JP2011092851A - Protein impregnated filter - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To provide a protein carrying filter of enzymes, antibody materials, etc. which sorbs various kinds of bacteria, fungi, virus, allergen materials, etc. and can inactivate them efficiently. <P>SOLUTION: Polyethylene oxide coexists to allow the antibody materials and enzymes low in a refining degree to function effectively on the filter. <P>COPYRIGHT: (C)2011,JPO&INPIT

Description

  The present invention relates to a filter adhering to an antibody capable of adsorbing and inactivating various bacteria, molds, viruses, allergen substances and the like. More specifically, the present invention relates to a filter in which polyethylene oxide is simultaneously impregnated with a low-purity protein having a purity value of 0.9 or less determined by effective protein mass / total protein mass.

  Various filter media for removing harmful substances such as various bacteria, molds, viruses, and allergen substances have been proposed so far. In addition, a filter in which a protein such as an enzyme or an antibody is attached to the filter and a moisturizing component coexists on the filter for the purpose of supplying water necessary for expression of the protein activity is also known. However, there has been no proposal of a filter in which polyethylene oxide is simultaneously added to a protein having a low purity of 0.9 or less, which is determined by effective protein mass / total protein mass.

  Patent Document 1 discloses a virus removal filter in which at least one of sialic acid, a sialic acid derivative, and a saccharide, glycoprotein, and glycolipid containing these is a virus trap. Patent Document 2 discloses a fiber material having a high degree of microfibrosis, in which at least one fiber is attached with a natural receptor for virus or a part thereof or an analog thereof for the purpose of capturing the virus. For the purpose of derivatization with cyanogen bromide. However, the method of removing harmful substances in the air by filtration using a filter or physical adsorption using an adsorbent is non-specific and has low accuracy. In addition, in order to prevent the removed harmful substances from re-floating or the harmful substances growing on the filter to become a new source of contamination, it is necessary to combine technologies for sterilization and inactivation of harmful substances. It was.

  Further, Patent Document 3 discloses an antiviral mask composed of a string that holds a non-woven fabric with tea extract components attached thereto, and Patent Document 4 discloses a water-insoluble polymer anti-allergen agent having a phenolic hydroxyl group and hygroscopicity. A filter carrying a material is disclosed. Tea-extracted components and water-insoluble polymers with phenolic hydroxyl groups are known to have antibacterial activity, but they are specific enough to inactivate specific bacteria such as enzymes and antibodies. It has no reactivity. Proteins such as enzymes and antibodies are preferred because they can be prepared according to the target harmful substance, and a more reliable effect can be obtained. In addition, tea-extracted components and water-insoluble polymers having phenolic hydroxyl groups have a low affinity with water, and have a problem that they are poorly workable, for example, they do not mix well when adhering to a filter. On the other hand, although proteins such as enzymes and antibodies vary depending on their types, they generally dissolve well in water and have excellent processability when attached to a filter.

  In order to sterilize / inactivate harmful substances on the filter, it is effective to carry proteins such as enzymes and antibodies having the ability to sterilize / inactivate harmful substances on the filter. However, a filter in which various enzymes are supported on a carrier by a method such as a covalent bond, an ionic bond, a cross-linking method, or a comprehensive method disclosed in Patent Documents 5 to 8 has a problem that the loading method is complicated and expensive. Therefore, it has been desired to carry a protein by a simple method and to express its activity.

  Furthermore, Patent Document 4 discloses a method in which a hygroscopic material with a filter surface adsorbs moisture necessary for the expression of the activity of the antiallergen agent from the ambient atmosphere. There is a problem that the amount of protein activity is not always sufficient.

JP-A-9-234317 JP-T-2001-527166 JP-A-8-333271 JP 2004-290922 A International Publication No. 98/04334 Pamphlet JP 60-49795 A JP-A-2-41166 JP 2003-210919A

  The present invention relates to a filter carrying a protein such as an enzyme or an antibody that can adsorb various bacteria, molds, viruses, allergen substances, etc. on the filter and can inactivate them efficiently. It is an object of the present invention to effectively act even when a protein material having a low purity is used in a protein material that is difficult to be formed.

  As a result of intensive studies to improve the performance of the protein-carrying filter, the present inventors have found that a protein having a low purity can be specifically stabilized by simultaneously adding polyethylene oxide, and finally complete the present invention. It reached. That is, the present invention is as follows.

(1) A filter in which polyethylene oxide is impregnated with a protein having a purity value of 0.9 or less determined by effective protein mass / total protein mass.

(2) The filter according to (1), wherein the effective protein is bromelain.

(3) The filter according to (1), wherein the effective protein is an egg yolk-derived antibody (IgY).

  The protein-attached filter of the present invention uses a protein having a low purity by specifically stabilizing the activity expression of a protein such as an enzyme or an antibody substance having a low purity by simultaneously attaching polyethylene oxide. In addition, it is possible to obtain a filter that adsorbs various bacteria, molds, viruses, allergen substances and the like and can be inactivated efficiently on the filter.

  The protein used in the present invention has a purity value of 0.9 or less determined by effective protein mass / total protein mass. The degree of purification mentioned here can be obtained by calculation from the effective protein mass and the total protein mass.

  The effective protein mass referred to here is the mass of proteins such as enzymes and antibodies attached to inactivate various bacteria, molds, viruses, allergen substances and the like.

  The total protein mass referred to here is the mass of all proteins attached to the filter and includes effective proteins.

  The degree of purification of the protein attached to the filter can be determined by calculation by determining the masses of effective protein and total protein by SDS-PAGE analysis.

  In the present invention, the value of the protein purification degree was set to 0.9 or less because the protein is generally obtained by purifying a material derived from a living body, but if a protein having a purification degree exceeding 0.9 is obtained, the protein is purified. This is because many costs are required. In addition, proteins purified to a degree of purification exceeding 0.9 generally have low storage stability. This is because the contaminating protein contributes to the stability of the target protein. A preferred degree of purification is 0.5 to 0.9.

  The polyethylene oxide used in the present invention is supported for the purpose of retaining moisture and providing moisture and a reaction field necessary for the expression of protein activity.

  In order to obtain a sufficient effect, the amount of polyethylene oxide supported is preferably 0.01% by mass or more based on the carrier sheet. In addition, when the amount exceeds 5.0% by mass, even if the amount is increased further, the effect of improving the stabilization of protein activity cannot be expected. On the contrary, the adhesion on the fiber surface increases, and the carrier sheet This is not preferable because hardness spots and the like are generated when the material is processed. A more preferable loading amount is 0.1 to 3.0% by mass.

  Polyethylene oxide may be applied to the fiber either before or after protein attachment such as enzyme or antibody. Specifically, there is a method of applying to a fiber using a processing roller or the like when producing a sheet constituting a carrier sheet, or a method of mixing polyethylene oxide into a protein solution and simultaneously supporting the protein and polyethylene oxide. Can be mentioned.

  The material for the carrier sheet of the protein-carrying filter of the present invention preferably contains polyester fibers, and more preferably such polyester fibers contain an amorphous copolymerized polyester component. This is because the polyester fiber containing the amorphous copolymerized polyester component has good wettability with water and good workability when carrying proteins such as enzymes and antibodies.

  In addition, the polyester containing the amorphous copolymer polyester component has moderate humidity control, so that polyethylene oxide absorbs and retains moisture from the polyester fiber containing the amorphous copolymer polyester component and the surrounding atmosphere. Thus, by providing a reaction field to the protein and stabilizing the activity expression, it is possible to provide a protein-carrying filter in which the activity expression of the protein is highly stabilized. The moderate humidity control here is a performance capable of providing water necessary for the expression of the activity of the protein supported on the fiber surface. If the amount of water provided to the protein is too large, the protein will be prematurely deteriorated, and if it is too small, the activity will not be expressed. In addition, the amount of water provided to the protein present on the fiber surface has no direct correlation with the water content representing the amount of water present inside the fiber.

  The amorphous copolymerized polyester component is preferably obtained by adding a copolymerized component during polyester formation by polycondensation reaction of an aromatic dicarboxylic acid and a glycol component. More preferably, it is based on terephthalic acid and ethylene glycol, and examples of copolymer components include isophthalic acid, adipic acid, sebacic acid, azelaic acid, dodecanoic acid, diethylene glycol, propanediol, butanediol, pentanediol, hexanediol, and polyethylene glycol. And neopentyl glycol. Such an amorphous copolyester has a glass transition temperature Tg in the range of 50 to 100 ° C. and does not exhibit a clear crystalline melting point.

  In the present invention, it is preferable that the amorphous copolyester component contains terephthalic acid, isophthalic acid, ethylene glycol, diethylene glycol in order to carry a protein such as an enzyme or an antibody substance and stabilize its activity expression. The copolymer molar ratio is (terephthalic acid / isophthalic acid) = (40/60) to (80/20), and (ethylene glycol / diethylene glycol) = (70/30) to (97/3). More preferably.

  The fiber containing the amorphous copolymerized polyester component is preferably a composite fiber of the above-mentioned amorphous copolymerized polyester component and a polyalkylene terephthalate-based polyester component. Specific examples of the polyalkylene terephthalate polyester include polyethylene terephthalate and polybutylene terephthalate. The composite fiber may be in the form of a sheath / core type, an eccentric sheath / core type, a side-by-side type, or the like. Among them, a sheath-core type composite fiber having amorphous copolymer polyester as a sheath component and polyethylene terephthalate as a core component is preferable in terms of processability. Further, the composite ratio of the amorphous copolymerized polyester component is 10 to 90%, and preferably 30 to 70% from the viewpoints of performance and workability.

  The material for the carrier sheet of the protein-carrying filter of the present invention preferably contains rayon. Rayon has a high moisture content, and has an appropriate humidity control property, similar to a polyester containing an amorphous copolyester component.

  In addition to those listed here, examples of the material for the carrier sheet of the protein-carrying filter of the present invention include acrylic, nylon, polyolefin, cellulose, and pulp, but are not particularly limited.

  The fineness of the fibers constituting the carrier sheet is preferably adjusted in the range of 1 to 30 dtex from the viewpoint of processability and filter characteristics during sheet formation.

Carrier sheet is in the form of non-woven fabric such as spunbond nonwoven fabric, spunlace nonwoven fabric, needle punch nonwoven fabric, melt blown nonwoven fabric, flash spun nonwoven fabric, thermal bond nonwoven fabric, chemical bond nonwoven fabric, stitch bond nonwoven fabric, and wet papermaking nonwoven fabric, woven fabric, or paper sheet If it comprises, it will not specifically limit. Moreover, the basis weight is not particularly limited, but a preferable range is 10 to 200 g / m ² . If it is less than 10 g / m ² , it may not be possible to sufficiently capture inactivated objects such as various bacteria, molds, viruses, and allergen substances, and if it exceeds 200 g / m ² , the pressure loss of the filter increases, which is not preferable. .

  As a method for loading a protein such as an enzyme or an antibody substance on a carrier sheet, a method in which the carrier sheet is impregnated with an aqueous protein solution having an appropriate concentration and dried at an appropriate temperature and time is a preferred example. The aqueous protein solution used here is preferably adjusted to a pH suitable for the expression of the activity of each protein. This is because proteins have different pHs suitable for activity expression depending on the type, and normally, sufficient activity expression cannot be obtained unless the pH is around. In addition, it is important that the drying temperature and time are such that the protein carried is not inactivated by denaturation. Proteins vary greatly in heat resistance depending on the type. Usually, drying at a high temperature results in good efficiency after a short time, but it is preferable to determine the drying conditions in consideration of the heat resistance of the protein.

  Preferred examples of effective proteins attached to the filter include bromelain and egg yolk-derived antibody (IgY).

  Bromelain is a pineapple-derived proteolytic enzyme and can be obtained in large quantities at a low cost if it has a low degree of purification.

  Egg yolk-derived antibodies (IgY) can also be obtained in large quantities at low cost if they have a low degree of purification.

  In addition to those listed here, enzymes such as enzymes and antibodies applicable to the protein-carrying filter of the present invention include lytic enzymes (lysozyme), proteolytic enzymes (proteases), and enzymes that oxidize and reduce various allergens (oxidoreductases). Examples include, but are not limited to, antibodies that inactivate bacteria, molds, viruses, environmental allergens, and the like.

  In addition, the enzyme here is “a protein biocatalyst produced in living cells”, and the antibody is “a protein that specifically binds to an antigen produced in vivo by stimulation of an antigen in an immune reaction”. "Protein is a group of high molecular nitrogen-containing organic compounds that are mainly contained in cells of animals, plants, microorganisms, and so on called organisms" (Iwanami Biochemical Dictionary, 3rd edition Iwanami) Bookstore).

  In general, the activity of proteins such as enzymes and antibodies is not expressed in a dry state. Therefore, when proteins such as enzymes and antibodies are supported on a carrier sheet and used, it is necessary to supply moisture. Therefore, there is known a method for stabilizing the expression of activity by coexisting a moisturizing component on the filter so that the moisturizing component retains moisture in the surrounding atmosphere and provides a reaction field for proteins. Yes.

  In the case of a protein having a low degree of purification, the activity expression of the protein is specifically stabilized by using polyethylene oxide as a moisturizing component. This effect is particularly prominent in bromelain and egg yolk-derived antibody (IgY).

  EXAMPLES Hereinafter, although an Example demonstrates this invention in detail, this invention is not limited at all by this.

(Manufacture of carrier sheet)
As the amorphous copolymer polyester of the sheath component, the acid component is copolymerized in a molar ratio of 60% terephthalic acid, 40% isophthalic acid, the diol component in a molar ratio of 95% ethylene glycol, and 5% diethylene glycol. Amorphous copolyester having an intrinsic viscosity of 0.56 and Tg of 64 ° C., and polyethylene terephthalate having an intrinsic viscosity of 0.64, Tg of 67 ° C., and Tm (melting point) of 256 ° C. as the core component. Each pellet was dried under reduced pressure, then composite-spun with a sheath-core type composite spinning machine, and stretched and cut with a short fiber drawing machine, and mass ratio (sheath / core) = (50 / 50), a sheath-core type composite fiber having a single yarn fineness of about 2.2 dtex was obtained. Next, this fiber was cut into 50 mm, a web was formed by carding, and then needle punching was performed to obtain a carrier sheet 1 having a basis weight of 30 g / m ² .

(Enzyme activity test: Test example 1)
Sprinkle the granules of freeze-dried Micrococcus luteus on the protein-carrying filters of Examples 1 and 2 and Comparative Examples 1 to 5 described below. It left still for 24 hours in the hold | maintained desiccator. Then, it observed with the low vacuum scanning electron microscope, and visually observed the grade of the lysis of Luteus bacteria. The case where the sphere shape of the bacterium collapsed was determined to have lytic activity, and the case where the sphere shape remained remained was determined to have no lytic activity.

(Influenza virus inactivation test: Test example 2)
Examples 3 and 4 and Comparative Examples 6 to 10 described below were cut into 33 mm squares as test pieces and placed in sealed containers, each containing 0.5 mg of influenza virus per ml. Was sprayed into a 0.5 ml container and then treated at room temperature for 15 hours. Thereafter, an aqueous solution containing 1 mg of inactivated influenza virus per 1 ml is sprayed in a 0.5 ml container to block the antibody, and the treated test piece is washed out with 9 ml of a phosphate buffer solution. After inoculating the eggs and culturing at 37 ° C. for 48 hours, the CAM solution was collected and subjected to HA test, and the virus infectivity EID ₅₀ (50% egg-infective doses) was calculated by the Karber method. In the blank test, a filter not subjected to protein loading was used.

(Enzyme activity test: Test example 3)
The protein-carrying filters of Examples 1 and 2 and Comparative Examples 1 to 5 described below were allowed to stand for 24 hours in a constant temperature and humidity chamber at a temperature of 50 ° C. and a relative humidity of 50%, and then subjected to the test shown in Test Example 1. did.

(Enzyme activity test: Test example 4)
The protein-carrying filters of Examples 3 and 4 and Comparative Examples 6 to 10 described below were allowed to stand in a constant temperature and humidity chamber at a temperature of 50 ° C. and a relative humidity of 50% for 24 hours, and subjected to the test shown in Test Example 2. .

Example 1
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain having a purity of 0.9 is suspended so that the total protein amount becomes 1% by mass, and further an aqueous solution containing 0.3% by mass polyethylene oxide is added. Then, after the carrier sheet 1 was immersed for 1 hour, the carrier that had been taken out and removed the excess adhering moisture was dried in a dryer maintained at a temperature of 60 ° C. for 10 minutes to prepare a protein-carrying filter.

(Example 2)
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain with a purity of 0.5 is suspended so that the total protein mass is 1% by mass, and further, an aqueous solution containing 0.3% by mass polyethylene oxide is added. Then, after the carrier sheet 1 was immersed for 1 hour, the carrier that had been taken out and removed the excess adhering moisture was dried in a dryer maintained at a temperature of 60 ° C. for 10 minutes to prepare a protein-carrying filter.

(Comparative Example 1)
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain having a purity of 0.8 was suspended so that the total protein mass was 1% by mass, and further an aqueous solution containing 0.3% by mass polyethylene glycol was added. After the carrier sheet 1 was soaked for 1 hour, the carrier from which the extra adhering moisture was removed was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter.

(Comparative Example 2)
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain having a purity of 0.8 was suspended so that the total protein mass was 1% by mass, and further an aqueous solution containing 0.3% by mass sodium alginate was added. After the carrier sheet 1 was soaked for 1 hour, the carrier from which the extra adhering moisture was removed was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter.

(Comparative Example 3)
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain having a purity of 0.99 is suspended so that the total protein mass is 1% by mass, and further an aqueous solution containing 0.3% by mass polyethylene oxide is added. After the carrier sheet 1 was soaked for 1 hour, the carrier from which the extra adhering moisture was removed was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter.

(Comparative Example 4)
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain having a purity of 0.99 is suspended so that the total protein mass is 1% by mass, and further, an aqueous solution containing 0.3% by mass polyethylene glycol is added. After the carrier sheet 1 was soaked for 1 hour, the carrier from which the extra adhering moisture was removed was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter.

(Comparative Example 5)
In 100 mM Tris-HCl buffer (pH 8.0), a bromelain having a purity of 0.99 was suspended so that the total protein mass was 1% by mass, and further an aqueous solution containing 0.3% by mass sodium alginate was added. After the carrier sheet 1 was soaked for 1 hour, the carrier from which the extra adhering moisture was removed was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter.

(Example 3)
Prepare an aqueous solution containing a 100 mM phosphate buffer (pH 7.0) containing an anti-influenza yolk-derived antibody (IgY) with a purity of 0.9 at a total protein concentration of 5 mg / ml and polyethylene oxide of 0.3% by mass. Then, after the carrier sheet 1 was immersed in the aqueous solution for 1 hour, the carrier, which was taken out and removed the excess adhering moisture, was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter. .

Example 4
Prepare an aqueous solution containing a 100 mM phosphate buffer (pH 7.0) containing an anti-influenza yolk-derived antibody (IgY) with a purity of 0.5 and a total protein concentration of 5 mg / ml and polyethylene oxide of 0.3% by mass. Then, after the carrier sheet 1 was immersed in the aqueous solution for 1 hour, the carrier, which was taken out and removed the excess adhering moisture, was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter. .

(Comparative Example 6)
An aqueous solution containing a 100 mM phosphate buffer (pH 7.0) containing an anti-influenza yolk-derived antibody (IgY) with a purity of 0.8 and a total protein concentration of 5 mg / ml and polyethylene glycol of 0.3% by mass. After the carrier sheet 1 is soaked in the aqueous solution for 1 hour, the carrier, which has been taken out and freed of excess adhering moisture, is dried for 10 minutes in a dryer maintained at a temperature of 60 ° C. to prepare a protein-carrying filter. did.

(Comparative Example 7)
Prepare an aqueous solution containing a 100 mM phosphate buffer (pH 7.0) containing an anti-influenza yolk-derived antibody (IgY) with a purity of 0.8 at a total protein concentration of 5 mg / ml and sodium alginate of 0.3% by mass. Then, after the carrier sheet 1 was immersed in the aqueous solution for 1 hour, the carrier, which was taken out and removed the excess adhering moisture, was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter. .

(Comparative Example 8)
Prepare an aqueous solution containing a 100 mM phosphate buffer (pH 7.0) containing an anti-influenza egg yolk-derived antibody (IgY) with a purity of 0.99 and a total protein concentration of 5 mg / ml and 0.3% by mass of polyethylene oxide. Then, after the carrier sheet 1 was immersed in the aqueous solution for 1 hour, the carrier, which was taken out and removed the excess adhering moisture, was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter. .

(Comparative Example 9)
Prepare an aqueous solution containing a 100 mM phosphate buffer (pH 7.0) containing an anti-influenza yolk-derived antibody (IgY) with a purity of 0.99 and a total protein concentration of 5 mg / ml and polyethylene glycol of 0.3% by mass. Then, after the carrier sheet 1 was immersed in the aqueous solution for 1 hour, the carrier, which was taken out and removed the excess adhering moisture, was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter. .

(Comparative Example 10)
Prepare an aqueous solution of 100 mM phosphate buffer (pH 7.0) containing an anti-influenza yolk-derived antibody (IgY) with a purity of 0.99 and a total protein concentration of 5 mg / ml and sodium alginate of 0.3% by mass. Then, after the carrier sheet 1 was immersed in the aqueous solution for 1 hour, the carrier, which was taken out and removed the excess adhering moisture, was dried for 10 minutes in a drier kept at a temperature of 60 ° C. to prepare a protein-carrying filter. .

  The enzyme activity test shown in Test Example 1 was performed on the protein-carrying filters of Examples 1-2 and Comparative Examples 1-5. The results are shown in Table 1. In Examples 1 and 2 and Comparative Example 3, the decay of Luteus by lysozyme lysis was confirmed. In Comparative Examples 1, 2, 4 and 5, the decay of Luteus was not confirmed.

  The enzyme activity test shown in Test Example 3 was performed on the protein-carrying filters of Examples 1-2 and Comparative Examples 1-5. The results are shown in Table 1. In Examples 1 and 2, the decay of Luteus by lysozyme lysis was confirmed. On the other hand, in Comparative Examples 1-5, the decay | disintegration of Luteus bacteria was not confirmed.

The influenza virus inactivation test shown in Test Example 2 was performed on the protein-carrying filters of Examples 3 to 4 and Comparative Examples 6 to 10. The results are shown in Table 1. As a result of the blank test, the virus infection titer was EID ₅₀ = 0.5 × 10 ^8.5 . The viral infectivity values of Examples 3 and 4 and Comparative Example 8 are EID ₅₀ = 0.5 × 10 ^3.9 , 0.5 × 10 ^4.1 , 0.5 × 10 ^4.4 in this order, and protein It was confirmed that the amount of activated virus by the carrier filter was reduced by 4 orders of magnitude, that is, 99.99% inactivation. On the other hand, the virus infectivity values of Comparative Examples 6, 7, 9, and 10 were EID ₅₀ = 0.5 × 10 ^7.1 , 0.5 × 10 ^7.5 , 0.5 × 10 ^7.3 , and. 5 × 10 ^7.5 , which was an order of magnitude decrease in the amount of activated virus, ie 90% inactivation.

The influenza virus inactivation test shown in Test Example 4 was performed on the protein-carrying filters of Examples 3 to 4 and Comparative Examples 6 to 10. The results are shown in Table 1. As a result of the blank test, the virus infection titer was EID ₅₀ = 0.5 × 10 ^8.5 . The viral infectivity values of Examples 3 and 4 are EID ₅₀ = 0.5 × 10 ^5.1 and 0.5 × 10 ^5.5 , and the amount of activated virus is reduced by 3 orders of magnitude, that is, 99.9% inactive. Was confirmed. On the other hand, the virus infectivity value of Comparative Example 8 was EID ₅₀ = 0.5 × 10 ^7.3 , which was a one-digit decrease in the amount of activated virus, that is, 90% inactivation. Moreover, the viral infectivity values of Comparative Examples 6, 7, 9, and 10 are EID ₅₀ = 0.5 × 10 ^7.9 , 0.5 × 10 ^8.4 , 0.5 × 10 ^8.1 , 0.5 × 10 ^8.2 , and the effect of virus inactivation was very low.

  The protein-carrying filter of the present invention achieves high performance by contributing to the activity expression of proteins such as enzymes and antibodies with low purity by simultaneous addition of polyethylene oxide. Therefore, it can be easily used industrially.

Claims (3)

  A filter in which polyethylene oxide is impregnated with a protein having a purity value of 0.9 or less determined by the amount of effective protein / total protein.   The filter according to claim 1, wherein the effective protein is bromelain. The filter according to claim 1, wherein the effective protein is an egg yolk-derived antibody (IgY).