C. Then, 200 ppm of CaCl₂x2H₂O (relative to the collagen solution) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.6 with a 10% NaOH solution. In the next step, 0.1% Alcalase (relative to the collagen solution) was added to the collagen solution at 2.4 L. The average molecular weight of the collagen peptides after a hydrolysis time of 60 min was 3.4 kDa. The inventive collagen peptide preparation obtained was used in Example 6 as Sample 3. 1.7 Hydrolysis of a hydroxylated collagen peptide of bovine origin, recombinantly produced in Pichia pastoris with a size of 45 kDa using alkaline protease A 5.53% collagen solution was tempered in a 250 ml glass bottle in a cryostat, initially at a temperature of 55°C. Then, 200 ppm of CaCl₂x2H₂O (relative to the collagen solution) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.59 with a 2% NaOH solution. In a subsequent step, 0.2% Alcalase (relative to the collagen solution) was added to the collagen solution at 2.4 L. The average molecular weight of the collagen peptides after a hydrolysis time of 150 min was determined to be 7 kDa. The resulting inventive collagen peptide preparation was used in Example 7 as Sample 4. 1.8 Hydrolysis of a hydroxylated collagen peptide of bovine origin, recombinantly produced in Pichia pastoris with a size of 45 kDa using alkaline protease A 5.00% collagen solution was tempered in a 100 ml glass bottle in a cryostat, initially at a temperature of 55°C. Then, 200 ppm of CaCl₂x2H₂O (relative to the collagen solids concentration) was added to the collagen solution at this temperature, and the pH of the solution was adjusted to 7.60 with a 2% NaOH solution. In the next step, 0.25% NZ₃7071 (relative to the collagen solids concentration) was added to the collagen solution. The average molecular weight of the collagen peptides after a hydrolysis time of 240 min was 5.6 kDa. The inventive collagen peptide preparation obtained was used in Example 7 as Sample 5. 1.9 Hydrolysis of a hydroxylated collagen peptide of bovine origin, recombinantly produced in Pichia pastoris with a size of 45 kDa using alkaline protease frczcnn / Lznz / B / Yi Starting from the collagen peptide hydrolysate obtained according to example 1.7, the higher molecular weight components of the hydrolysate were removed using a concentrator (e.g., Vivaspin 20) with a 5000 Da size exclusion membrane. The average molecular weight of 1.3 kDa was determined for the collagen peptides thus obtained. The inventive collagen peptide preparation was used in Example 7 as Sample 6. 1.10 Gel chromatographic analysis of collagen peptide hydrolysates The molecular weight distribution of the collagen peptide hydrolysates obtained in Examples 1.3 to 1.5, as well as two commercially available comparator products with average molecular weights of 2.3 kDa and 1.7 kDa, were determined by gel filtration chromatography (Knauer, Germany). Statistical analysis was performed using WinGPC software (PSS GmbH, Mainz, Germany). The following parameters were used for gel filtration chromatography: Stationary phase: TSK 2000 SW XL (TOSOH Bioscience GmbH) Mobile phase: 0.4 mol / l sodium dihydrogen phosphate, pH 5.3 Flow rate: 0.5 ml / min Calibration standard: Defined type 1 collagen fragments (FILK) Detection: UV detection at 214 nm (Knauer) Sample concentration: 1% For the different collagen peptide hydrolysates, the proportions in percent represented in Table 1 and Figure 1 resulted from individual collagen peptides in defined molecular weight ranges. Table 1: Evaluation of the percentage proportions of individual collagen peptides in defined molecular weight ranges. The analysis was performed by gel filtration chromatography using defined type 1 collagen peptide standards. frczcnn / ίζηζ / Β / γι Comparative product 1 2.3 kDa Comparative product 2 1.7 kDa Example 1.3 Example 1.4 Example 1.5 Molecular weight range of individual peptides in Da % by weight % by weight % by weight % by weight % by weight % by weight < 500 5.81 13.09 2.72 2.47 3.26 1500 - 500 43.63 50.84 45.78 39.69 47.84 3500 - 1500 31.87 25.52 43.67 40.82 39.29 7500 - 3500 15.63 8.93 7.64 16.74 9.23 13500 - 7500 2.88 1.41 0.19 2.28 0.38 >13500 0.2 0.21 0 0 0 Figures 2A to 4 show the chromatograms for each case of a 1% solution of the comparative products and of the collagen peptide preparations according to Examples 1.3 to 1.5. Thanks to the narrower molecular weight distribution, the absence of higher molecular weight peptides, and the inventive execution of the hydrolysis, the proportion of peptides > 500 Da can be significantly reduced, yet a product with an average molecular weight below 1500 kDa can be obtained. At the same time, the amount of peptides in the preferred size range of 1500 to 3500 Da was increased. While the specialist characterizes peptides > 1500 Da as taste-neutral, it is precisely the peptides with a molecular weight < 500 Da that contribute to the bitter taste of the collagen peptide products. Avoiding the generation of such peptides is another advantage for producing collagen peptides that are sensorially and organoleptically excellent and classified by consumers as having a neutral flavor. The same applies to products with a higher average molecular weight in the 3 to 7 kDa range. It can be deduced from the aforementioned embodiment examples that, thanks to the inventive method and the use of uniform recombinant collagen fragments as starting material for hydrolysis, it is possible to form preferred individual peptides within a narrow molecular weight distribution that has characteristic peaks, depending on the selection of hydrolysis conditions, usually between 4 and 6 (Fig. 3A, Fig. 3B, Fig. 4). The formation of these individual peptides can be precisely controlled by selecting the starting fragment and also by the hydrolysis conditions, which is almost impossible if animal starting material is used because of its lack of homogeneity. Example 2 - ex vivo hydroxylation of collagen fragments For the post-translational modification (hydroxylation of proline residues) of collagen fragments ex vivo, a 4-OH prolyl hydroxylase (P4H) was used in the presence of the cofactors α-ketoglutarate, iron(II) ions, and O2. The use of non-specific hydroxylases is also possible. For this purpose, 8 mM of the collagen fragment was incubated under shaking (300 RPM) at 37°C in a temperature-controlled mixer for 14–18 hours in the presence of 14 mM α-ketoglutarate, 0.5 mM iron(II) sulfate, and 1.5 mM L-ascorbic acid in 50 mM MES buffer (pH 6.5) and an enzyme solution in a total volume of 1 mL. Alternatively, the incubation can also be carried out in an incubator under the aforementioned conditions. Example 3 - osteoblast activity (particularly bone health): To analyze the biological activity of the inventive collagen peptide preparation in terms of bone health maintenance and the prevention and treatment of bone diseases, its stimulatory effect on the synthesis of matrix proteins and enzymes involved in matrix construction and mineralization by osteoblasts in vitro is investigated. This is done by determining the expression of the corresponding mRNA using real-time PCR and a semi-quantitative evaluation (compared to a control without collagen hydrolysate). Human osteoblasts are first isolated from knee joints by incubating bone material under vigorous shaking at 37°C for 1 h in Hanks' solution, supplemented with 7 mg / ml of hyaluronidase type I and III-S and 5 mg / ml of pronase. Disintegration then continues at 37°C for 3 to 5 h in Hanks' solution, supplemented with 16 mg / ml of CLS IV collagenase. The resulting primary osteoblasts are cultured after enzymatic disintegration in Ham's F12 medium, supplemented with 10% fetal calf serum, 20 U / ml of penicillin streptomycin, 50 pg / ml of partricin, 0.05 mg / ml of ascorbic acid, and 0.15 mg / ml of glutamine. The frczcnn / Lznz / B / Yi primary osteoblasts (Article No. C-12760; 2019) for biological activity research can also be purchased from PromoCell GmbH, Heidelberg, Germany.The cell culture is then performed in Ham's F12 medium supplemented with 10% fetal calf serum, 20 U / ml penicillin streptomycin, 50 pg / ml partricin and 0.15 mg / ml glutamine. For the investigation of biological activity, single-layer cell cultures of isolated human osteoblasts are incubated for 24 h in a medium supplemented with 0.5 mg / ml of the collagen peptide preparation in question. A control is incubated in each case in a medium without the preparation. The respective mRNA expression is then determined. Example 4 - fibroblast activity (particularly skin health): Example 4.1 stimulation of mRNA synthesis: The stimulation of collagen (type I) and proteoglycan synthesis Biglykan and Versican is investigated in vitro in human dermal fibroblasts (skin cells). The cells are incubated for 24 hours with 0.5 mg / ml of a low molecular weight collagen peptide preparation and an inventive preparation, respectively, and then the expression of collagen RNA, Biglykan RNA, and Versican RNA is determined by real-time PCR and evaluated semi-quantitatively (relative to a control without preparation). Example 4.2 - stimulation of connective tissue protein synthesis: To determine the stimulation of connective tissue protein synthesis by collagen peptide preparations, primary human dermal fibroblasts are cultured after enzymatic digestion in HAM F12 medium, comprising 10% FCS, 20 U / ml penicillin streptomycin, 50 pg / ml partricin, 0.05 mg / ml ascorbic acid, and 0.15 mg / ml glutamine. After reaching 80% confluence, the culture medium is replaced with a medium without collagen peptide (control) or with 0.5 mg / ml of a test collagen peptide preparation, and the primary human fibroblasts are incubated for at least 14 days, preferably 14 to 21 days, and in particular 14 days, in the medium in question. The expression of the different connective tissue proteins can then be determined by means of appropriate assays (see, for example, Examples 6 and 7) and evaluated. Example 5 - chondrocyte activity (in particular, cartilage health): Porcine and human chondrocytes, respectively, were isolated from cartilage tissue using standard methods and seeded at a density of approximately 350,000 cells / cm² on culture plates. Ham's F12 medium, containing 10% fetal calf serum, 10 pg / ml gentamicin, and 5 pg / ml amphotericin B, was used as the culture medium. Alternatively, 10 pg / ml penicillin streptomycin could be used instead of 10 pg / ml gentamicin. Culture was performed at 37°C in a reduced-oxygen atmosphere (5% O₂, 5% CO₂, and 90% N₂). Determination of the biological synthesis of collagen: The quantification of collagen synthesized by chondrocytes (essentially type II) is performed by radioactive labeling with 14C-proline which is incorporated into the collagen. Radioactive 14C-proline is first added to the culture medium, and chondrocytes are cultured under these conditions until the time of determination. To distinguish between incorporated and unincorporated 14C-proline during detection, the culture medium containing the isotope is replaced with pure culture medium for 3 days. The culture medium is then discarded, and the adherent cell layer is mixed with distilled water to disrupt the cell membranes through osmotic stress and release unbound cytosolic 14C-proline. Cell fragments, along with the synthesized extracellular matrix, are centrifuged to form pellets. These pellets are resuspended in fresh distilled water and mixed with a scintillation xylene cocktail. The amount of collagen synthesized can then be quantified by detecting 14C-proline using a beta counter. Quantification can alternatively be carried out using the Sircol Collagen Assay Kit (article number 054S5000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions (see examples 6 and 7). Determination of the biological synthesis of proteoglycan: The quantification of proteoglycans synthesized by chondrocytes is carried out by staining with alcian blue and photometric determination of glycosaminoglycans (GAGs) that are components of proteoglycans. To determine the GAG ​​content in the cell culture, the culture medium is first discarded, and the adherent cell layer is washed with PBS buffer (pH 7). The cells are then fixed at 4°C for 2 hours in a 10% formaldehyde solution in PBS. After formaldehyde removal, alcian blue staining reagent (5% alcian blue in 3% acetic acid) is applied to the cell layer, and it is incubated overnight at 4°C. Unbound alcian blue is discarded, and the cell layer is carefully washed three or four times with PBS. GAG complexes are then separated from the cell layer by adding an acidic guanidine solution (8 mol / L). The amount of glycosaminoglycans can then be quantified photometrically at a wavelength of 620 nm. Quantification can alternatively be carried out using the Blyscan Glycosaminoglycan Assay Kit (Article No. 054B3000, 2019, tebu-bio, Offenbach, Germany, and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions (see examples 6 and 7). Example 6 - Stimulation of collagen, elastin and proteoglycan synthesis in primary human fibroblasts by non-hydroxylated collagen peptide preparations. Inventives: For the determination of the stimulation of collagen, elastin and proteoglycan synthesis, primary human dermal fibroblasts were incubated according to example 4.2 for a period of at least 14 days, preferably 14 to 21 days, in particular 14 days in a medium without collagen peptide (control 1) and in the presence of 0.5 mg / ml of a 100 kDa collagen peptide (control 2), of a collagen peptide preparation with an average molecular weight of 1.8 kDa (sample 1), of a collagen peptide preparation with an average molecular weight of 2.4 kDa (sample 2) and of a collagen peptide preparation with an average molecular weight of 3.4 kDa (sample 3). Example 6.1 - determination of the stimulation of collagen synthesis The determination of collagen synthesis by primary human dermal fibroblasts was carried out using a Sircol Collagen Assay Kit (article number 054S5000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions. The assay results are shown in Table 2 and Figure 5. frczcnn / Lznz / B / Yi Table 2: Determination of optical density (OD) at a wavelength of 450 nm for the determination of collagen synthesis according to the Sircol Collagen Assay (tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively). frczcnn / Lznz / B / Yi Control 1 Control 2 (Molecular weight = 100 kDa) Sample 1 (Average molecular weight = 1.8 kDa) Sample 2 (Average molecular weight = 2.4 kDa) Sample 3 (Average molecular weight = 3.4 kDa) Average (OD450) 1 1.01 1.2 1.24 1.21 Standard deviation 0 0.01 0.07 0.1 0.06 Example 6.2 - determination of the stimulation of elastin synthesis The determination of elastin synthesis by primary human dermal fibroblasts was carried out using a Fastin Elastin Assay (article number 054S2000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions. The assay results are shown in Table 3 and Figure 6. Table 3: Determination of optical density (OD) at a wavelength of 450 nm for the determination of elastin synthesis according to the Fastin Elastin Assay (tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively). Control 1 Control 2 (Molecular weight = 100 kDa) Sample 1 (Average molecular weight = 1.8 kDa) Sample 2 (Average molecular weight = 2.4 kDa) Sample 3 (Average molecular weight = 3.4 kDa) Average (OD450) 1 0.96 1.28 1.25 1.38 Standard deviation 0 0.22 0.13 0.02 0.3 Example 6.3 - Determination of the stimulation of glycosaminoglycan synthesis The determination of glycosaminoglycan synthesis by primary human dermal fibroblasts was carried out using a Blycsan Glycosaminoglycan Assay (article number 054B3000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions. The assay results are shown in Table 4 and Figure 7. Table 4: Determination of optical density (OD) at a wavelength of 450 nm for the determination of glycosaminoglycan synthesis according to the Blycsan Glycosaminoglycan Assay (tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively). Control 1 Control 2 (molecular weight = 100 kDa) Sample 1 (average molecular weight = 1.8 kDa) Sample 2 (average molecular weight = 2.4 kDa) Sample 3 (average molecular weight = 3.4 kDa) Average (OD450) 1 1 1.28 1.26 1.2 Standard deviation 0 0.09 0.08 0.08 0.06 Example 7 - stimulation of collagen, elastin and proteoglycan synthesis in primary human fibroblasts by inventive hydroxylated collagen peptide preparations: For the determination of the stimulation of collagen, elastin and proteoglycan synthesis, primary human dermal fibroblasts were incubated according to example 4.2 for a period of at least 14 days, preferably 14 to 21 days, in particular 14 days in a medium without collagen peptide (control 1) and in the presence of 0.5 mg / ml of a 7.0 kDa collagen peptide (sample 4), a collagen peptide preparation with an average molecular weight of 5.6 kDa (sample 5) and a collagen peptide preparation with an average molecular weight of 1.3 kDa (sample 6). Example 7.1 - determination of the stimulation of collagen synthesis The determination of collagen synthesis by primary human dermal fibroblasts was carried out using a Sircol Collagen Assay Kit (article number 054S5000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions. The assay results are shown in Table 5 and Figure 8. The mean value determined for the untreated control (control 1) was normalized to 1, as per standard. Table 5: Determination of optical density (OD) for the determination of collagen synthesis according to the Sircol Collagen Assay (tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively). frczcnn / Lznz / B / Yi Control 1 Sample 4 (average molecular weight = 7.0 kDa) Sample 5 (average molecular weight = 5.6 kDa) Sample 6 (average molecular weight = 1.3 kDa) Average 1 1.35 1.36 1.39 Standard deviation 0 0.16 0.1 0.09 Example 7.2 - determination of the stimulation of elastin synthesis The determination of elastin synthesis by primary human dermal fibroblasts was carried out using a Fastin Elastin Assay (article number 054S2000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions. The assay results are shown in Table 6 and Figure 9. The average value determined for the untreated control (control 1) was normalized to 1, as per standard. Table 6: Determination of optical density (OD) at a wavelength of 450 nm for the determination of collagen synthesis according to the Fastin Elastin Assay (tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively). Control 1 Sample 4 (average molecular weight = 7.0 kDa) Sample 5 (average molecular weight = 5.6 kDa) Sample 6 (average molecular weight = 1.3 kDa) Average 1 1.32 1.33 1.31 Standard deviation 0 0.11 0.07 0.04 Example 7.3 - Determination of the stimulation of glycosaminoglycan synthesis The determination of glycosaminoglycan synthesis by primary human dermal fibroblasts was carried out using a Blycsan Glycosaminoglycan Assay (article number 054B3000, 2019, tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively) according to the manufacturer's instructions. The assay results are shown in Table 7 and Figure 10. The average value determined for the untreated control (control 1) was normalized to 1, as per standard. Table 7: Determination of optical density (OD) for the determination of glycosaminoglycan synthesis according to the Blycsan Glycosaminoglycan Assay (tebu-bio, Offenbach, Germany and Biocolor Ltd., UK, respectively). Control 1 Sample 4 (average molecular weight = 7.0 kDa) Sample 5 (average molecular weight = 5.6 kDa) Sample 6 (average molecular weight = 1.3 kDa) Average 1 1.37 1.41 1.4 Standard deviation 0 0.15 0.11 0.12 frczcnn / Lznz / B / Yi

Claims

1. A method for producing a collagen peptide preparation containing recombinant collagen peptides, the method being characterized in that it comprises the following steps: a) providing an in vitro expression system including at least one expression cassette, the expression cassette including at least one nucleotide sequence encoding a collagen peptide having a molecular weight in the range of 8 to 100 kDa; b) incubating the expression system under conditions allowing expression of the collagen peptide; c) obtaining the collagen peptide; d) hydrolyzing the collagen peptide under conditions resulting in the production of a collagen peptide preparation including collagen peptides having an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa; and e) obtaining the collagen peptide preparation.

2. The method according to claim 1, further characterized in that the expression system is a host cell selected from the group consisting of bacterial cells, yeast cells, fungal cells, mammalian cells, insect cells, and plant cells.

3. The method according to any of the preceding claims, further characterized in that the collagen peptide encoded by the nucleotide sequence is a collagen peptide from a vertebrate, in particular a mammal, a bird, a fish, an amphibian, a reptile, or a non-vertebrate animal.

4. The method according to any of the preceding claims, further characterized in that the expression system is a host cell that is capable of hydroxylating proline residues, Usine residues, or proline and Usine residues of the expressed collagen peptide.

5. The method according to claim 4, further characterized in that the host cell includes at least one expression cassette comprising a polynucleotide sequence encoding a prolyl-4-hydroxylase, and an in vivo hydroxylated collagen peptide preparation obtained in step e) of the method.

6. The method according to claim 4 or 5, further characterized in that the host cell includes at least one expression cassette having a polynucleotide sequence encoding lysylhydroxylase, and an in viva hydroxylated collagen peptide preparation obtained in step e) of the method.

7. The method according to any of claims 1 to 3, further characterized in that the expression system is not capable of causing hydroxylation of proline residues, lysine residues or proline and lysine residues of the expressed collagen peptide.

8. The method according to claim 7, further characterized in that the collagen peptide obtained in step c) of the method is hydroxylated in a step x1) of the method, prior to the execution of step d) of the method, and in step e) of the method a hydroxylated collagen peptide preparation is obtained in ex vivo pre-lysal form. frczcnn / ίζηζ / E / γι 9. The method according to claim 7, further characterized in that the collagen peptide preparation produced in step d) of the method is hydroxylated in a step x2) of the method, after the execution of step d) of the method, and in step e) of the method a hydroxylated collagen peptide preparation is obtained in ex vivo post-lysal form.

10. The method in accordance with any of the preceding claims, further characterized in that the hydrolysis is an enzymatic or acid-catalyzed hydrolysis.

11. A collagen peptide preparation characterized in that it is produced by one of the methods as claimed in claims 1 to 10.

12. A collagen peptide preparation characterized in that it is produced by hydrolysis of recombinantly produced collagen peptide in a host cell having a molecular weight in the range of 8 to 100 kDa; the collagen peptide preparation includes collagen peptides having an average molecular weight of 1 to 7 kDa and a molecular weight in the range of 0.1 to 13.5 kDa.

13. The preparation of collagen peptide according to any of claims 11 or 12, further characterized in that it is non-hydroxylated, partially hydroxylated, or fully hydroxylated.

14. The collagen peptide preparation according to any of claims 11 to 13, further characterized in that the collagen peptide preparation is an ex vivo hydroxylated collagen peptide preparation in pre-lysal form or an ex vivo hydroxylated collagen peptide preparation in post-lysal form.

15. The collagen peptide preparation as claimed in any of claims 11 to 14, for use in a method for preserving and improving bone health; for preventing and / or treating osteoporosis; for preventing and / or treating sarcopenia; for preventing and / or treating degenerative loss of muscle mass; for improving muscle strength; for preventing and / or treating a pathological condition characterized by decreased mitochondrial activity; in particular, for preventing and / or treating a pathological condition characterized by decreased endurance power; for stimulating fat reduction; for reducing body weight; and / or for preventing and / or treating degenerative joint diseases; for preventing and / or treating cartilage diseases; for preventing and / or treating tendon and ligament diseases; for preventing and / or treating skin diseases; for treating injuries;to prevent and / or treat degenerative nerve diseases; to prevent and / or treat dementia; to prevent and / or treat Alzheimer's disease; to prevent and / or treat a pathological condition characterized by a decline in cognitive ability; to prevent and / or treat diseases related to dysfunctions of the blood-brain barrier; to prevent and / or treat intestinal diseases; to prevent and / or treat diseases of the cardiovascular system; and / or to prevent or treat diseases of the dental support structures.

16. Non-therapeutic use of a collagen peptide preparation as claimed in any of claims 11 to 14, for optically and structurally improving the skin; for accelerating nail growth and / or reducing nail brittleness; for optically and structurally improving hair; for increasing the number of mitochondria and / or mitochondrial activity; for improving prolonged endurance power and / or for improving cognitive ability.

17. A product characterized in that it comprises a collagen peptide preparation as claimed in any of claims 11 to 14, and at least one additive.

18. A food supplement characterized in that it comprises a collagen peptide preparation as claimed in any of claims 11 to 14, and at least one food-acceptable additive. 5 19. A pharmaceutical composition characterized in that it comprises a collagen peptide preparation as claimed in any of claims 11 to 14, and at least one pharmaceutically acceptable additive.

20. A cosmetic product characterized in that it comprises a collagen peptide preparation as claimed in any of claims 11 to 14, and at least one skin-compatible additive 10.