JPH0657629A - Activation of oxidation and reduction functions of keratin fibers - Google Patents

Abstract

PURPOSE:To activate the catalytic function of electron transfer characterized by reversible change of cystine into cysteine in keratin fibers with high reactivity. CONSTITUTION:The nonkeratin protein is in a copper complex form and inhibits the chain fission by increasing the electron density on the bond, when cystine is twisted. In a water solution containing a metal ion which is an electrophilic catalyst and can become a sacrificial anode for copper, a strain is given to the keratin fibers to promote the conversion of cystine into cysteine and the keratin substance on the surface is removed by oxidation, then the protected electron transfer medium is exposed to the surface. The oxidation and reduction mechanism well functions responding to the external conditions to give stabilized and durable functions such as antioxidation, ageing resistance, antimicrobial or deodorization.

Description

Detailed Description of the Invention

[0001]

The present invention relates to the function of catalyzing an enzyme-like redox electron transfer reaction by exposing the redox chemical function of natural keratinous fiber without damage while activating it. Regarding the method of giving.

[0002]

2. Description of the Related Art As means for solving environmental, resource and energy problems, animals and plants carry out highly selective reactions smoothly and efficiently under natural conditions using water as a medium. It is necessary to enhance the activity of this natural product and extract and utilize it without damage. In the past, keratin fibers have only been used physically as clothing.

While it is known that natural keratin fibers have a redox function, they are covered with epidermal cells (2) having mechanically and chemically tough keratinous substances on the front side to block the function. However, when oxidized for the purpose of removing this, in the continuous layer that joins the cortical cells (1) of the fiber body, the metal part of the non-keratin protein (3, 24), which is the medium of electron transfer, also melts and loses its function. Be seen.

[0004] As a reforming technique for improving the shrinkage prevention and higher grades, the inventor has established and has already proposed a scale exfoliation method utilizing a catalytic action of a transition metal or the like (Japanese Patent Publication No. 62-1954).
0) The method is to immerse an animal substance fiber in an aqueous solution containing a metal ion and to open a hydrophilic portion on the surface of the fiber, that is, a joint portion of the scale and a non-keratin protein portion (3, 3) of the endocuticle connected to the hydrophilic portion. 24) Adsorbing a metal on it, and then treating it with a high-concentration aqueous solution of an oxidizing agent to cause catalytic oxidative decomposition, whereby the epidermal cell tissue is disintegrated and detached from the inside.

In the above method, since metal ions are adsorbed on the non-keratin protein portion (3, 24) and catalytic oxidation is carried out, the scale mechanism of the electron transfer medium is simultaneously collapsed and exfoliated, and the chemical function is not expressed. I can't expect it.

[0006] Further, in an operation of merely adding strain to the keratin fiber in an aqueous solution containing metal ions, the hydrophobic keratin materials (22, 23) covering the surface block the reaction, and the chemical activity is almost changed. do not do.

[0007]

From the above viewpoints, the object of the present invention is to facilitate the conversion of keratinous keratinous keratinous cystine bonds into cysteines and to improve the function of non-keratinous proteins (3, 24). It is to provide a treatment method that exposes while protecting.

[0008]

To activate the redox function of keratin fibers according to the present invention, a force such as bending and stretching is repeatedly applied in a water-based bath in which copper or a metal having a larger ionization than copper is dissolved. The cystine bond that supports the higher-order structure of the hard protein keratin, which causes fiber strain, mechanically assists the conversion of the cystine bond that cleaves into a highly reactive cysteine, and then oxidizes. This is characterized by decomposing and removing the keratinous parts (22, 23) of the epidermal cells (2) and exposing the inner non-keratin protein parts (3, 24) containing copper as a complex and serving as an electron transfer medium. And

The term "keratin fiber" as used herein refers to all mammalian body hair from wool, llama, alpaca and the like to human hair, regardless of the mode of implementation.

[0010]

[Function] As is well known, the structure of keratin fibers is
As shown in FIG. 1 and FIG. 2, the fiber body, which is a large number of aggregates of keratinous “cortical cells” (1) that are almost spindle-shaped, and the “epidermal cells” that surround the outside in a scaly shape.
(2) and a non-keratin protein intercellular junction substance (3), which serves as a water conduit for filling between cortical cells and between epidermal cells and the fiber body, and which joins each cell.

The epidermal cell (2) has a structure as shown in FIG. 3, and the epicuticle (21), exocuticle A (22), exocuticle B (23), and
It is composed of an end cuticle (24) inside thereof.
Exocuticle A contains 35% cystine and exocuticle B is a keratinous material containing 15% cystine, whereas endocuticle is a non-keratin protein containing only 3% cystine, of the same quality. It is linked to the intercellular junction substance (3).

As described above, keratin fibers have different mechanical and chemical properties between a hard protein, which is a main component, which is a hard protein and is hydrophobic, and a non-keratin protein which is hydrophilic and flexible and has a small cystine content. It is composed of two components.

The higher-order structure of the protein is supported by cystine bonds, which are strong crosslinks such as glaze, and make the keratin substance, which has many such bonds, rigid. Cleavage of the bond results in a highly reactive cysteine that is reversibly transformed into an electron reservoir. The electron transfer medium is a non-keratin protein.

In general, when a force acts in a direction to break a cystine bond of a protein such as twisting, the electron density between the bonds is increased and it is difficult to break the bond. According to the present invention, in an aqueous bath that also loosens other weak bonds that support the structure of proteins, when a mechanical strain such as bending and stretching is applied to the keratin fibers while depriving electrons by the action of the metal ion that is an electrophilic catalyst,
When the cystine bond is broken and cleaved into a large electron-donating cysteine, and an oxidant acts on it, the outer keratinous components (22, 23) of cortical cells are first oxidatively dissolved.

Further, according to the present invention, the metal adsorbed to the non-keratin protein (3,24) by the treatment in the metal ion protects the mechanism of the copper complex in the same material as a sacrificial anode from the oxidation treatment, and the electron of this portion is protected. It allows the moving media function to be exposed without damage.

That is, the metal ion in the present invention functions as an electrophilic catalyst for cleaving the cystine bond and as a substitute sacrificial anode for protecting the copper complex-forming non-keratin protein from oxidation.

As a means for imparting a mechanical strain to the fibers to produce the above effects, for example, as shown in FIG. 4, a pair of gear-type rolls (5A, 5A, 5A, 5) that are loosely engaged with each other.
B) may be used with bending stresses applied through the bundle of fibers (4) in between, or alternatively, a box crimping device may be used for this application.

The strain applied to the fiber is determined by observing the peeling state of the keratinous portion. Fiber thickness, length,
Adjusted by the strength of engagement and the number of times the device is passed, although it depends on the previous history.

[0019]

Example 1 A sliver (30 g / m) of Australian Merino wool (average fineness 22.0 μm) was applied 4 times / m.
Stretch the natural crimp by applying a certain amount of twist and use this wool for N
It was immersed in an aqueous solution containing 40 ppm of i ² ions, and FIG.
Repeat the 30% elongation and relaxation with the device shown in
After dehydration, chlorination was performed in a solution of hypochlorous acid containing 6.0% owf of available chlorine, treated in a dechlorination solution containing acidic sodium sulfite, washed with water and dried. It was confirmed under a microscope that the keratinous portion of the epidermal cells was decomposed, and it was revealed from the diffusion state in water that a hydrophilic non-keratin protein became the surface.

The redox powers before and after processing are
The amount of thioglycolic acid oxidized and the amount of thiol in the bound state at that time were examined by the Ellman method in which dithionitrobenzoic acid was used to compare the color of thionitrobenzoate formed at a wavelength of 420 nm. Consumption of thioglycolic acid Treatment with thiol amount It was confirmed that the previous wool 68 26 and the wool 102 65 after the treatment according to the present invention and the redox function were significantly increased.

The sliver obtained in Example 1 was made into a 3/48 thread by French worsted spinning, which was dyed in a deep gray color with a reactive dye using a cheese dyeing machine, and this thread was used for men's socks. Knitted into When this product was judged by a public institution designated by the Textile Products Sanitary Processing Council using the processing evaluation manual established by the association and the method for measuring the number of Staphylococcus aureus bacteria, Increase / decrease value difference (l
(ogB / A-logC / A) is the same product
The value was 3.1 (association acceptance value = 1.6 or more), showing antibacterial properties comparable to those of chemical processing.

The above product is further manufactured in accordance with JIS. L-021
After washing 30 times with No. 7,103, an antibacterial test was conducted by the same method for measuring the number of bacteria.
It was found that the value was higher than the original product and the antibacterial property was almost permanent.

[0023]

[Example 2] A raw fabric woven with Australian Merino wool in a twill weave is used with copper sulfate to have a copper concentration of 45 pp.
The operation of immersing in the aqueous solution adjusted to m and passing between the rollers shown in FIG. 4 is repeated 7 times, and then the liquid is removed.
Treated in a bath of oxidant containing 0% owf hydrogen peroxide,
Further, the mixture was passed through a bath containing acidic sodium sulfite to stop oxidation, washed with water and dried. Observation under a microscope and hydrophilicity tests confirmed that the fibers were of the same shape and properties as those obtained in Example 1.

[0024] A, raw fabric cloth b, a used in the above-mentioned examples or obtained in an intermediate stage, was subjected to the method of the present invention by the method of the present invention to adsorb copper ions and cloth c, b was oxidized to form a skin. The three points of the modified cloth of the present invention in which the keratinous material of cells is removed. At the same time, on the modified cloth of c, three kinds of chemicals which are usually used for antibacterial and deodorant treatment were selected, processed according to the manufacturer's prescription, and compared with an unprocessed product (cotton gold width). However, the antibacterial test was carried out by measuring the number of bacteria using Staphylococcus aureus. Number of bacteria after 18 hours Difference in increase / decrease value of bacteria a. Raw fabric cloth 2.3 × 10 ⁸ 0.75 b. a + After adsorption of copper ions 1.8 × 10 ⁸ 0.86 c. b + the present invention keratin-removing cloth 8.1 × 10 ⁴ 4.21 d. c + modified fatty acid ester processing 2.6 × 10 ⁴ 4.70 e. c + alkylamine processing 1.3 × 10 ³ 6.00 f. c + Silicon-based quaternary ammonium salt processing <3 x 10 ² 6.64 Blank standard cloth (cotton gold width) 1.3 x 10 ⁹ (pass value 1.6 or more)

As a result, it cannot be said that the raw fabric cloth before treatment is effective in antibacterial property as compared with the blank standard cloth. Further, the cloth in which copper ions are simply adsorbed while distorting the cloth is a slight increase, and the processed cloth according to the present invention is not inferior to the processed cloth subjected to the chemical treatment for claiming antibacterial and deodorant growth of bacteria. It showed a suppressing effect.

[0026]

EFFECTS OF THE INVENTION When keratin fibers such as wool are treated according to the activation of the present invention, a durable hygienic process which has been heretofore obtained only by chemical processing in clothing can be obtained safely and easily.

Drugs having a cysteine group are widely used in medicine such as glutathione and cystamine, and the keratin fibers of various modes have the functions obtained by the present invention and can be applied to medical purposes.

Further, the keratin fiber as a raw material of the present invention can be easily obtained in a large amount, such as wool, and can be expanded to be used as an antioxidant material.

[Brief description of drawings]

FIG. 1 is a vertical cross-sectional view for explaining the structure of keratin fibers.

FIG. 2 is a cross-sectional view for explaining the structure of keratin fibers.

FIG. 3 is an enlarged cross-sectional view schematically showing the structure near the surface layer of the keratin fiber of FIG.

FIG. 4 is a diagram showing an example of a specific method for applying a mechanical force to a bundle of keratin fibers in order to carry out the activation treatment method of the present invention.

[Explanation of symbols]

 1 ... Cortical cells 2 ... Epidermal cells 21 ... Epicuticle 22 ... Exocicle A 23 ... Exocicle B 24 ... Endocicle 3 ... Intercellular junction material 31 ... Cell indirect Opening of compound material 4 Bundle of keratin fibers 5A, 5B ... Gear type roll

Claims (1)

[Claims] 1. In a water-based bath in which copper or a metal whose ionization is larger than that of copper is dissolved, a force such as bending and stretching or twisting is repeatedly applied to cause strain in the fiber, thereby forming a higher order structure of keratin which is a hard protein. The supporting cystine bond
Mechanically assisting the conversion to cysteine, which is cleaved and becomes highly reactive, and then performing oxidative treatment to decompose and remove the keratinous portion (22, 23) of the epidermal cell (2),
Activation of redox function of keratin fiber characterized by exposing non-keratin protein part (3, 24) serving as a medium of electron transfer, containing copper as a complex