United States Patent 119] [11] Patent Number: 4,576,817 Montgomery et al. [45] Date of Patent: Mar. 18, 1986

[54] ENZYMATIC BANDAGES AND PADS 4,226,232 lO/l980 Spence ...... 128/156 Inventors: Robert E. Montgomery, Paci?c 4,269,822 5/1981 14111666141...... 424/94x [75] 4,379,141 4/1983 Hasegawa 61 al...... 424/94 Palisades; Michael A. Pellico, Los 4,476,108 lO/l984 108851616441...... 424/13ox Angeles, both of Calif. 4,486,408 12/1984 Kiel ...... 424/94 [73] Assignee: Laclede Professional Products, Inc., 4,537,764 8/1985 Pellico et al...... 424/94 X Gardena, Calif. FOREIGN PATENT DOCUMENTS

[21] Appl. No.: 618,071 2488797 2/1982 France ...... 424/94 [22] Filed: Jun. 7, 1984 Primary Examiner—Helen M. McCarthy Attorney, Agent, or Firm—Donald Diamond [51] Int. Cl.‘ ...... A61K 37/48 [52] U.S. Cl...... 424/94; 128/127; [57] ABSTRACT 128/156; 424/ 130; 435/25; 604/375; 604/904 [58] Field of Search ...... 604/289, 369, 375, 904; Enzymatic absorbent materials such as bandages and 424/14, 94, 130; 128/127, 130, 156; 435/25 pads, for body contact applications, contain serum activated for producing hydro [56] References Cited gen peroxide upon contact of the enzymatic materials U.S. PATENT DOCUMENTS with serum. An illustrative serum-activated oxidore

4,031,202 6/1977 Laughlin et al...... 128/130 X ductase enzyme is glucose oxidase with the correspond 4,122,158 10/1978 Schmitt ...... 424/94 X ing substrate in serum being glucose. 4,150,113 4/1979 Hoogendoorn et al...... 424/50 4,178,362 12/1979 Hoogendoorn et al...... 424/94 X 20 Claims, No Drawings 4,576,817 1 2 It would, of course, be advantageous to provide ab ENZYMATIC BANDAGES AND PADS sorbent materials in the form of bandages, pads, strings and the like that would inhibit bacterial growth in body BACKGROUND OF THE INVENTION ?uids which are absorbed by or otherwise associated This invention relates to absorbent materials adapted with such absorbent materials or structures. for use in body contact applications and, more particu It is disclosed in the prior art that polymeric wound larly, to enzymatic absorbent materials such as ban dressings for burns may include antibacterial agents, dages and pads that produce a bacteriostatic effect upon antibiotics, antifungal agents, proteolytic as contact with body ?uids such as serum. well as local anesthetics, hormonal compounds and Absorbent materials in the form of bandages and pads lubricating and barrier chemicals. See, for example, have long been employed in body contact applications U.S. Pat. No. 4,122,158 (Schmitt, 1978) and U.S. Pat. where coverage and protection of a wound and absorp No. 4,226,232 (Spence, 1980). tion of its ?uids are desirable. Bandaging can serve to It is also disclosed in the prior art that enzymatic physically protect an open wound from the surrounding agents can be incorporated into oral products such as environment, which is often replete with harmful bac toothpaste and chewing gum for producing hydrogen teria, and to absorb ?uid materials such as pus, blood peroxide during oral use. and serum to thereby promote the healing of the U.S. Pat. No. 4,150,113 (Hoogendoom et al., 1979) wound. Accordingly, bandages are constructed of and U.S. Pat. No. 4,178,362 (Hoogendoom et al., 1979) strong, yet absorbent, materials such that retention of disclose, respectively, an enzymatic toothpaste and an extraneous ?uids can be accomplished without a con enzymatic chewable dentifrice containing glucose oxi commitant loss of strength. dase which acts on glucose present in saliva and tooth Absorbent materials such as woven ?bers, porous plaque to produce . The patentees foam pads, absorbent membranes and solvent-based note that oral bacteria, through enzymes systems having porous elastomers have been utilized in the manufacture SH-GROUPS, effect glycolysis of food products con of bandages and pads. A wide of variety of raw materi taining sugars and point out that , which als have been employed in an attempt to obtain physi is present in saliva, provides the means for transferring cally occlusive structures that retain their strength oxygen from hydrogen peroxide to the oral bacteria when soaked with ?uid from an open or weeping resulting in the oxidation of the SH-containing enzymes wound or other body ?uid source. Materials such as into inactive disul?de enzymes. It is further disclosed cellulose and its derivatives (cellulosics), polyester, 30 that the dentifrice may be formulated with potassium nylon, polyacrylamide, collagen, polyurethane and pol thiocyanate. yvinyl alcohol have been fabricated into structures such U.S. Pat. No. 4,269,822 (Pellico et al., 1981) discloses as woven ?bers, foam pads, porous membranes, elasto an antiseptic dentifrice containing an oxidizable amino mers and multi-layered combinations of the aforemen acid substrate and an oxidoreductase enzyme speci?c to tioned structures. Regardless of the material used, all such substrate for producing hydrogen peroxide and bandages and pads employed in the protection of open ammonia upon oral application of the dentifrice, with wounds must satisfy the requirement of good absor pre-application stability being maintained by limiting bency in order to be effective. the quantity of any water present in the dentifrice. An absorbent material in contact with an open or SUMMARY OF THE INVENTION weeping wound will retain a substantial amount of In accordance with one aspect of this invention, there blood, blood serum, pus and a variety of wound exu is provided enzymatic absorbent material for body dates. Bandages are often constructed in such a way that moisture retained by the absorbent material in contact application containing, per gram of material, from about 1.0 to about 1,000 International Units of contact with the wound will transpire through the side 45 serum-activated oxidoreductase enzyme for producing of the bandage opposite to that of the source of the hydrogen peroxide upon contact of said material with ?uids, i.e., the open wound. Although structures such as serum. these tend to decrease the amount of moisture retained In accordance with a second aspect of this invention, by the absorbent material, other exudates such as white there is provided enzymatic absorbent ?ber for conver blood cells, bacteria, eletrolytes, and red blood cells are sion into enzymatic absorbent material that is adapted retained. These exudates accumulate as a function of the for body contact application, wherein the ?ber con amount of time an absorbent material is in contact with tains, per gram of ?ber, from about 1.0 to about 1,000 an open or weeping wound. International Units of serum-activated oxidoreductase As a result of the retention of such a wide variety of enzyme for producing hydrogen peroxide upon contact biological substances, a moist absorbent structure can with serum. become an effective breeding ground for potentially harmful bacteria. Such an absorbent structure in contact DETAILED DESCRIPTION with body ?uid of the type mentioned above can be The enzymatic absorbent materials of this invention characterized as a culture support medium that can give comprise ?uid absorbent structures that incorporate rise to a large number of potentially harmful bacterial serum-activated oxidoreductase enzyme for producing colonies in a relatively small volume. Since the accumu hydrogen peroxide upon contact with serum. Fluid lated bacteria and their ‘waste products remain in absorbent structures, in the form of bandages, pads, contact with the open or weeping wound, they can strips and the like, can be prepared from precursors and leach out of the absorbent structure and back to the by processes well-known in the art to provide appropri body. In this connection, symptoms classi?able as toxic 65 ate designs and con?gurations that are adapted for par shock syndrome have been associated with the use of ticular body contact applications. Structural precursors certain types of feminine hygiene tampons, i.e., inter such as woven ?bers, porous foam pads, absorbent nally disposed feminine hygiene absorbent pads. membranes and solvent-based porous elastomers can be 4,576,817 3 4 utilized in the manufacture of the ?uid absorbent struc Oxygen-accepting anions in serum include thiocya tures. Gauze bandaging alone or secured to adhesive nate, chloride and iodide ions which, in the presence of strip and feminine hygiene absorbent pads and tampons, hydrogen peroxide and , are oxidized to as well as other externally and internally utilizable body hypothiocyante, and hypoiodite, respec contact devices having high absorbency characteristics, tively. . can be advantageously utilized in the practice of this The enzymatic absorbent material described herein invention. may be augmented by additionally incorporating into The enzymatic absorbent material of this invention, the material supplementary ingredients as, for example, which incorporates oxidoreductase enzyme, is adapted (a) oxidizable substrate speci?c to the oxidoreductase to be used in body contact applications that encounter enzyme utilized in the material, and (b) oxidizable salt body ?uids. These ?uids, including blood and tissue such as the thiocyanate, chloride or iodide salt of so serum, contain oxidizable substrate and other ingredi dium, potassium, ammonium, calcium or magnesium or ents which undergo an enzymatic reaction in the pres mixtures of such salts. ence of oxidoreductase enzyme speci?c to the substrate The oxidizable substrate is generally present in the to produce hydrogen peroxide. oxidoreductase en enzymatic absorbent material in an amount from about zymes which can be utilized in the practice of this in 0.015 to about 0.6 millimole per gram of material and, vention and the corresponding oxidizable substrates in preferably, in an amount from about 0.025 to about 0.1 serum are set forth in the following table: millimole per gram of material. The oxidizable salt is TABLE A generally present in the enzymatic absorbent material in 20 an amount from about 0.0001 to about 0.01 millimole OXIDOREDUCTASE OXIDIZABLE ENZYME SUBSTRATE per gram of material and, perferably, from about 0.001 to about 0.006 millimole per gram of material. The term Glucose Oxidase B-D-glucose Hexose Oxidase Hexose millimole identi?es that quantity in grams correspond ing to the molecular weight of the composition divided Cholesterol Oxidase Cholesterol 25 Galactose Oxidase D-galactose by one thousand. Pyranose Oxidase Pyranose The operable integrity of the enzymatic system can Choline Oxidase Choline Pyruvate Oxidase Pyruvate be affected by which is present in commercial Oxalate Oxidase Oxalate glucose oxidase as well as mucous membrane tissue, Glycollate Oxidase Glycollate 30 blood and blood serum. Catalase, which is extraneous to D-aminoacid Oxidase D-aminoacid the enzymatic system of this invention, competes with lactoperoxidase for hydrogen peroxide. In order to In an illustrative enzymatic reaction, glucose oxidase reduce loss of hydrogen peroxide through the presence in the enzymatic absorbent material catalyzes the inter of catalase, an effective amount of an enzymatic inhibi action of Beta-D-glucose, water and oxygen in the 35 tor speci?c to catalase can be advantageously incorpo serum to produce hydrogen peroxide and gluconic acid. rated into the enzymatic absorbent material. An ascor Glucose oxidase is characterized in the literature as a bic salt such as sodium ascorbate, potassium ascorbate, glycoprotein containing two molecules of ?avine-ade ascorbyl palmitate, or mixtures thereof can be used as "inine dinucleotide which has a molecular weight of ap an enzymatic inhibitor which is speci?c to catalase. An rproximately 150,000, an isoelectric point at pH 4.2 and 40 effective amount of ascorbate salt for catalase inhibition "an optimum pH at 5.5 with a broad pH range from 4 is from about 0.000001 to about 0.0001 millimole per through 7. gram of enzymatic absorbent material. Iron salts such as The oxidoreductase enzyme is generally present in ferrous sulfate can be incorporated into the enzymatic the enzymatic absorbent material in an amount from absorbent material as a potentiator for ascorbate salt in about 1.0 to about 1,000 International Units (hereinafter 45 its role as catalase inhibitor. sometimes abbreviated as IU) per gram of material and, The enzymatic material of this invention may advan preferably, in an amount from about 10 to about 500 IU tageously be formulated with an aminohexose as, for per gram of material. The term International Unit(s) example, an aminoglucose such as glucosamine, N identi?es that amount of enzyme that will effect cataly acetyl glucosamine or mixtures thereof in order to in sis of 1.0 micromole of substrate per minute at pH 7.0 50 crease the yield or accumulation of oxidized anionic and 25° C. Oxidoreductase enzymes are supplied in dry bacterial inhibitor. The aminoglucose is generally pres or liquid form with the label specifying the concentra ent in the enzymatic material in an amount from about tion in International Units on a per gram or per milliliter 0.0001 to about 0.002 millimole per gram of enzymatic basis, as appropriate. material and, preferably, in an amount from about 0.003 7 In addition to the oxidoreductase enzyme for produc 55 to about 0.001 millimole per gram of enzymatic mate ing hydrogen peroxide, the enzymatic material can be rial. provided with a second enzyme, namely, a peroxidatic In an alternative embodiment of this invention, the peroxidase for interacting with hydrogen peroxide and oxidoreductase enzyme can be incorporated into absor an oxygen-accepting anion in serum for producing an bent ?bers of natural or synthetic materials for conver oxidized anionic bacterial inhibitor. which 60 sion into enzymatic bandages and pads. can be used in the practice of this invention include The enzymes of this invention may be advanta lactoperoxidase, , iodide peroxi geously encapsulated to enhance storage stability in the dase, chloride peroxidase and . The enzymatic bandage or pad until utilization of the same. peroxidase is generally present in the enzymatic absor The encapsulating material can be composed of a water bent rnaterial in an amount from about 0.1 to about 65 soluble polymer or a polymer permeable to a substrate 10,000 International Units per gram of material, and, speci?c to the enzyme or enzymes contained therein. preferably, in an amount from about 10 to about 500 An illustrative encapsulating material is carboxymethyl International Units per gram of material. cellulose. 4,576,817 5 6 The enzymatic absorbent materials can be prepared and admixed with the cellulose triacetate solution for 30 by various procedures including: (a) solution deposition minutes which resulted in an emulsion of the aqueous of the oxidoreductase enzyme and optional ingredients phase in the organic phase. onto the absorbent structure, (b) incorporation of the Fibers were formed from the enzymes/polymer oxidoreductase enzyme into a spinning solution that is emulsion by wet spinning technique. A 10 ml hypoder extruded as ?ber ?lament which can be converted into bandages and pads, and (c) incorporation of the oxido mic syringe was ?lled with the emulsion. The syringe reductase enzyme into the chemical constituency which was used to extrude the emulsion through a No. 20 form polymeric foams and subsequent injection or sol hypodermic needle into 100 m1 of toluene that was contained in a 150 ml graduated cylinder. vent despostion of the aforementioned optional ingredi 10 ents as well as other special purpose additives. During the extrusion process, the emulsion coagu lated as a ?ber in the form of ringlets about 2 cm in EXAMPLE I diameter which slowly settled to the bottom of the This example illustrates the solution depositiontof an graduated cylinder. The rate of extrusion was con oxidoreductase enzyme onto a spun cotton pad and the trolled to provide a continuous ?ber strand of the ring bacteriostatic effect of the resulting enzymatic pad. lets at a rate slow enough to prevent sticking at the An aqueous enzymatic solution was prepared by add bottom of the cylinder. Upon completion of the extru ing 0.2 gm of polyvinylpyrolidone (Mol. Wt. 250,000) sion step, the ?bers were removed from the toluene bath and 1,000 IU of glucose oxidase (approx. 4.0 mg) to a and air-dried before testing for bacteriostatic properties. vessel containing 10 ml of distilled water with stirring 20 Approximately 9.6 gm of ?ber were obtained. through the use of a magnetic stirring bar and electric The ?ber was assayed for activity in respect of both stirrer. Low turbulence was maintained during stirring glucose oxidase and lactoperoxidase. An activity of 300 to avoid any impairment of the enzyme. IU per gram of ?ber was obtained for each enzyme. A spun cotton pad with dimensions of 3.0 cm by 3.0 A ?rst control ?ber was prepared by the foregoing cm by 1.0 cm was impregnated with 1.0 ml of the aque 25 extrusion procedure, except that the extrusion composi ous enzyme solution by applying the solution to the pad tion did not contain either glucose oxidase or lac through a standard medicinal dropper. The residual toperoxidase. A second control ?ber was prepared in water was allowed to evaporate from the pad at room accordance with the procedure used in the preparation temperature (25° C). The resulting pad and a non of the ?rst control ?ber, except that the extrusion com enzymatic control pad were tested for bacteriostatic 30 position was modi?ed to contain bovine serum albumin, properties. a protein. Neither of the control ?bers showed any The enzymatic and non-enzymatic pads were placed enzyme activity in tests for either glucose oxidase or in separate culture tubes, and approximately 10 ml of lactoperoxidase. human blood serum was added to each of the culture The ?bers described above are of the type that are tubes. The tubes were then innoculated with Staphylo 35 suitable for the manufacture of woven bandages. caccus aureus at a concentration level of 1.0>< l05 organ The ?bers were tested for bacteriostatic properties isms per milliliter of serum and assayed for bacterial using Staphylococcus aureus (ATCC 653A) and E. coli counts at the end of each 4-hour segment for 24 hours. (ATCC 25923). Each organism was inoculated into a 20 Cultures to determine counts were prepared from tryp ml portion of tryptic soy broth and incubated at 35° C. tic soy agar and incubated at 35° C. for 48 hours under 40 for 24 hours. Each of the resulting cultures was washed aerobic conditions. The results are set forth in the fol lowing table: with a phosphate buffer (pH 6.5 and 0.01 M) by centri fuging to obtain a suspension of cells, which was diluted TABLE I 1:10. Glucose Oxidase Fresh human blood serum samples were prepared in Enzymatic Pad Non-Enzymatic Pad 45 6 screw cap tubes that held 20 ml of serum in each. Time, hr. S. aureus Count/ml S. aureus Count/ml Twenty microliters of the diluted bacterial cell suspen 0 1.2 >< 105 1.4 x 105 sion were inoculated into each of the tubes containing 4 8.6 >< 104 2.9 X 105 s 6.6 x 104 8.5 >< 10S serum. Thereafter, a 100 mg ?ber sample was placed in 12 5.9 X 104 4.4 x 106 . each of the inoculated serum tubes which were incu 16 5.1 X 104 9.1 X 106 bated at 35° C. for the duration of the testing. Occa 20 4.0 X 104 3.6 X 107 sional manual agitation of the tubes was undertaken 24 3.2 X 104 7.0 X 107 during the test period. Bacterial counts of the samples were taken at the end EXAMPLE II of each 4-hour segment for 24 hours. Tryptic soy agar 55 was used as the plating medium for each sample and the This example illustrates the preparation of enzymatic plates were incubated at 35" C. for 48 hours under aero ?bers by incorporating oxidoreductase enzyme and bic conditions. The results are set forth in the following peroxidatic peroxidase enzyme into a Wet spinning solu table: tion that is extruded in ?ber form. In addition, this ex ample illustrates the bacteriostatic effect of the resulting 60 TABLE II enzymatic ?ber. Time, hr. S. aureus Count E. 0011' Count/m] To methylene dichloride contained in a 250 ml bea 2A ker, there was added 10 gm of celluose triacetate in Enzymatic Fiber pellet form to bring the total volume of the contents to Glucose Oxidase & Lactoperoxidase 100 ml. An aqueous enzymatic solution having a vol 65 0 2.0 X 105 1.0 X 105 ume of 15 ml was prepared by admixing glucose oxidase 4 6.2 x 103 3.2 X 104 s 2.0 x 103 2.2 x 104 (500 IU/ml) and lactoperoxidase (500 IU/ml) with dis 12 1.8 X 103 7.6 >< 1o3 tilled water. The aqueous enzyme solution was added to 16 <1,0o0 5.1 x 103 4,576,817 7 8 TABLE II-continued was prepared by placing 5 grams of non-enzymatic foam in a culture tube containing 10 ml of whole pig’s Time, hr. S. nureus Count E. 0011' Count/ml blood which was inoculated with approximately 2o <300 1.4 >< 1o3 200,000 organisms of S. aureus. Bacterial counts, per 24 <10o <100 one ml of blood, were taken at the end of each 4-hour Non-Enzymatic Fiber segment for 24 hours. The results are set forth in the 0 2.0 >< 105 1.0 X 105 following table: 4 6.6 X 105 9.5 >< 105 s 2.1 X 106 5.1 X 107 TABLE III 12 8.8 X 106 4.9 X 108 16 2.2 >< 107 1.0 X 109 10 Glucose Oxidase 20 3.7 >< 107 1.1 x 109 Enzymatic Foam Non-Enzymatic Foam 24 5.0 X 107 1.6 x 10° Time, hr. S. aureus Count E. coli Count/ml o 2.0 X 105 2.0 >< 1o5 Fiber/Bovine Serum Albumin 4 9.6 x 104 3.5 x 105 0 2.0 X 105 1.0 X 105 s 2.2 X 104 5.8 x 105 4 4.5 x 105 9.5 >< 105 15 12 5.0 X 104 3.9 >< 106 s 9.9 x 105 5.3 x 106 16 6.6 X 103 1.7 x 107 12 6.1 X 106 8.9 x 106 20 3.4 X 103 6.8 x 107 16 8.4 X 106 1.2 X 107 24 2.2 X 103 9.5 X 107 20 1.0 >< 107 8.6 X 107 24 4.2 >< 107 2.1 x 109 20 By incorporating a spermicidal composition in the enzymatic foam, a contraceptive ?exible foam pad is EXAMPLE III I obtained. This example illustrates a method for incorporating EXAMPLE IV oxidoreductase enzyme into yieldable, semi-rigid foam and the bacteriostatic properties of the resulting enzy 25 This example illustrates an enzymatic pad which is matic foam. self-contained with respect to oxidoreductase enzyme An aqueous enzyme solution was prepared by admix and corresponding oxidizable substrate for producing ing 1,000 IU of glucose oxidase (approx. 4.0 mg) with 40 hydrogen peroxide in the presence of serum. ml of cold, distilled water, under moderate agitation, An enzymatic solution was prepared by dissolving, until the enzyme dissolved. with stirring, glucose oxidase (5,000 IU) and glucose An isocyanate terminated, prepolymer solution was (5.0 gm) in methylene dichloride (50 ml). One millime prepared by reacting stoichiometric amounts of 80/20 ter of the enzymatic solution was added to a spun cotton 2,4-/2,8 tolylenediisocyanate and Carbowax 1,000 poly pad similar to that described in Example I to effect oxyethylene polyol (Mol. Wt. 1,000) at 135° C. for 5 solution deposition of the ingredients. hours in the presence of a catalyst comprising 2-ethyl 35 hexanoic acid and tin octoate. The resulting urethane EXAMPLE V prepolymer was diluted to 90% solids with acetone. This example illustrates an enzymatic pad which is To 24.5 gm of the acetone solution of prepolymer, self-contained with respect to oxidoreductase enzyme, there was added 0.22 gm of Tween 80 (a polyoxyethyl oxidizable substrate, peroxidatic enzyme and oxidizable ene derivative of sorbitan fatty acid ester having a mo 40 salt for producing an oxidized anionic bacterial inhibitor lecular weight of about 1,309) and the viscous mixture in the presence of serum. was stirred by hand for approximately 30 seconds. An enzymatic solution was prepared by dissolving, Twenty milliliters of the aqueous enzyme solution was with stirring, glucose oxidase (1,000 IU), glucose (10 added to the prepolymer composition and the resulting gm), lactoperoxidase (500 IU), and potassium thiocya paste-like mixture was stirred to obtain a dispersion of 45 nate in methylene dichloride (50 ml). One millimeter of the ingredients. The remaining aqueous enzyme solu the enzymatic solution was added to a spun cotton pad tion was then added to the reaction mixture which was similar to that described in Example I to effect solution again stirred to obtain dispersion of the ingredients. deposition of the ingredients. Upon completion of the enzyme addition and dispersion 50 In view of the foregoing description and examples, it steps, the reacting mass was poured into a Petri dish will become apparent to those of ordinary skill in the art (100 mm diameter) and allowed to remain at ambient temperature for 5 minutes at which time the reaction that equivalent modi?cations thereof may be made was substantially complete. without departing from the spirit and scope of this in There was obtained from the reaction a white, vention. spongy, wet, semi-rigid, enzymatic foam that was ap 55 That which is claimed is: proximately l.2 to 1.4 centimeters thick. The wet foam 1. An enzymatic substantially organic absorbent ma was removed from the dish and stored in a refrigerator terial for body contact application containing, per gram at approximately 5° C., with the foam remaining damp of material, from about 1.0 to about 1,000 International during storage. One gram of this foam material (dry Units of serum-activated oxidoreductase enzyme for weight) was assayed for glucose oxidase activity using 60 producing hydrogen peroxide upon contact of said glucose as a substance, horseradish peroxidase and o material with serum. dianisidine as a chromogen. The activity of the one 2. The enzymatic material of claim 1 wherein the gram piece of foam was approximately 12 IU per gram, concentration of oxidoreductase enzyme is from about or about 60% of the original activity. 10 to about 500 International Units. Five grams of enzymatic foam (dry weight) were 65 3. The enzymatic material of claim 1 wherein the placed in a large culture tube containing 10 m1 of whole oxidoreductase enzyme is glucose oxidase. pig’s blood. The blood was inoculated with approxi 4. The enzymatic material of claim 1 wherein the mately 200,000 organisms of S. aureus. A control tube oxidoreductase enzyme is oxalate oxidase. 4,576,817 10 5. The enzymatic material of claim 1 which also con ing anion selected from the group consisting of thiocya tains from about 0.1 to about 10,000 International Units nate, chloride and iodine or mixtures of such salts. of peroxidatic peroxidase per gram of material. 14. The enzymatic material of claim 13 wherein the 6. The enzymatic material of claim 5 wherein the concentration of the alkali metal salt is from about 0.001 concentration of peroxidatic peroxidase is from about to about 0.006 per gram of material. 10 to about 500 International Units per gram of mate 15. The enzymatic material of claim 13 wherein the rial. alkali metal salt is potassium thiocyanate. 7. The enzymatic material of claim 5 wherein the 16. The enzymatic material of claim 1 which also peroxidatic peroxidase is lactoperoxidase. contains an aminoglucose selected from the group con 8. The enzymatic material of claim 5 wherein the sisting of glucosamine, N-acetyl glucosamine and mix peroxidatic peroxidase is myeloperoxidase. tures thereof in an amount from about 0.001 to about 9. The enzymatic material of claim 1 which also con 0.002 millimole per gram of material. tains, per gram of material,‘ from about 0.03 to about 1.2 17. The enzymatic material of claim 16 wherein the millimoles of substrate speci?c to oxidoreductase en aminoglucose is present in an amount from about 0.0003 zyme in said material for producing hydrogen peroxide 15 to about 0.001 millimole per gram of material. upon contact of said material with serum. 18. The enzymatic material of claim 1 which also 10. The enzymatic material of claim 9 wherein the contains an effective amount of an enzymatic inhibitor concentration of substrate is from about 0.06 to 0.6 speci?c to catalase. millimoles per gram of material. 19. The enzymatic material of claim 18 wherein the 20 11. The enzymatic material of claim 9 wherein the catalase inhibitor is an ascorbate salt in an amount from substrate is glucose and the oxidoreductase enzyme is about 0.000001 to about 0.0001 millimole per gram of glucose oxidase. material. 20. An enzymatic substantially organic, absorbent 12. The enzymatic material of claim 11 which also ?ber for conversion into enzymatic absorbent material contains from about 0.1 to about 10,000 International 25 for body contact application containing, per gram of Units of lactoperoxidase per gram of material. ?ber, from about 1.0 to about 1,000 International Units 13. The enzymatic material of claim 5 which also of serum-activated oxidoreductase enzyme for produc contains, per gram of material, from about 0.000lto ing hydrogen peroxide upon contact with serum. about 0.01 millimole of a metal salt of an oxygen accept * * * * 1k 30

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