JPH0118878B2 - - Google Patents

Description

DETAILED DESCRIPTION OF THE INVENTION <<Industrial Application Field>> The present invention relates to a recording material having a thermal recording layer containing a modified protein compound as a heat-sensitive component. <Prior Art> A technology relating to a recording material and a recording method in which a heat recording layer having a heat-sensitive component of a thermocoagulable protein compound that coagulates when an aqueous solution of a protein compound is heated is provided on a support (a) is a special technology. Publication Showa 54-10870, (b) Japanese Patent Publication Showa
52-121331, (c) Unexamined Japanese Patent Publication No. 55-15817, (d) Unexamined Japanese Patent Application No. 1983-
15818. On the other hand, (e) a heat-sensitive recording material containing a graft copolymer consisting of a thermocoagulable protein and a polymerizable monomer as disclosed in JP-A-56-15395; Recording materials containing coagulable proteins: (g) A recording material containing thermocoagulable proteins chemically modified in a non-crosslinking manner has been proposed in Japanese Patent Application No. 172,643/1983. In these modification techniques involving chemical reactions of thermocoagulable proteins, as described in column (e) 3 above, "When using the reaction product as the heat-sensitive recording material of the present invention, thermocoagulable proteins are It is necessary to avoid thermal coagulation during the reaction, and in fact, modification of thermocoagulable proteins is carried out at a relatively low temperature at which thermal coagulation does not occur. In other words, these modifications are called chemical modifications of proteins.
Modification). The disclosed technologies (a) to (g) above are characterized in that in each case, undenatured thermocoagulable proteins are used. H.Neurath et al.Chem.Rev. 34 , 157
(1944), denaturation is a non-hydrolytic change in the structure of natural proteins, and the Rikagaku Dictionary, 3rd edition expanded edition, page 814 (Iwanami Shoten 1981) states that the cause of denaturation of protein compounds is physical. Furthermore, changes that occur during denaturation include a decrease in solubility, collapse of crystallinity, changes in molecular weight and molecular shape, and the appearance of S-H or S-S groups. It is stated that it is possible to give Biochemistry Experiment Course 1. Protein Chemistry 104
Page (Tokyo Kagaku Doujin 1977) states that chemical modification and denaturation are different concepts, such as ``no denaturation of the protein occurs during the modification reaction'' or ``modification of the protein in a denatured state.'' has been done. The conventional technology requires relatively low temperature drying as described in (a) Japanese Patent Publication Publication No. 54-10870, column 3, line 23, and therefore requires slow formation of the recording layer in a low humidity atmosphere. In this case, it was necessary to lengthen the drying area and install large dehumidification equipment. By using a modified protein compound obtained by modifying a thermocoagulable protein compound as a heat-sensitive component, the present inventors have solved the restrictions on manufacturing conditions that could not be achieved with conventional techniques using thermocoagulable proteins and their derivatives, or The present invention was completed based on the knowledge that various performances of recording materials can be improved. <<Problems to be Solved by the Invention>> Accordingly, an object of the present invention is to provide a recording material having good performance while reducing restrictions on manufacturing conditions in a recording material containing a thermocoagulable protein compound as a heat-sensitive component. It is in. <<Means for Solving the Problems>> The above-mentioned object of the present invention is to provide a thermocoagulable protein compound with chemical denaturation using a protein compound denaturant, physical denaturation using heat, pressure, shaking, and freezing methods, and
This was achieved using a recording material comprising a heat-sensitive recording layer provided on a support, which contains, as a heat-sensitive component, a denatured protein compound modified by at least one modification method selected from the group of biological modification using microorganisms or enzymes. In the present invention, thermocoagulable protein compounds include isolated proteins such as albumin, hemoglobin, globulin, prolamin, and glutelin, as well as albumin-based albumin, dried egg white, hemoglobin-based blood meal, and globulin. These include soy protein (dried soy milk, concentrated soy protein powder) whose main ingredients are soybean protein, wheat gluten (active wheat protein) whose main ingredients are promilan and glutelin, and "corn" protein (zein) whose main ingredient is prolamin. In addition to these, (e) the graft copolymer described in JP-A-56-15395, (f) the thermocoagulable protein into which a photosensitive group is introduced as described in JP-A-55-13017, (g)
55-172643, which is chemically modified in a non-crosslinking manner, can also be used. The denatured protein compound used in the recording component of the present invention is
For example: (1) a Acyclic amidine derivatives such as guanidine, aminoguanidine, acetamidine, carbamoylguanidine, biguanide, and salts of the above derivatives such as hydrochloric acid, carbonic acid, hydrobromic acid, iodic acid, thiocyanic acid, etc., or imidazole, 3
- Amidine derivatives consisting of heterocyclic amidine derivatives such as aminotriazole. b Thiourea derivatives such as thiourea, methylthiourea, 1,3-diethylthiourea. c Carbamates such as urethane, N-methylurethane, and n-butyl carbamate. d glycine, glycylglycine, N-acetyl-D, L-alanine, N-acetyl-D,
Amino acids such as L-leucine. e Ammonium formate, ammonium chloride, potassium iodide,
Organic and inorganic salts such as sodium salicylate, sodium thioglycolate. f Organic acids such as acetic acid, lactic acid, and citric acid. g Formamide, acetamide, glycolamide, N,N-dimethylacetamide, ε
-Amides and imides such as caprolactam. h Urea derivatives such as urea, methylurea, ethylurea, semicarbazide. i Amines and their salts such as ethylamine hydrochloride, triethylamine hydrochloride, triethanolamine, propanolamine, tetramethylammonium chloride, hydroxylamine. j Alcohols such as methanol, ethanol, and butanol. k Ethers or acetals such as dioxane, furfural, diethylacetal. l Acetone, methyl ethyl ketone, diacetone alcohol, holone, cyclohexanone,
Ketones such as acetophenone. m ethylene glycol monomethyl ether,
Polyhydric alcohol derivatives such as ethylene glycol monobutyl ether, ethylene glycol monoacetate, and ethylene glycol esters. n Phenol derivatives such as catechol, phloroglycinol, pyrogallol. o Sulfonic acid derivatives such as benzenesulfonic acid and P-toluenesulfonic acid and their salts. Thiazole derivatives such as p2-mercaptobenzothiazole, acetamidothiazole, benzothiazole. A thermocoagulable protein compound chemically modified with at least one protein compound denaturant selected from the group such as (2) Thermocoagulable protein compounds physically modified by heat, pressure, shaking, freezing, etc. (3) Biologically modified thermocoagulable protein compounds using microorganisms, enzymes, etc. (4) A thermocoagulable protein compound that has been heated, that is, thermally denatured, while undergoing the above-mentioned chemical denaturation, (and) the above-mentioned physical denaturation excluding thermal means, or (and) the above-mentioned biological denaturation. (5) A thermocoagulable protein compound that has been chemically denatured, (and) physically denatured excluding thermal means, or (and) biologically denatured and then heated, that is, thermally denatured. When preparing the above-mentioned modified protein compound, modifiers such as surfactants, water-soluble polymers, dyes, preservatives, and fungicides may be present in order to facilitate subsequent steps. To produce the recording material of the present invention, one or more modified protein compounds as described above are emulsified and dispersed in a dispersion medium such as water, coated on a support, and dried to form a recording layer. A recording layer may be formed on a support by mixing an appropriate amount of the modified protein compound of the present invention into a thermocoagulable substance made of the thermocoagulable proteins described in the above-mentioned documents (a) to (g). A sensitizer, a photothermal conversion substance, a coloring agent, etc. can be added to the recording layer of the present invention. Heat sensitizers that can be added to the recording layer are (b)
Acid amides such as acetamide, acrylamide and nicotinamide, thioacid amides such as thioacetamide, imides such as urea and ε-caprolactam, glucose, citric acid, and gluconic acid proposed in JP-A-52-121331. These include oxycarboxylic acids and their salts such as sodium, polyhydric alcohols such as ethylene glycol and glycerin, and nitrogen-containing cyclic compounds such as hexamethylenetetramine. One or two sensitizers
Appropriate amounts of seeds or more can be added to the recording layer. The recording layer contains (c) carbon black, graphite, and atomic weight described in JP-A-55-15817.
45 to 210 fine metal powders or fine powders of oxides or sulfides of these heavy metals, photothermal conversion substances such as black or dark dyes or organic pigments, (d) JP-A-Sho
Colorants such as yellow, orange or red dyes and pigments proposed in No. 55-15818, or other dyes and pigments may also be added. The support on which the recording layer is provided is polyester,
Plastic films such as polyacetate, polystyrene, and polycarbonate, matted films such as polyester films with matted surfaces, synthetic paper, glass, and the like may be used, and may be provided with an undercoat layer. Methods for thermally recording the recording material of the present invention can be roughly divided into external heating methods and internal heating methods. External heating methods include direct heat or heat pattern contact to selectively insolubilize the heat, and reflective exposure method, which receives heat generated and accumulated during exposure in the heat ray absorption region of the document and selectively insolubilizes the document. In some cases, insolubilization is performed. The internal heating method is mainly (c)
It is applied to a recording layer containing a photothermal conversion substance described in JP-A-55-15817. In this method, the recording layer is exposed to light through a mask to selectively apply electromagnetic radiation, and the recording layer is insolubilized by heat generated by a photothermal conversion substance. In order to form a recorded image from a recording layer that has been heated as described above, either a portion of the recording layer that has been changed by the heat or an unaltered portion is removed to obtain the recorded image. Usually water, dilute acid aqueous solution, dilute alkali aqueous solution,
By using an aqueous solution such as a neutral salt solution and removing the unaltered portion in the recording layer by a method such as shower development, spray development, immersion development, or wipe development, the portion corresponding to the thermal pattern can be obtained as a recorded image. It will be done. Examples are shown below to further explain the present invention in detail, but the present invention is not limited thereto. Example 1 10g of egg albumin (manufactured by Tokyo Chemical Industry Co., Ltd.) was added to water.
This solution was heated at 70° C. for 10 minutes to obtain a white cloudy substance. The heat-denatured product 50 cooled to room temperature
20 g of water and carbon black (Columbian
Carbon Co. After ultrasonic dispersion, 2 g of the solution was added to a polyester film (manufactured by the same company) and applied with a wire bar onto a polyester film, followed by drying with hot air at 80° C. to form a recording layer. A transparent negative original was placed in close contact with the recording material obtained in this way, and a xenon flash light source (Riso Kagaku Kogyo Co., Ltd.
After exposure using Xenofax FX-150 (manufactured by Co., Ltd.), the unexposed areas were removed and a clear positive recorded image was obtained by washing with running water. Example 2 5 g of dried egg white (manufactured by Yamatoya Shokai Co., Ltd.) was dissolved in 45 g of water, and this solution was added dropwise to 50 g of boiling water at 95°C using a dropper while stirring. The temperature of the hot water was maintained at 90° C. or higher until the dropwise addition was completed, and a white suspension was obtained. 5 g of water and 0.5 g of the red pigment Lake Red 4R (manufactured by Toyo Ink Mfg. Co., Ltd.) were added to 11 g of the heat-denatured product cooled to room temperature, followed by ultrasonic dispersion, and then coated on a polyester film with a wire bar.
Drying was performed with hot air at 110°C. The obtained recording material and a reflective original having a black line drawing pattern are brought into close contact, and the recording material is exposed from the side using a xenon flash light source, and then the non-image areas of the original are developed by spraying with water. The portion was removed and a clear positive recorded image was obtained. Example 3 20g of acetone (manufactured by Kanto Kagaku Co., Ltd.) was added dropwise to 50g of raw egg white while stirring, and stirring was continued to obtain a white suspension. 2g of carbon black and 1g of glycerin were then added and ultrasonic dispersion was performed. It was applied onto synthetic paper (manufactured by Oji Yuka Co., Ltd.) with a wire bar and dried with hot air at 70°C. Example 1 using the obtained recording material
The same process was performed and similar results were obtained. Example 4 5 g of glacial acetic acid was added dropwise to 50 g of raw egg white using a whole pipette while stirring, and then 45 g of water was added to obtain a suspension. Using this, the same treatment as in Example 2 was carried out to obtain the same results. The same results as above were obtained by replacing glacial acetic acid with a 10% aqueous solution of catechol, 1,4-dioxane, and a 10% aqueous solution of p-toluenesulfonic acid. Example 5 A suspension obtained by adding 30 g of a 10% egg white aqueous solution dropwise over 2 minutes to 30 g of ethanol heated to 70°C and stirred was cooled to room temperature, and carbon black (Columbian
(manufactured by Corbon Co.) was added, subjected to ultrasonic dispersion, applied onto a polyester film, and dried at 100°C for 2 minutes. This recording material was treated in the same manner as in Example 1 to obtain a similar recorded image. Example 6 5 g of dried egg white (manufactured by Yamatoya Shokai Co., Ltd.) was dissolved in 92 g of water, 3 g of a 25% urea aqueous solution was added, and the suspension was heated at 85° C. for 3 minutes. After cooling the resulting suspension to room temperature, Example 1 A recording material was prepared in the same manner as above, and a clear recorded image was obtained by performing the same treatment. Example 7 10 g of soybean protein "Solby" (manufactured by Nisshin Oil Co., Ltd.) was dispersed in 95 g of water, heated at 70°C for 30 minutes, and the film formed on the surface of the liquid was crushed in a mortar, and water was added twice the weight of the film. After emulsifying and dispersing the mixture, it was coated on a polyester film and dried with hot air at 80°C. A reflective original having a black line drawing pattern is closely attached to the recording material obtained, and the recording material is exposed to light using a xenon flash light source from the side, and the portion corresponding to the non-image is removed by water shower development to create a positive. I got a recorded image of the relationship. When this recording film was immersed in a methylene blue alcohol solution and washed with water, a clear blue original image was obtained. Example 8 Using human serum globulin (manufactured by Wako Pure Chemical Industries, Ltd.), enzyme papain (manufactured by Wako Pure Chemical Industries, Ltd.), and sodium cyanide, HPLundgren, J.Biol.Chem.
138, 293 (1941), a cloudy white liquid with a solid content of 3% by weight was obtained. A recording material was prepared and recorded in the same manner as in Example 2 using the biologically modified white turbid liquid, and similar results were obtained. Example 9 After dissolving 5 g of dried egg white (manufactured by Yamatoya Shokai Co., Ltd.) in 95 g of water, 5 g of the red pigment Sumitone Red 6F (manufactured by Sumitomo Chemical Co., Ltd.) was stirred and subjected to ultrasonic dispersion, and then the dispersion was mixed with a roller. Pressure modification was performed by applying shearing force to obtain a non-viscous coating that was insoluble in water. This coating
100 g of water was added to 100 g, emulsified and dispersed in a mortar, coated on a polyester film, and dried with hot air at about 100° C. to obtain a recording material. Exposure and spray development were carried out in the same manner as in Example 2, and a clear red positive image was obtained. Example 10 [Table] In Table 1, Experiment No. 1 is the case where the heat-sensitive component was the undenatured thermocoagulable protein compound disclosed in Japanese Patent Publication No. 10870/1983. Experiments Nos. 2 to 4 are cases of the present invention in which a denatured protein compound subjected to denaturation is used as a heat-sensitive component. Further, the specific sensitivity is a relative sensitivity measured by comparing the sensitivity obtained when a coating liquid having the composition of Experiment No. 1 was applied and dried at 30° C. for 15 minutes to form a recording layer, with the sensitivity being 100. Each of the above compositions was subjected to ultrasonic dispersion, applied onto a polyester film with a wire bar, dried at 30°C or 100°C, a reflective original was closely attached to the resulting recording material, and a xenon flash light source was applied from the side of the recording material. The specific sensitivities were calculated from the wedges obtained by exposure and spray development with water, and the results were as shown in the table above. 100℃5 in the composition of experiment number 1
In the recording material obtained by drying for 1 minute, no recorded image could be obtained due to thermal coagulation on the entire surface, whereas the recording materials made of the compositions of Experiment Nos. 2, 3, and 4 using the modified protein compound of the present invention showed excellent results. I got it. The contents of Production Examples 1 to 3 in the above table are described below. Production example 1 Add 10g of egg albumin (manufactured by Tokyo Chemical Industry Co., Ltd.) to water.
90 g of the solution was dissolved, 30 g of urea was added thereto, the mixture was stirred at room temperature for 24 hours, and then dialyzed against tap water for 3 days to obtain a cloudy white liquid with a solid content of 6%. Production example 2 Dissolve 10g of egg albumin in 90g of water and then heat to 90℃
The mixture was heated for 5 minutes and then cooled to room temperature to obtain a white cloudy substance. Production Example 3 After dissolving 10 g of egg albumin in 90 g of water, 5 g of urea was added thereto, heated at 85° C. for 5 minutes, and then cooled to room temperature to obtain a white cloudy substance. <<Effects of the Invention>> As detailed above, since the recording material of the present invention contains a heat-coagulable protein compound that has been denatured in advance as a heat-sensitive component, the heat-sensitive recording layer is coated on a support and dried. There is no need to dry at low temperatures when drying, and heat drying can be performed. Therefore, when producing the recording material of the present invention, it is necessary to install a long drying zone or a large dehumidifying device in the production machine, as in the case of producing a conventional recording material using a thermocoagulable protein compound as a heat-sensitive component. Therefore, the present invention not only makes it possible to downsize the manufacturing machine and save energy, but also facilitates the manufacture of the recording material itself. Furthermore, the recording material of the present invention has excellent storage stability, and the images obtained are extremely clear.

Claims (1)

[Claims] 1 At least one denaturation method selected from the group of chemical denaturation using a protein compound denaturing agent, physical denaturation consisting of heat, pressure, shaking, and freezing methods, and biological denaturation using microorganisms or enzymes for thermocoagulable protein compounds. A recording material comprising a heat-sensitive recording layer containing a modified protein compound as a heat-sensitive component on a support.