KR100750780B1 - Development of regenerated protein fiber from collagen and water-soluble polymer complex - Google Patents

Abstract

A method for manufacturing a regenerated protein fiber is provided to supplement the material property of the protein fiber, by adding polyvinyl alcohol and alginic acid into collagen protein so as to form a spinning solution for the protein fiber. A spinning solution is formed by mixing collagen protein, polyvinyl alcohol, and a cross-linking material, wherein the collagen protein is obtained by using saving scrap as a raw material. The spinning solution is wet-spun within a coagulation bath containing two or more kinds of coagulation material. The resultant material is chemically cross-lined within a cross-linking bath containing a cross-linking material. The spinning solution is formed by mixing the collagen protein, the polyvinyl alcohol, the cross-linking material, and alginic acid of 0.1~10 wt%.

Description

Development of regenerated protein fiber from collagen and water-soluble polymer complex

The present invention relates to a method for producing protein fibers, and more particularly, to a method for producing regenerated protein fibers having improved physical properties using collagen and a water-soluble polymer complex.

As is well known, regenerated collagen protein fiber is generally treated with alkalis or enzymes from animal skins or raw materials to decompose and remove the telopeptide portion of collagen to obtain water-soluble collagen protein, which contains inorganic salts by wet spinning. Manufactured by discharging into a coagulation bath.

Collagen proteins used in fiber manufacturing vary greatly in molecular weight depending on extraction conditions (eg, temperature, time, type of drug, amount of chemicals used, etc.), and therefore, the physical properties of the fiber and the properties of the spinning dope are greatly different. You lose.

In general, when the molecular weight is large, the physical properties of the fiber are enhanced, and when the molecular weight is small, the physical properties also tend to be deteriorated. Therefore, care should be taken in using the temperature and the drug when separating the collagen protein from the shaving scrap. Due to the drawback of collagen protein re-dissolving at high temperatures in the process of manufacturing fibers, the temperature of the coagulation bath must be lowered, which leads to a lower concentration of inorganic salts, making it difficult to fiberize the collagen protein as well as weak strength. It has a hard disadvantage.

On the other hand, polyvinyl alcohol (hereinafter referred to as "PVA") is a hydroxy group-containing linear crystalline polymer prepared by saponifying a vinyl ester polymer with an acid or an alkali, and as shown in the manufacturing process, excellent solvent resistance and oil resistance Have. The PVA also has a wide range of applications, ranging from gels, clothing or industrial textiles, polarizing and packaging films, separation filters and medical polymers, depending on molecular weight, degree of saponification and stereoregularity. Because of its elastic modulus, the fibers made from it have excellent mechanical properties and have excellent alkali resistance, seawater resistance, oxygen barrier properties and adhesion compared to other polymers. Recently, biodegradability associated with environmental friendliness has emerged, and its utility in a wide range of fields is increasing.

On the other hand, alginic acid is a polysaccharide that is generally extracted from brown algae, and shows various physical properties according to molecular weight like collagen protein and PVA. In general, the molecular weight is very large, ranging from hundreds of thousands to millions of Daltons, so that a high viscosity increase can be obtained even with a small amount of use. It is used in dyeing industry, film and capsule.

In addition, the prepared collagen protein fibers are soluble in water and treated with aldehyde compounds (formaldehyde, glutaraldehyde, etc.) in various ways to modify these properties, various metal salts (chromium salts, aluminum salts, zirconium salts, etc.) ), A method of treating with an epoxy compound, and a method of mixing and treating such methods have already been taught, but there is a problem in that continuity of work is reduced and productivity is decreased by a method of dipping for a long time after fiber production. .

Accordingly, an object of the present invention for solving the above problems is to use a collagen protein, polyvinyl alcohol, alginic acid and crosslinking material of a polymer extracted from a shaving scrap which is a leather waste. By mixing and spinning, a collagen protein fiber containing two or more coagulants and a cross-linking bath containing a crosslinking material are continuously used to obtain natural collagen protein fibers having improved productivity and workability. It is to provide a method of manufacturing.

In addition, another object of the present invention is to reduce the environmental pollution that may occur during the disposal process in terms of recycling of protein resources by utilizing the leather manufacturing process waste, and to provide a material suitable for use by re-fiberizing the collagen protein extracted.

Hereinafter, a preferred embodiment according to the present invention will be described in detail. In the following description, it should be noted that only parts necessary for understanding the method for producing collagen protein fibers of the present invention will be described, and descriptions of other parts will be omitted so as not to distract from the gist of the present invention.

The raw material of the collagen protein used in the present invention is a shaving scrap inevitably generated during the leather manufacturing process, which is obtained in the process of mechanically removing the back side of the leather to control the thickness of the leather. Most of these shaving scraps are made of insoluble collagen protein, like raw hides, but they contain chromium, which is used to convert animal proteins into minerals.

In addition, even leather that has already undergone an impurity removal process contains lipids, glycoproteins, and albumins other than insoluble collagen protein, so that biochemical and filtration treatments can be carried out in consideration of the radiation stability and the strength and quality of the fiber. Must be removed.

The solubilization treatment to the above-mentioned shaving scraps to obtain collagen proteins include acid treatment, alkali treatment and enzyme treatment. However, the collagen protein obtained through the acid treatment has a low recovery rate, and the enzyme treatment method is suitable for obtaining a homogenized molecular weight, but the protein tends to be low molecular weight, so the application of alkali treatment alone is most suitable in the present invention. In addition, it is preferable to remove the collagen protein of low molecular weight through filtration in order to have a uniform physical distribution when the collagen protein obtained by the treatment as described above is fiberized.

The collagen protein thus obtained is formic acid for the prevention of coacervation caused by the difference in concentration of colloids with polyvinyl alcohol and alginic acid, which are water-soluble high molecular compounds to be added and mixed. The ratio of collagen protein and PVA is 1: 1, 1: 2, 1: 3 in an acidic aqueous solution adjusted to pH 1.0 ~ 5.0 with organic acids such as (formic acid), acetic acid, and lactic acid. Furnace at a concentration of 5 to 60% by weight, preferably at a concentration of 10 to 50% by weight. PVA to be used must have a molecular weight of 1,500 ~ 3,500 only when the fiber is excellent in physical properties, if less than 1,500 the problem of strength degradation occurs. The mixing ratio of the alginic acid to be added is most preferably 0.1 to 10% in consideration of solubility and agitation. Dissolution temperature is dissolved at a temperature of 30 ~ 70 ℃, preferably 35 ~ 60 ℃ to prevent molecular weight destruction and denaturation of collagen protein.

In addition, in order to control viscosity and enhance crosslinking ability, 0.001 to 0.02% by weight of a crosslinking material is added, and when it is more than 0.02% by weight, collagen protein and PVA due to excessive concentration may cause crosslinking reaction during stirring, causing entanglement. . Filtration is carried out to remove insoluble components, and bubbles generated during stirring are removed to degas, thereby preventing breakage of fibers that may occur during the spinning process.

The mixture of collagen, polyvinyl alcohol, and alginic acid is discharged into an aqueous inorganic salt solution through a spinning nozzle, and fiberization is possible. Metal salts such as sodium acetate and boric acid can be used, and the concentration of metal salts is 10 to 50% by weight, and it is most preferable to use sodium sulfate at 20 to 40% by weight, in combination with 0.5 to 1.0M boric acid. Most preferably. The pH of the aqueous inorganic salt solution is best between pH 3.0 and 6.0, near the isoelectric point where collagen protein is dehydrated best. In addition, the water temperature of the inorganic salt aqueous solution is best the condition of 30 ~ 36 ℃ that can have the maximum solubility of the inorganic salt without re-dissolving the coagulated fiber.

The cross-linking process is required since the fiber is redissolved immediately after washing to remove salts attached to the coagulated collagen protein fiber through the coagulation tank containing the inorganic salt. The washing process should be performed later. Therefore, the coagulated collagen fibers are immediately crosslinked through a crosslinking bath containing 0.1 to 5.0% by weight of glutaraldehyde, 0.5 to 1.0M of boric acid, and 1.0 to 6.0% by weight of an emulsion, and a drawing process is performed to increase the yield and strength of the fiber. Proceed in parallel.

In addition, in order to stabilize the crosslinking of the cross-linked collagen fibers are subjected to a pre-drying process at 30 ~ 60 ℃ and then aged 2 to 3 hours at 80 ~ 100 ℃. In addition, the washing process may be performed as necessary to remove the inorganic salts attached to the fibers.

Hereinafter, the present invention will be described in detail with reference to the preferred embodiments. However, the present invention is not limited to the embodiments, and detailed descriptions such as wet spinning processes and equipment drawings will be omitted.

{Example 1}

Alkali-solubilized chromium content containing less than 5 ppm of alkali-soluble chromium, with a molecular weight of about 100,000 Da and PVA having a molecular weight of 1,700 in a ratio of 1: 1 with formic acid, pH 1.0-5.0 It was dissolved in 10 to 50% by weight in an aqueous solution adjusted to prepare a spinning solution.

After filtration and defoaming, it is put into a spinning solution storage tank fixed at 60 ° C. of a wet spinning device, and 20-40% by weight of sodium sulfate and boric acid (through a nozzle having a diameter of 0.1 mm and a hole number of 330 by a gear pump). Boric acid) was discharged at a rate of 5 ~ 10m / min in a coagulation bath of 30 ~ 36 ℃ water temperature containing 0.5 ~ 1.0M to prepare a natural collagen fiber with improved radioactivity and workability.

{Example 2}

Alginic acid (Alginic acid) is added 0.1 ~ 10% by weight in the preparation of the spinning solution, glutaraldehyde 0.1 ~ 5.0%, sorbitan monooleate 1.0 ~ 6.0%, boric acid (Boric acid) Through the crosslinking tank containing 0.5-1.0M, the drawing was carried out using the difference in the rotation speed between the winding speed of the winding machine and the intermediate feed roller. To produce a natural collagen fiber with increased productivity.

{Example 3}

To prepare the spinning solution, add 0.001 ~ 0.02% by weight of crosslinking material, 24% glutaraldehyde, 0.1 ~ 5.0% glutaraldehyde through a coagulation bath, and sorbitan monooleate Proceed in the same manner as in Example 2 except that stretching was performed using a winding speed of the winding machine and the rotational speed of the intermediate feed roller through a crosslinking tank containing 1.0 to 6.0% and boric acid 0.5 to 1.0 M. To increase the draw ratio and physical properties and to simplify the cross-linking process to produce a natural collagen fiber with increased productivity.

{Example 4}

In the preparation of the spinning solution, 0.001 to 0.02 wt% of 24% glutaraldehyde, which is a crosslinking material, was added, and the collagen fibers prepared through the crosslinking process were dried in a hot air dryer at 30 to 60 ° C for 2 hours, and then at 80 to 100 ° C. In addition to the heat treatment for 2-3 hours in the same manner as in Example 3 to prepare a natural collagen fiber with excellent water resistance and physical properties.

{Example 5}

10% to 50% by weight of collagen protein having a chromium content of 5 ppm or less and a molecular weight of about 100,000 Da and a PVA having a molecular weight of 1,700 in a ratio of 1: 2, 24% glutaraldehyde, 0.001 to 0.02% by weight, and formic acid It was dissolved in an aqueous solution adjusted to pH 1.0 ~ 5.0 and re-dissolve 0.1 ~ 10% by weight of alginic acid to prepare a spinning solution.

After filtration and defoaming, it is put into a spinning solution storage tank fixed at 60 ° C of a wet spinning device, and a gear pump pumps a nozzle with a diameter of 0.1mm and a hole number of 330 through 20-40% by weight of sodium sulfate and boric acid (Boric acid) It was discharged at a rate of 5 ~ 10m / min to a coagulation bath of 30 ~ 35 ℃ water temperature containing 0.5 ~ 1.0M.

Glutar aldehyde 0.1 ~ 5.0%, Sorbitan monooleate through coagulation bath Stretching was performed using the difference between the winding speed of the winder and the rotational speed of the intermediate feed roller through a cross-linking tank containing 1.0 ~ 6.0% and 0.5 ~ 1.0M boric acid.

The prepared collagen fibers were dried in a hot air dryer at 30 to 60 ° C. for 2 to 3 hours, and heat-treated at 80 to 100 ° C. for 2 to 3 hours to prepare natural collagen fibers having excellent stretch ratio and excellent elasticity.

As described above, the present invention comprises a 0.001 ~ 0.02% by weight of crosslinking material by extracting a high molecular weight collagen protein having a chromium content of 5 ppm or less through biochemical treatment and filtration of the shaving scrap inevitably generated during the leather manufacturing process Collagen protein, PVA, and alginic acid are mixed in an acidic aqueous solution of 30 ~ 70 ℃ adjusted to pH 1.0 ~ 5.0 with organic acid such as formic acid, acetic acid, and lactic acid. And dissolving to increase the viscosity and strength of the spinning solution to increase spinning stability and to increase the solidification rate due to two or more high concentrations of coagulants, thereby stabilizing and improving work.

In addition, by adding PVA and alginic acid, which are harmless polymers to the human body, it is possible to compensate for the insufficient properties of collagen protein fibers and to apply them for various purposes. There is an increase in the efficiency and productivity of the work that has been a problem in the spinning process.

The collagen protein fiber produced in this way can be spotlighted through the use of environmentally harmful effects and natural collagen fibers for apparel, industrial use, etc. by using hazardous waste that was a problem when discarding.

Claims (5)

During the leather manufacturing process, a spinning solution is prepared by mixing collagen protein, a polyvinyl alcohol, and a crosslinking material, which is used as a waste scrap, as a raw material, followed by a coagulation bath containing two or more coagulants and a crosslinking tank containing a crosslinking material. Method for producing regenerated protein fibers using collagen and a water-soluble polymer composite, characterized in that the process consisting of. During the leather manufacturing process, a spinning solution was prepared by mixing collagen protein, a polyvinyl alcohol, and crosslinking material with 0.1 to 10% by weight of alginic acid as a raw material, which is a waste scrap. Method for producing regenerated protein fibers using collagen and a water-soluble polymer composite, characterized in that the process made through the included cross-linking bath. The method according to claim 1 or 2, It is extracted only by the alkali treatment in the shaving scrap, characterized in that the process consisting of producing a mixture of high molecular weight polyvinyl alcohol having a molecular weight of 1,500 ~ 5,000 and a collagen protein having a chromium content of 5ppm or less and a molecular weight of 100,000 Da or more Method for producing regenerated protein fibers using collagen and water-soluble polymer complex. The method according to claim 1 or 2, The mixing ratio of collagen protein and polyvinyl alcohol in a solvent adjusted to pH 1.0-5.0 with formic acid, acetic acid and lactic acid containing 0.001 to 0.02% by weight of glutaraldehyde, which is the crosslinking material, is 1 to 9 and 5 to 60% by weight Method for producing regenerated protein fibers using collagen and a water-soluble polymer composite, characterized in that it is prepared through a spinning solution dissolved in water. The method according to claim 1 or 2, The composition of the coagulation bath and crosslinking bath is 30-35 ° C. with a water temperature of pH 3.0-6.0 in which 20-40% by weight of sodium sulfate (Na ₂ SO ₄ ) and 0.5-1.0M boric acid (H ₃ BO ₃ ) are mixed. It contains 0.1 ~ 5.0% of tar aldehyde, 1.0 ~ 6.0% of sorbitan monooleate, 0.5 ~ 1.0M of boric acid, and it is placed next to the coagulation bath and crosslinking process, and it is 2 ~ in a hot air dryer of 30 ~ 60 ℃. Method for producing regenerated protein fibers using collagen and water-soluble polymer composite, characterized in that the drying for 3 hours and heat-treated at 80 ~ 100 ℃ for 2 to 3 hours.