CA1258228A - Enzymatic bandages and pads - Google Patents

Abstract

ENZYMATIC BANDAGES AND PADS
ABSTRACT OF THE DISCLOSURE
Enzymatic absorbent materials such as bandages and pads, for body contact applications, contain serum-activated oxidoreductase enzyme for producing hydrogen peroxide upon contact of the enzymatic materials with serum. An illustrative serum-activated oxidoreductase enzyme is glucose oxidase with the corresponding substrate in serum being glucose.

Description

j~ 1'251~3~28 1 BACKGROUND OF T~E INVENTION

3 This invention relates to absorbent materials adapted for 4 use in body contact applications and, more particularly, to enzymatic absorbent materials such as bandages and pads that 6 produce a bacteriostatic effect upon contact with body fluids 7 such as serum.
8 Absorbent materials in the form of bandages and pads have 9 long been employed in body contact applications where coverage and protection of a wound and absorption of its fluids are 11 desirable. Bandaging can serve to physically protect an open 12 wound from the surrounding environment, which is often replete 31 with harmful bacteria, and to absorb fluid materials such as 14 I pus, blood and serum to thereby promote the healing of the 15 ¦ wound. Accordingly, bandages are constructed of strong, yet lG ! absorbent, materials such that retention of extraneous fluids 17 ¦ can be accomplished without a concommitant loss of strength.
18 ! Absorbent materials such as woven fibers, porous foam 19 i pads, absorbent membranes and solvent-based porous elastomers have been utilized in the manufacture of bandages and pads~ A
21 wide of variety of raw materials have been employed in an 22 attempt to obtain physically occlusive structures that retain 23 their strength when soaked with fluid from an open or weeping 24 wound or other body fluid source. Materials such as cellulose and its derivatives (cellulosics), polyester, nylon, 2G polyacrylamide, collagen, polyurethane and polyvinyl alcohol 27 have been fabricated into structures such as woven fibers, foam 28~ ~ pads, poro~ membranes, elastomers and multi-layered combinationsj I
.~ I -2-~$
, - .

l~SI-3;~:8 1 of the aforementioned structures. Regardless of the material

2 used, all bandages and pads employed in the protection of ope~

3 wounds must satisfy the requirement of good absorbency in order

4 to be effective.
An absorbent material in contact with an open or weeping 6 wound will retain a substantial amount of blood, blood serum, 7 pus and a variety of wound exudates. Bandages are often 8 constructed in such a way that moisture retained by the absorbent material in contact with the wound will transpire through the side of the bandage opposite to that of the source of the 11 fluids, i.e., the open wound. Although structures such as 12 these tend to decrease the amount of moisture retained by the 13 absorbent material, other exudates such as white blood cells, 14 ¦ bacteria, electrolytes, and red blood cells are retained.
15 ¦ These exudates accumulate as a function of the amount of time lG an absorbent material is in contact with an open or weeping ~7 wound.
18 1l As a result of the retention of such a wide variety of 19 I biological substances, a moist a~sorbent structure can become 20 ~ an effective breeding ground for potentially harmful bacteria.
21 Such an absorbent structure in contact with body fluid of the 22¦¦ type mentioned above can be characterized as a culture support 23 j medium that can give rise to a large number of potentially 24 ¦ harmful bacterial colonies in a relatively small volume. Since 25 I the accumulated bacteria and their waste products remain in 2G ¦ contact with the open or weeping wound, they can leech out of 27 ¦ the absorbent structure and back to the body. In this connection 2~ I symptoms classifiable as toxic shock syndrome have been 51~ 28 1 associated with the use of certain types of feminine hygiene 2 tampons, i.e., internally disposed feminine hygiene absorbent 3 pads.
4 It would, of course~ be advantageous to provide absorbent materials in the form of bandages, pads, strings and the like 6 that would inhibit bacterial growth in body fluids which are 7 absorbed by or otherwise associated with such absorbent materials 8 or structuresO
9 It is disclosed in the prior art that polymeric wound 10 j dressings for burns may include antibacterial agents, ¦ antibiotics, antifungal agents, proteolytic enzymes as well as 12 I local anesthetics, hormonal compounds and lubricating and 13 ¦ barrier chemicals. See, for example, U.S. Patent 4,122,158 14 ¦ (Schmitt, 1978) and U.S. Patent 4,226,232 (Spence, ~9~0).
15 , It is also disclosed in the prior art that enzymatic 16 I agents can be incorporated into oral products such as toothpaste 17 I and chewing gum for producing hydrogen peroxide during oral 1~ ¦ use.
19 I U.S. Patent 4,150,113 (Hoogendoorn et al., 1979) and U.S.
20¦¦ Patent 4,178,362 (Hoogendoorn et al., 1979) disclose, 21~¦ respectively, an enzymatic toothpaste and an enzymatic chewable 22 I dentifrice containing glucose oxidase which acts on glucose 23 present in saliva and tooth plaque to produce hydrogen peroxide.
24 The patentees note that oral bacteria, through enæymes systems having SH-GROUPS, effect glycolysis of food products containing 26 ¦ sugars and point out that lactoperoxidase, which is present in 27 I saliva, provides the means for transferring oxygen from hydrogen 28 ¦ peroxide to the oral bacteria resulting in the oxidation of the '.

~ 58X;~8 1 ¦ SH-containing enzymes into inactive disulfide enzymes. It is 2 further disclosed that the dentifrice may be formulated with 3 potassium thiocyanate.
4 U.S. Patent 4,269,822 (Pellico et al., 1981) discloses an antiseptic dentifrice containing an oxidizable amino acid 6 substrate and an oxidoreductase enzyme specific to such substrate 7 ¦ for producing hydrogen peroxide and ammonia upon oral application 8 ¦ of the dentifrice, with pre-application stability being maintainec 9 ~ by limiting the quantity of any water present in the dentifrice.
10 ll 12 l 13 ¦ In accordance with one aspect of this invention, there is 14 I provided enzymatic absorbent material for body contact applicatior 15 , containing, per gram of material, from about 1.0 to about 1,000 lG I International Units of serum-activated oxidoreductase enzyme 17 ' for producing hydrogen peroxide upon contact of said material 18 I with serum.
19 In accordance with a second aspect of this invention, 20¦ there is provided enzymatic absorbent fiber for conversion into 21' enzymatic absorbent material that is adapted for body contact 22¦ application, wherein the fiber contains, per gram of fiber, 23 I from about 1.0 to about 1,000 International Units of serum-24 i activated oxidoreductase enzyme for producing hydrogen peroxide 25 ~ upon contact with serum.

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~l%5~3~ 2~3 3 The enzymatic absorbent materials of this invention comprise 4 fluid absorbent structures that incorporate serum-activated oxidoreductase enzyme for producing hydrogen peroxide upon 6 contact with serum. Fluid absorbent structures, in the form of 7 bandages, pads, strips and the like, can be prepared from 8 precursors and by processes well-known in the art to provide 9 appropriate designs and configurations that are adapted for particular body conLact applications. Structural precursors 11 1 such as woven fibers, porous foam pads, absorbent membranes and 12 I solvent-based porous elastomers can be utilized in the manufactur~
13 I of the ~luid absorbent structures. &auze bandaging alone or 14 secured to adhesive strip and feminine hygiene absorbent pads 15 I and tampons, as well as other externally and internally utilizabl lG I body contact devices having high absorbency characteristics, 17 I can be advantageously utilized in the practice of this inventionO
18 I The enzymatic absorbent material of this invention, which 19 I incorporates oxidoreductase enzyme, is adapted to be used in 20 I body contact applications that encounter body fluids. These 21 fluids, including blood and tissue serum, contain oxidizable 22 I substrate and other ingredients which undergo an enzymatic 23 I reaction in the presence of oxidoreductase enzyme specific to 24 I the substrate to produce hydrogen peroxide. Oxidoreductase 25 ¦ enzymes which can be utilized in the practice of this invention 2G i and the corresponding oxidizable substrates in serum are set 27 ¦ forth in the following table:

125~3~28 OXIDOREDUCTASE OXIDIZABLE
ENZYME SUBSTRATE

4 Glucose Oxidase B-D-glucose Hexose Oxidase Hexose 6 Cholesterol Oxidase Cholesterol 7 Galactose Oxidase D-galactose 8 Pyranose Oxidase Pyranose Choline Oxidase Choline Pyruvate Oxidase Pyruvate 11 Oxalate Oxidase Oxalate 12 Glycollate Oxidase Glycollate 13 I D-aminoacid Oxidase D-aminoacid 14 l 15 ¦ In an illustrative enzymatic reaction, glucose oxidase in lG ¦ the enzymatic absorbent material catalyzes the interaction of 17 I Beta-D-glucose, water and oxygen in the serum to produce hydrogen 18 ¦ peroxide and gluconic acid.
19 , Glucose oxidase is characterized in the literature as a 20 I glycoprotein containing two molecules of flavine-adenine 21 ~ dinucleotide which has a molecular weight of approximately 22 ¦ 150,000, an isoelectric point at pH 4.2 and an optimum pH at 5.5 23 I with a broad pH range from 4 through 7. , 24 I ' The oxidoreductase enzyme is generally present in the 25 i enzymatic absorbent material in an amount from about 1.0 to 26¦l about 1,000 International Units (hereinafter sometimes abbreviatec 27 I as IU) per gram of material and, preferably, in an amount 2~ from about 10 to about 500 IU per gram of material. The term .::

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~ 8 1 International Unit(s) identifies that amount of enzyme that 2 will effect catalysis of l.O micromole of substrate per minute 3 at pH 7.0 and 25C. Oxidoreductase enzymes are supplied in dry 4 or liquid form with the label specifying the concentration in International Units on a per ~ram or per milliliter basis, as fi appropriate.
7 In addi~ion to the oxidoreductase enzyme for producing 8 hydrogen peroxide, the enzymatic material can be provided with a 9 second enzyme, namely, a peroxidatic peroxidase for interacting with hydrogen peroxide and an oxygen-accepting anion in serum Il for producing an oxidized anionic bacterial inhibitor.
12 Peroxidases which can be used in the practice of this invention 13 include lactoperoxidase, horseradish peroxidase, iodide 14 peroxidase, chloride peroxidase and myeloperoxidase. The peroxidase is generally present in the enzymatic absorbent IG material in an amount from about O.l to about lO,OOO
17 International Units per gram of material, and, preferably, in 18 an amount from about lO to about 500 International Units per 19 gram of material.
Oxygen-accepting anions in serum include thiocyanate, 21 chloride and iodide ions which, in the presence of hydrogen 22 peroxide and peroxidase, are oxidized to hypothiocyante, 2.~ hypochlorite and hypoiodite, respectively.
2~ The enzymatic absorbent material described herein may be '~) augmented by additionally incorporating into the material '~G supplementary ingredients as, for example, (a) oxidizable ~)7 substrate specific to the oxidoreductase enzyme utilized in the ~8 material, and (b) oxidizable salt such as the thiocyanate, i ~ 2~8 1 chloride or iodide salt of sodium, potassium, ammonium, calcium 2 or magnesium or mixtures of such salts.
3 The oxidizable substrate is generally present i~ the 4 enzymatic absorbent material in an amount from about 0.015 to about 0.6 millimole per gram of material and, preferablyr in an amount from about 0.025 to about 0.1 millimole per gram of 7 ¦ material. The oxidizable salt is generally present in the 8 ¦ enzymatic absorbent material in an amount from about 0.0001 to 9 1 about 0.01 millimole per gram of material and, perferably, from 10 I about 0.001 to about 0.006 millimole per gram of material. The 11 ¦ term millimole identifies that quantity in grams corresponding 12 I to the molecular weight of the composition divided by one 13 I thousand.
14 I The operable integrity of the enzymatic system can be 15 I affected by catalase which is present in commercial glucose 1~ I oxidase as well as mucous membrane tissue, blood and blood 17 I serum. Catalase, which is extraneous to the enzymatic system 8 I of this invention, competes with lactoperoxidase for hydrogen 19 ' peroxide. In order to reduce loss of hydrogen peroxide through 20 I the presence of catalase, an effective amount of an enzymatic 2,1l inhibitor specific to catalase can be advantageously incorporated 221¦ into the enzymatic absorbent material. An ascorbic salt such 23 ~ as sodium ascorbate, potassium ascorbate, ascorbyl palmitate, 24 I or mixtures thereof can be used as an enzymatic inhibitor which 25 ¦ is specific to catalase. An effective amount of ascorbate salt 2G I for catalase inhibition is from about 0.000001 to about 0.0001 27 I millimole per gram of enzymatic absorbent material. Iron salts 2~ ~ such as ferrous sulfate can be incor~orated into the enzymatic . . I _g_' ' - '

5~3~Z8 1 absorbent material as a potentiator for ascorbate salt in its 2 role as catalase inhibitor.
3 The enzymatic material of this invention may advantageously 4 be formulated with an aminohexose as, for example, an aminoglucose such as glucosamine, N-acetyl glucosamine or mixtures thereof

6 in order to increase the yield or accumulation of oxidized

7 anionic bacterial inhibitor. The aminoglucose is generally

8 ¦ present in the enzymatic material in an amount from about 0.0001 ~ i to about 0.00~ millimole per gram of enzymatic material and, lO ¦ preferably, in an amount from about 0.0003 to about 0.001 11 ¦ millimole per gram of enzymatic material.
12 ¦ In an alternative embodiment of this invention, the 13 I oxidoreductase enzyme can be incorporated into absorbent fibers l~ I of natural or synthetic materials for conversion into enzymatic ~5 ! bandages and pads.
lG ¦ The enzymes of this invention may be advantageously 17 ¦ encapsulated to enhance storage stability in the enzymatic 8 ¦ bandage or pad until utilization of the same. The encapsulating 19 I material can be composed of a water soluble polymer or a 20 ¦ polymer permeable to a substrate specific to the enzyme or 21 ' enzymes contained therein. An illustrative encapsulating 22 material is carboxymethylcellulose.
23 , The enzymatic absorbent materials can be prepared by 24 ¦ various procedures including: (a) solution deposition of the 25 ¦ oxidoreductase enzyme and optional ingredients onto the 26 I absorbent structure, (b) incorporation o~ the oxidoreductase 27 ~ enzyme into a spinning solution that is extruded as fiber 2~ filament ~hich can be converted into bandages and pads, and (c) o :

~ 2 1 incorporation of the oxidoreductase enzyme into the chemical 2 constituency which form poly~eric foams and subsequent 3 injection or solvent deposition of the aforementioned optional 4 ingredients as well as other special purpose additives.

6 RXAMPLE I.

8 This example illustrates the solution deposition of an oxidoreductase enzyme onto a spun cotton pad and the 0 bacteriostatic effect of the resulting enzymatic pad.
11 An aqueous enzymatic solution was prepared by adding 12 0.2 gm of polyvinylpyrolidone (Mol. Wt. 250,000) and l,000 IU
13 of glucose oxidase (approx. 4.0 mg) to a vessel containing 14 10 ml of distilled water with stirring through the use of a magnetic stirring bar and electric stirrer. Low turbulence lG was maintained during stirring to avoid any impairment of the 17 enzyme.
18 A spun cotton pad with dimensions of 3.0 cm by 3. n cm by 19 1.0 cm was impregnated with 1.0 ml of the aqueous enzyme solution ~0 by applying the solution to the pad through a standard medicinal 21 dropper. The residual water was allowed to evaporate from the 22 pad at room temperature (25C). The resulting pad and a 23 non~enzymatic control pad were tested for bacteriostatic 24 properties.
The enzymatic and non-enzymatic pads were placed in separate 26 culture tubes, and approximately 10 ml of human blood serum was 27 added to each of the culture tubes. The tubes were then 28 innoculated with Staphylococcus aureus at a concentration level ~s~
1 of 1.0 x 105 organisms per milliliter of serum and assayed for 2 bacterial coun~s at the end of each 4-hour segment for 24 hours.
3 Cultures to determine counts were prepared from tryptic soy 4 agar and incubated at 35C for 48 hours under aerobic conditions.
The results are set forth in the following table:

Glucose Oxidase

9 Enzymatic Pad Non-Enzy~atic Pad

10 Timej hr S. aureus Count/ml S. aureus Count/ml 0 1.2 x 105 1.4 x 105 4 8.6 x 104 2.9 x 105 12 8 6.6 x loA 8.5 x 105 12 5.9 x 104 4.4 x 106 3 16 5.1 x 1~4 9.1 x 106 4.0 x 104 3.6 x 107 1~ 24 3.2 x 104 7.0 x 107 16 EXAMPLE II.

18 This example illustrates the preparation of enzymatic 19 fibers by incorporating oxidoreductase enzyme and peroxidatic peroxidase enzyme into a wet spinning solution that is extruded 21 in fiber form. In addition, this example illustrates the 22 bacteriostatic effect of the resulting enzymatic fiber.
23 To methylene dichloride contained in a 250 ml beaker, 2~ there was added 10 gm of celluose triacetate in pellet form to ~5 bring the total volume of the contents to 100 ml. An aqueous 2G enzymatic solution having a volume of 15 ml was prepared by 27 admixing glucose oxidase (500 IU/ml) and lactoperoxidase 28 (500 IU/ml) with distilled water. The aqueous enzyme solution ~ 1 125~228 1 was added to and admixed with the cellulose triacetate solution 2 for 30 minutes which resulted in an emulsion of the aqueous 3 phase in the organic phase.
4 Fibers were formed from the enzymes/polymer emulsion by wet spinning technique. A 1~ ml hypodermic syringe was filled with the emulsion. The syringe was used to extrude the emulsion 7 through a No. 20 hypodermic needle into 100 ml of toluene that 8 was contained in a 150 ml graduated cylinder.
9 During the extrusion process, the emulsion coagulated as a ]0 fiber in the form of ringlets about 2 cm in diametex which

11 slowly ~ettl^d to the bottom of the gradllated cylinder. The

12 rate of extrusion was controlled to provide a continuous fiber

13 strand of thP ringlets at a rate slow enough to prevent sticking 1~ at the bottom of the cylinder. rJpon completion of the extrusion 16 step, the fibers were removed from the toluene bath and 16 air-dried before testing for bacteriostatic properties.
17 Approximately 9.6 gm of fiber were obtained.
18 The fiber was assayed for activity in respect of both 19 glucose oxidase and lactoperoxidase. An activity of 300 IU per gram of fiber was obtained for each enzyme.
21 A first control fiber w25 prepared by the foregoing 22 extrusion procedure, except that the extrusion composition did 23 not contain either glucose oxidase or lactoperoxidase. A second 24 control fiber was prepared in accordance with the procedure 25 used in the preparation of the first control fiber, except that 2G the extrusion composition was modified to contain bovine serum 27 albumin, a protein. Neither of the control fibers showed any 28 enzyme activity in tests for either glucose oxidase or . -l3-,. ; .

l 1~5~32Z8 1 lactoperoxidase. `
2 The fibers described above are of the type that are suitable 3 for the manufacture of woven bandages.
4 The fibers were tested for bacteriostatic properties using ~ Staphylococcus aureus (ATCC 653A) and E. coli (ATCC 25923).
6 Each organism was inoculated into a 20 ml portion of tryptic 7 soy broth and incubated at 35C for 24 hours. Each of the 8 resulting cultures was washed with a phosphate buffer (pH 6.5 9 and 0.01 M) by centrifuging to obtain a suspension of cells, which was diluted 1:10.
11 Fresh human blood serum samples were prepared in 6 screw 12 cap tubes that held 20 ml of serum in each. Twenty microliters 13 of the diluted bacterial cell suspension were inoculated into

14 each of the tubes containing serum. Thereafter, a 100 mg fiber sample was placed in each of the inoculated serum tubes which 16 were incubated at 35C for the duration of the testing.
17 Occasional manual agitation of the tubes was undertaken during 18 the test period.
l9 Bacterial counts of the samples were taken at the end of each 4-hour segment for 24 hours. Tryptic soy agar was used as 21 the plating medium for each sample and the plates were incubated 22 at 35UC for 48 hours under aerobic conditions. The results are 23 set forth in the following table:

, 3 Enzymatic Fiber Glucose Oxidase & Lactoperoxidase : 5 Time, hr.S. aureus Count E. coli Count/ml 6 0 2.0 x 105 1.0 x 105 4 6.2 x 103 3.8 x 104 7 8 2.0 x 103 2.2 x 104 12 1.8 x 103 7.6 x 103 8 16 <1,000 5.1 x 103 <300 1.4 x 103 9 24 <100 ~100 11 Non-Enzymatic Fiber 12 Time, hr. S. aureus CountE. coli Count/ml 3 0 2.0 x 105 1.0 x 105 4 6.6 x 105 9.5 x 105 14 8 2.1 x 106 5.1 x 107 12 8.8 x 106 4.9 x 108 16 2.2 x 107 1.0 x 109 3.7 x 107 1.1 x 109 16 24 5.0 x 107 1.6 x 109 Fiber/Bovine Serum Albumin 20 Time, hr. S. aureus CountE. coli Count/ml .~ o 2.0 x 105 1.0 x 105 : 21 4 4~5 x 105 9.5 x 105 : 8 9.9 x 105 5.3 x 106 22 12 6.1 x 106 8.9 x 106 ~; 16 8.4 x 106 1.2 x 107 23 20 1.0 x 107 8.6 x 107 .
24 24 4.2 x 107 2~1 x 109 26 EXAMPLE III.

28 This example illustrates a method for incorporating .

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1 oxidoreductase enzyme into yieldable, semi-rigid foam and the 2 bacteriostatic properties of the resulting enzymatio foam.
3 An aqueous enzyme solution was prepared by admixing 4 1,000 IU of glucose oxidase (approx. 4.0 mg) with 40 ml of cold, distilled water, under moderate agitation, until the 6 enzyme dissolved.
7 An isocyanate terminated, prepolymer solution was prepared 8 by reacting stoichiometric amounts of 80/20 2,4-/2,8 9 tolylenediisocyanate and Carbowax*l,000 polyoxyethylene polyol (Mol. Wt. 1,000) at 135C for 5 hours in the presence of a 11 catalyst comprising 2-ethylhexanoic acid and tin octoate. The 12 resulting urethane prepolymer was diluted to 90~ solids with 13 acetone.
14 To 24.5 gm of the acetone solution of prepolymer, there was added 0.22 gm of Tween*80 !a polyoxye~hylene derivative of 16 sorbitan fatty acid ester having a molecular weight of about 17 1,309) and the viscous mixture was stirred by hand for approximately 30 seconds. Twenty milliliters of the aqueous 19 enzyme solution was added to the prepolymer composition and the 20 ¦ resulting paste-like mixture was stirred to obtain a dispersion 21 of the ingredients. The remaining aqueous enz~me solution was 22 then added to the reaction mixture which was again stirred to 23 obtain dispersion of the ingredients. Upon completion of the 24 enzyme addition and dispersion steps, the reacting mass was poured into a Petri dish (100 mm diameter) and allowed to 26 remain at ambient temperature for 5 minutes at which time the 27 reaction was substantially complete.
2~ There was obtained from the reaction a white, spongy, wet, *Trademark .' ~, .

~s~z~:~
semi-rigid, enzymatic foam that was approximately 1.2 to 1.4 ~ centimeters thick. The wet foam was re~oved from the dish and 3 stored in a refrigerator at approximately 5C, with the foam 4 remaining damp during storage. One gram of this foam material (dry weight) was assayed for glucose oxidase activity using 6 glucose as a substrate, horseradish peroxidase and o-dianisidine as a chromogen. The activity of the one gram piece of foam was 8 approximately 12 IU per gram, or about 60% of the original activity.
Five grams of enzymatic foam (dry weight) were placed in a 11 large culture tube containing 10 ml of whole pig's blood. The 12 blood was inoculated with approximately 200,000 or~anisms of 13 S. aureus. A control tube was prepared by placing 5 grams of 14 ¦non-enzymatic foam in a culture tube containing 10 ml of whole

15 Ipig's blood which was inoculated with approximately 200,000

16 ¦organisms of S. aureus. Bacterial counts, per one ml of blood,

17 were taken at the end of each 4-hour segment for 24 hours. The

18 results are set forth in the following table:

19 Table III
21 Glucose Oxidase 22 Enzymatic Foam Non-Enzymatic Foam 23 Time, hr. S. aureus Count E. coli Count/ml 0 2.0 x 105 2.0 x 105 241 4 9.6 x 104 3.5 x 105 8 8.2 x 104 5.8 x ln5 25 12 5.0 x 1043 3.9 x 106 16 6.6 x 10 1.7 x 107 26 20 3.4 x 1033 6.8 x 107 27 24 2.2 x 10 9.5 x 1~7 28 By incorporating a spermicidal composition in the 1;~5~

1 enzymatic foam, a contraceptive flexi~le foam pad is obtained.

3 EXAMPLE IV.

This example illustrates an enzymatic pad which is 6 self-contained with respect to oxidoreductase enzyme and 7 corresponding oxidizable substrate for producing hydrogen 8 peroxide in the presence of serum.
9 An enzymatic solution was prepared by dissolving, with stirring, glucose oxidase (5,000 IU) and glucose (5.0 gm) in 11 methylene dichloride (50 ml). One millimeter of the enzymatic 12 solution was added to a spun cotton pad similar to that described 13 in Example I to effect solution deposition of the ingredients.
1~ .
EXAMPLE V.
lG
17 This example illustrates an enzymatic pad which is 18 self-contained with respect to oxidoreductase enzyme, oxidizable substrate, peroxidatic enzyme and oxidizable salt for producing an oxidized anionic bacterial inhibitor in the presence of 21 serum.
22 An enzymatic solution was prepared hy dissolving, with 23 stirring, glucose oxidase (l,000 IU), glucose (l0 gm), 2~ lactoperoxidase (500 I~), and potassium thiocyanate in methylene dichloride (5U ml). One milliliter of the enzymatic 26 solution was added to a spun cotton pad similar to that described 27 in Example I to effect solution deposition of the ingredients.
28 In view of the fore~oing description and examples, it will `'~ .

.
~' ~ S~ '8 1 become apparent to those of ordinary skill in the art that .
2 equivalent modifications thereof ~ay be made without departing 5 l ¦from the Eirit and scope of this invention.

8~

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Claims (20)

The embodiments of the invention in which an exclusive property or privilege is claimed are defined as follows:

1. An enzymatic absorbent material for body contact application containing, per gram of material, from about 1.0 to about 1,000 International Units of serum-activated oxidoreductase enzyme for producing hydrogen peroxide upon contact of said material with serum.

2. The enzymatic material of claim 1 wherein the concentration of oxidoreductase enzyme is from about 10 to about 500 International Units.

3. The enzymatic material of claim 1 wherein the oxidoreductase enzyme is glucose oxidase.

4. The enzymatic material of claim 1 wherein the oxidoreductase enzyme is oxalate oxidase.

5. The enzymatic material of claim 1 which also contains from about 0.1 to about 10,000 International Units of peroxidatic peroxidase per gram of material.

6. The enzymatic material of claim S wherein the concentration of peroxidatic peroxidase is from about 10 to about 500 International Units per gram of material.

7. The enzymatic material of claim 5 wherein the peroxidatic peroxidase is lactoperoxidase.

8. The enzymatic material of claim 5 wherein the peroxidatic peroxidase is myeloperoxidase.

9. The enzymatic material of claim 1 which also contains, per gram of material, from about 0.03 to about 1.2 millimoles of substrate specific to oxidoreductase enzyme in said material for producing hydrogen peroxide upon contact of said material with serum.

10. The enzymatic material of claim 9 wherein the concentration of substrate is from about 0.06 to 0.6 millimoles per gram of material.

11. The enzymatic material of claim 9 wherein the substrate is glucose and the oxidoreductase enzyme is glucose oxidase.

12. The enzymatic material of claim 11 which also contains from about 0.1 to about 10,000 International Units of lactoperoxidase per gram of material.

13. The enzymatic material of claim 5 which also contains, per gram of material, from about 0.0001 to about 0.01 millimole of a metal salt of an oxygen accepting anion selected from the group consisting of thiocyanate, chloride and iodide or mixtures of such salts.

14. The enzymatic material of claim 13 wherein the concentration of the alkali metal salt is from about 0.001 to about 0.006 per gram of material.

15, The enzymatic material of claim 13 wherein the alkali metal salt is potassium thiocyanate.

16. The enzymatic material of claim 1 which also contains an animoglucose selected from the group consisting of glucosamine, N-acetyl glucosamine and mixtures thereof in an amount from about 0.001 to about 0.002 millimole per gram of material.

17. The enzymatic material of claim 16 wherein the aminoglucose is present in an amount from about 0.0003 to about 0.001 millimole per gram of material.

18. The enzymatic material of claim 1 which also contains an effective amount of an enzymatic inhibitor specific to catalase.

19. The enzymatic material of claim 18 wherein the catalase inhibitor is an ascorbate salt in an amount from about 0.000001 to about 0.0001 millimole per gram of material.

20. An enzymatic absorbent fiber for conversion into enzymatic absorbent material for body contact application containing, per gram of fiber, from about 1.0 to about 1,000 International Units of serum-activated oxidoreductase enzyme for producing hydrogen peroxide upon contact with serum.