Method for obtaining native type ii collagen of avian origin

专利摘要:
The invention relates to a method for obtaining native type II collagen from chicken cartilage, useful for preventing or alleviating symptoms of rheumatoid arthritis in humans and in mammals in general. The method describes the steps for obtaining, sanitising, drying and crushing said material to be able to use same innocuously in food supplements. The method generates a microbiologically innocuous, pathogen-free product that can be dispensed without risks, for consumption in formulations.
公开号:ES2748074A1
申请号:ES201990089
申请日:2018-03-15
公开日:2020-03-12
发明作者:Kilian Alonso Aranda
申请人:Olnatura SA de CV；
IPC主号:

专利说明:

[0001]
[0002] Process for obtaining native type II collagen of avian origin
[0003]
[0004] Brief description of the invention
[0005]
[0006] Technical field of the invention.
[0007]
[0008] The invention relates to a process for obtaining native type II collagen with adequate microbiological quality from chicken cartilage useful for preventing or alleviating symptoms of rheumatoid arthritis in humans and in mammals in general.
[0009]
[0010] Background of the Invention
[0011]
[0012] Collagen works as a lubricant in the joints, preventing direct friction between two bones. As the disease progresses, and the amount of collagen in a joint decreases, the bones begin to rub and wear down.
[0013]
[0014] The literature notes that a relevant factor in the pathogenesis of rheumatoid arthritis and osteoarthritis is the body's autoimmune response.
[0015]
[0016] The apparent origin of this problem is the presence of the Epstein-Barr virus, which has an amino acid sequence identical to that of human type II collagen. When the body generates the antibodies to attack this virus, they also attack collagen II itself. Chicken type II collagen shares some antigenic regions with the same collagen in humans.
[0017]
[0018] The effect of administering type II collagen activates a process known as oral tolerization. This tolerization refers to the observation that when a protein is administered orally, immunization is generated with the protein leading to a state of systemic hyporesponsiveness or de-sensitization to the immune factor.
[0019]
[0020] Antibodies to this collagen have a role in the referred pathogenesis, therefore their administration can lead to the induction of immune tolerance to this collagen.
[0021]
[0022] Chicken cartilage contains, among other types of collagen, type II collagen, in its form native, that is, with its quaternary helix-shaped structure.
[0023]
[0024] Chicken cartilage, specifically the sternum or keel thereof, due to the presence of this type of collagen, is an adequate source of the material for its use.
[0025]
[0026] Several studies have identified the beneficial potential of using this chicken type II collagen, administered orally, to alleviate discomfort associated with the aforementioned condition.
[0027]
[0028] There are several publications that refer to this type of effect on individuals with rheumatoid arthritis and osteoarthritis.
[0029]
[0030] There are several methodologies for processing chicken cartilage in the literature, many of them with the use of sodium hypochlorite, others with hydrogen peroxide, and others with cartilage radiation ( citations: 1,2). Cartilage is processed in various methodologies, including the use of the cartilage itself, the same cartilage suspended in liquids with different ingredients, or processed, dry and ground cartilage ( citations: 3.4).
[0031]
[0032] The processes referred to here generate a product within microbiological specifications, but the final product is left with an intermediate or close to high microbial load with respect to the general specifications, a load that can undergo changes over time, leading to the product falling out of the specifications. The process described here makes adjustments to the sanitization conditions, through a process with a higher concentration of the oxidizing agent and a longer exposure time, in order to find that the finished product meets a lower microbial load, which reduces the risks of falling out of specification over time. This is particularly important because given the animal origin of the product, there may be risks in this regard. The resulting process may take a little longer, but gives greater confidence in the microbiological quality of the finished product.
[0033]
[0034] Brief description of the invention
[0035]
[0036] The process of the present invention involves obtaining sanitized, dry and ground cartilage for use as a supplement to alleviate discomfort for individuals with rheumatoid arthritis and osteoarthritis.
[0037]
[0038] It is important to note that hydrolyzed collagen is used commercially for multiple uses, like cosmetic. The product obtained from this technique is not considered for these applications.
[0039]
[0040] The inventors identified that only a powerful oxidant, such as hydrogen peroxide, is necessary in higher concentrations, and with longer times than those known in the state of the art, but without generating harmful vapors for the health of the person. in charge of the process, to comply with the microbiological specifications of the product as input for food supplements.
[0041]
[0042] The process of the present invention ensures the total elimination of any pathogenic microorganism, and reduces the microbial count of aerobic mesophiles and of fungi and yeasts, to levels well below that specified by the corresponding standards, to ensure that this is not a risk. for the health of those who consume it.
[0043]
[0044] Other techniques that seek to obtain a dry product, use lower concentrations of hydrogen peroxide and less exposure time. In the case of the process of the present invention, the advantage of using stronger conditions allows us to obtain a product consistently within microbiological specifications, without affecting proteins, since it is the oxidizing agent that does not cause damage to the protein itself, even in concentrations greater. A relevant factor of the process of the present invention is that it worked with a maximum concentration of 4.5%, because above this value, the solution generates harmful vapors for the health of the personnel who process it. The aspect of the finished product itself, already dry and ground, is of a white to beige powder, which facilitates its mixing to make the final presentation for consumption, without the presence of mottling or tone variations, since the excipients frequently used in industry they are shades of white to beige too.
[0045]
[0046] With the concentrations, times and temperatures of the present process, a product can be obtained within microbiological specifications, without subjecting the protein to conditions that could cause significant degradation. For these purposes, it is necessary to dry said protein at a relatively low temperature of 40 ° C or less, in order to avoid damaging it.
[0047]
[0048] Detailed description of the invention.
[0049]
[0050] The sternum of a chicken obtained from a processing facility approved by the health authorities, is a hygienic source of collagens, particularly native type II collagen.
[0051]
[0052] It is of utmost importance to maintain the cold chain in the management of this input, from its supply to its processing. This is due to the presence of proteins such as collagen, which are sensitive to temperature, and due to the risk of microbiological contamination that occurs in any input of animal origin with high temperatures.
[0053]
[0054] From the cutting of the chicken sternum, its storage, transport and processing, until the humidity of the material is reduced, it is necessary that the temperature of the input does not exceed 4 ° C.
[0055]
[0056] This input is hydrated, washed and previously cut to remove impurities from the plant process, to obtain said sternum free of meat and other impurities. It is important to use purified water that is within microbiological specifications for the entire process.
[0057]
[0058] If the cartilage is not processed immediately, it must be stored under refrigeration, at temperatures no higher than 4 ° C.
[0059]
[0060] The cartilage is subsequently sanitized with a sanitizing agent, in this case hydrogen peroxide, in concentrations ranging from 3.5% to 4.5%, and with an exposure time of 2 to 4 hours. The use of hydrogen peroxide was done after testing the use of sodium hypochlorite, and finding greater effectiveness in hydrogen peroxide. At all times, it was sought to use a single sanitizing agent, to simplify the operation and avoid risks of any kind. The use of radiation was not tested so as not to jeopardize the organoleptic quality of the product. This in order to ensure that any pathogen is completely eliminated, and that the general accounts (aerobic mesophilics, fungi and yeasts) are lower than those specified for this type of product. Softer conditions (lower concentration and / or shorter time) or the use of other hydrogen peroxide substitute sanitizers, will result in inconsistency in the presence or absence of some pathogens, and variable amounts of aerobic mesophiles, which can lead to a product very close to the specification limit (1,000 CFU / gr of aerobic mesophiles, 100 CFU / gr of fungi and yeasts, absence of pathogenic microorganisms such as E. Coli, Salmonella, Stafilococcus aureus, Pseudomonas aeruginosa, with the corresponding risk.
[0061] Sanitization is carried out in sanitary containers, preferably stainless steel, preferably type 316. It must be ensured that all the keels are submerged in the sanitizing solution, to achieve the expected effect.
[0062]
[0063] The process temperature of said sanitization must be less than 30 ° C, to avoid any damage to collagen.
[0064]
[0065] Once the sternum has been sanitized, it is rinsed with purified water, in a proportion of 2 liters of purified water per kg of keels. This is done for 15 minutes, and is repeated three times, draining the water in each case. If the process is not continued at that time, the sanitized keel must be stored in refrigeration, at a temperature not higher than 4 ° C for further processing.
[0066]
[0067] The keels are dried in a tray dryer, under two variations: at 40 ° C, in an atmospheric operation (without applying a vacuum in the drying), or at 15 ° C or less with a vacuum of 16 mbar, until reaching a humidity less than 5.0%.
[0068]
[0069] Temperatures are essential, to ensure not to damage collagen, which begins to suffer degradation from 42 ° C.
[0070]
[0071] Drying below 5.0% humidity ensures that the finished product can be stored for long periods of time, without affecting its quality. By storing a product with humidities closer to or greater than 10%, the water activity is higher and there is a risk of microbial and fungal contamination mainly, which would modify its appearance and its feasibility of use for human consumption.
[0072]
[0073] The dry product is ground or pulverized to a particle size suitable for the type of presentation that will be required (capsules, tablets, etc.). During grinding or spraying, it is important to ensure that the powder does not heat above 35 ° C, to avoid damage to collagen.
[0074]
[0075] Examples of realization.
[0076]
[0077] Ex. 1- Chicken keel is taken from a certified processing facility by authorities, which must be refrigerated. This keel is hydrated with 5 liters of purified water for each kg of keel, washed in that water and excesses such as meat and others are cut off. It is finely cut and sanitized with 3.5% hydrogen peroxide for 2 hours at a temperature not higher than 30 ° C. All the sanitizations mentioned in the examples are carried out at 30 °. At the end of this stage, rinse with water (2 liters water per kg keel) for 15 minutes and the operation is repeated three times, discarding the resulting liquid. This product is loaded into a tray dryer and dried at 40 ° C the time necessary to lower the moisture of the finished product below 5.0%. The product obtained is ground or pulverized to an appropriate particle size for the use it will receive, either in tablets or capsules.
[0078]
[0079] Ex. 2- the process is carried out under the same conditions as in example 1, but the 4.0% hydrogen peroxide is used for the same time.
[0080]
[0081] Ex. 3- the process is carried out under the same conditions as in Example 1, but with 4.5% hydrogen peroxide.
[0082]
[0083] Ex. 4- the process is carried out under the same conditions as in example 1, but it is sanitized for 3 hours.
[0084]
[0085] Ex. 5- the process is carried out under the same conditions as in example 4, but the 4.0% hydrogen peroxide is applied
[0086]
[0087] Ex. 6- the process is carried out under the same conditions as in example 4, but the 4.5% hydrogen peroxide is applied
[0088]
[0089] Ex. 7- The process is carried out under the same conditions as in Example 1, but it is sanitized for 4 hours.
[0090]
[0091] Ex. 8- the process is carried out under the same conditions as in Example 7, but the 4.0% hydrogen peroxide is applied
[0092]
[0093] Ex. 9- the process is carried out under the same conditions as in Example 7, but the 4.5% hydrogen peroxide is applied
[0094]
[0095] Ex. 10- the product of example 1 is dried in trays at a temperature of 15 ° C, applying a vacuum of at least 16 mbar, until reaching a humidity below 5.0%.
[0096]
[0097] Ex. 11- comparative example: keel sanitization with 3.0% hydrogen peroxide for 20 minutes, they use the product without drying, only finely cut and thus administered to patients. Conditions described in US5750144A.
[0098]
[0099] Ex. 12,13- Tests with 3% peroxide and exposure times of one and two hours (insufficient result).
[0100]
[0101] Microbiological measurements were made in the cited examples, including samples generated according to the technique published in other patents (lower concentrations of sanitizing agent), in order to confirm that the microbiological quality of the product is improved with the technique proposed here. Common parameters were measured, such as the presence of aerobic mesophiles measured as colony-forming units-CFU / gr, Fungi and Yeasts (CFU / gr) and the absence or presence of pathogens such as coliforms, staphylococcus aureus, pseudomona aeuroginosa and salmonella spp.
[0102]
[0103]
[0104] Bibliographic references.
[0105]
[0106] 1. Pat. US5529786A
[0107] 2. Pat. US5645851A
[0108] 3. Pat. US5750144A
[0109] 4. Pat. US7846487B2
[0110] 5. Pat. WO1997037643A1
[0111] 6. Science 1993; 2611: 1727-1730.
[0112] 7. Clin.Prac.Alt.Med.2001; V2, No4, 254-259 8. Arthritis Rheum. 1998; 41: 290-297

权利要求:
Claims (6)
[1]
1. A process for obtaining native type II collagen from chicken keel, characterized by comprising:
a) obtain the cartilage from the chicken keel;
b) sanitize the cartilage with hydrogen peroxide at a concentration between 3.5 to 4.5% and at a temperature below 30 ° C;
c) rinsing the cartilage with purified water;
d) drying the cartilage at a temperature equal to or less than 40 ° C until reaching a humidity lower than 5.0%.
[2]
2. The process, according to claim 1, characterized in that the chicken sternum comes from a cold chain of no more than 4 ° C.
[3]
3. The process, according to any of claims 1, or 2, characterized in that the sanitization is carried out for 2 to 4 hours.
[4]
4. The process according to claim 1, characterized in that the drying step is carried out under atmospheric conditions.
[5]
5. The process according to claim 1, characterized in that the drying step is carried out at 15 ° C or less with a vacuum of 16 mbar.
[6]
6. The process according to claim 1, characterized in that it further comprises a grinding or spraying step at less than 35 ° C after the drying step.

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同族专利:

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公开号 | 公开日

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WO2018231042A1|2018-12-20|

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ES2748074B2|2020-07-28|

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MX2017007745A|2019-02-08|

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US20210187080A1|2021-06-24|

引用文献:

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公开号 | 申请日 | 公开日 | 申请人 | 专利标题

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US5637321A|1994-02-28|1997-06-10|Moore; Eugene R.|Method for preparing animal tissue for use in alleviating the symptoms of arthritis in mammals|

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US5750144A|1994-02-28|1998-05-12|Moore; Eugene R.|Method for alleviating the symptoms of arthritis in mammals|

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JP5753356B2|2010-09-13|2015-07-22|株式会社龍泉堂|Method for extracting non-denatured type II collagen having an active epitope|

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优先权:

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申请号 | 申请日 | 专利标题

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MX2017007745A|MX2017007745A|2017-06-13|2017-06-13|Method for obtaining native type ii collagen of avian origin.|

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PCT/MX2018/000020|WO2018231042A1|2017-06-13|2018-03-15|Method for obtaining native type ii collagen of avian origin|

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