CURABLE COMPOSITION

Abstract

A composition comprising a) a curable resin or prepolymer component having ethylenically unsaturated polymerizable groups, b) an ethylenically unsaturated polymerizable monomer, c) an oxidoreductase and d) at least one of an organic peroxide and hydrogen peroxide, wherein the composition comprises between 0.0 and 20.0% by weight of water, calculated on the total weight of the composition.

Claims

1. A composition comprising a) a curable resin or prepolymer component having ethylenically unsaturated polymerizable groups, b) an ethylenically unsaturated polymerizable monomer, c) an oxidoreductase and d) at least one of an organic peroxide and hydrogen peroxide wherein the composition comprises between 0.0 and 20.0% by weight of water, calculated on the total weight of the composition.

2. The composition according to claim 1, wherein the oxidoreductase is a peroxidase (EC 1.11.1).

3. The composition according to claim 2, wherein the peroxidase (EC 1.11.1) is one of a peroxidase (EC 1.11.1.7), catalase (EC 1.11.1.6) or mixtures thereof.

4. The composition according to claim 1, wherein the oxidoreductase is from plant, fungal, mammalian, yeast or bacterial origin.

5. The composition according to claim 1, wherein the amount of the oxidoreductase is in the range of 0.01 to 40.00 mg/g, based on the weight of components a)+b).

6. The composition according to claim 1, wherein the composition further comprises a mediator.

7. The composition according to claim 6, wherein the mediator is at least one of 6-hydroxy-2-naphtoic acid or Acetylacetone (ACAC).

8. The composition according to claim 1, wherein the composition is liquid at a temperature of 23° C.

9. The composition according to claim 1, wherein the composition comprises between 0.0 and 40.0% of organic solvent.

10. The composition according to claim 1, wherein the composition further comprises dimethyl sulfoxide.

11. The composition according to claim 1, wherein the composition further comprises solid particles selected from fillers, pigments, fibers, and combinations thereof.

12. A kit of parts for preparing the composition according to claim 1, comprising I. a binder module comprising a) a curable resin or prepolymer component having ethylenically unsaturated polymerizable groups, b) an ethylenically unsaturated polymerizable monomer, and c) an oxidoreductase, and II. a hardener module comprising at least one of an organic peroxide and hydrogen peroxide, wherein each module comprises between 0.0 and 20.0% by weight of water, calculated on the weight of the module.

13. A kit of parts for preparing the composition according to claim 1, comprising I. a binder module comprising a) a curable resin or prepolymer component having ethylenically unsaturated polymerizable groups, b) an ethylenically unsaturated polymerizable monomer, II. a hardener module comprising at least one of an organic peroxide and hydrogen peroxide, and III. an activator module comprising an oxidoreductase, wherein the binder module and the hardener module comprise between 0.0 and 20.0% by weight of water, calculated on the weight of the module.

14. A process of forming a three-dimensional shaped part comprising the steps of i. providing a composition according to claim 1, ii. bringing the composition in a desired three-dimensional shape, and iii. curing the composition by radical polymerization.

15. The process according to claim 14, wherein step ii) is carried out by introducing said composition in a mold.

16. The process according to claim 14, wherein the process further includes the step of impregnating fibers with said composition.

17. The process according to claim 14, further comprising the step of preparing said composition.

Description

EXAMPLES

[0073] Description of Raw Materials Used

TABLE-US-00001 TABLE 1 Raw materials Trade designation Chemical description Supplier Palatal P4-01 UP resin based on orthophthalic acid AOC and standard glycols dissolved in Aliancys >25-<50% styrene Derakane Epoxy vinyl ester resin based on Ashland Momentum 411- bisphenol-A epoxy resin dissolved in 350 >40-<50% styrene Palatal A-410 UP resin based on isophthalic acid AOC and neopentylglycol dissolved in Aliancys >25-<50% styrene Palatal A 400-01 UP resin based on isophthalic acid AOC FC and standard glycols dissolved in Aliancys >25-<50% styrene Advalite VH-1223 Vinyl hybrid resin, styrene free Reichhold Advalite Vinyl Vinyl hybrid resin Reichhold hybrid 35060-00 Atlac Premium Vinyl ester resin dissolved in AOC 100 methacrylate, styrene free Aliancys Butanox M-50 Methyl ethyl ketone peroxide Akzo Nobel dissolved in dimethylphthalate Trigonox 44B Acetylacetone peroxide dissolved in Akzo Nobel solvent mixture Butanox LPT-IN Methyl ethyl ketone peroxide Akzo Nobel dissolved in diisononylphthalate Butanox M-50VR Methyl ethyl ketone peroxide Akzo Nobel dissolved in dimethylphthalate with dye Hydrogen peroxide, 30% Merck Dimethyl sulfoxide, Ph. Eur. VWR Water, ultrapure Rhodiasolve Pentanoic acid, 5-(dimethylamino)-2- Solvay PolarClean HSP methyl-5-oxo-methyl ester Tamisolve NxG 1-Butylpyrrolidin-2-one Eastman 2-Pyrrolidone n-Formylmorpholine n-Methyl-2-pyrrolidone Peroxidase various supplier Catalase various supplier Acetylacetone (ACAC) Sigma Aldrich 6-Hydroxy-2-naphtoic acid AlfaAesar NL-49P Cobalt(ll) 2-ethylhexanoate, 1% Co Akzo Nobel

[0074] Sample Preparation

[0075] 10 g resin (Palatal P4-01 if not mentioned otherwise) were placed in a 50 ml PE-plastic beaker. Mediators in solid form (like 6-Hydroxy-2-naphtoic acid) were dissolved in DMSO or water. Liquid mediators (like ACAC) were added directly to resin. The solid enzyme was placed in a 50 ml centrifugation tube or 5 ml reaction tube, depending on needed final amount, and was dissolved in mediator-DMSO-solution, water, or pure DMSO. Liquid enzyme was added directly to the resin. The enzyme solution was vortexed and shortly centrifuged at 4° C. and 6000 rcf. All components were added to the resin as follows: first the enzyme-(mediator)-solution and the peroxide at the end. In case of the mediator being liquid, the enzyme-solution was added first and the mediator was added afterwards, followed by addition of the peroxide. After each addition, the mixture was stirred with a spatula by hand. All w % are calculated on the weight of the resin (component a+b).

[0076] Shore Hardness Measurement

[0077] After addition of all components, plastic beakers were closed with a cap. Incubation was performed in a Thermomixer comfort (Eppendorf) for 2, 24, 48 hours at 24° C. with closed lid. Shore A hardness measurements of samples were made with digitest II Type DTAA (Bareiss) after 2, 24 and 48 hours according to DIN ISO 7619.

[0078] Determination of Gel-Time

[0079] After addition of all components, samples were directly filled in test tubes (Duran #261302106) up to the mark (4 cm), corresponding to about 5 g of sample. Measurement was started immediately and gel-time was measured up to 2 hours at 23° C. with Gelnorm-Geltimer (Gel Instrumente AG) with measurement pin (H.Saur #020.30).

[0080] Non-Inventive Control with Accelerator NL-49P and Addition of Water

[0081] The samples were prepared as described above (see sample preparation) using the amounts as described in table 2 followed by incubation in a Thermomixer comfort (Eppendorf) for 2, 24, 48 hours at 24° C. with closed lid.

TABLE-US-00002 TABLE 2 water: 0-10.0 wt % accelerator (NL-49P): 1 wt % peroxide (Butanox M-50): 2 wt %

TABLE-US-00003 TABLE 3 Results water started to [wt %] cure [h] 0 <0.15 4.3 15 6.0 15 8.0 24 10.0 24

[0082] Started to cure was determined by poking the reaction mixture with a spatula. When poking with a spatula left an indentation in the reaction mixture, and no flow-back of the reaction mixture to the indentation was observed, gelation was considered to have occurred.

[0083] The table shows that an increased addition of water resulted in an increased reaction time of curing with the Cobalt accelerator.

[0084] Variation of Enzyme Concentration

[0085] The samples were prepared as described above (see sample preparation) using the amounts as described in table 4 followed by incubation in a Thermomixer comfort (Eppendorf) for 2, 24, 48 hours at 24° C. with closed lid. The enzyme (peroxidase, Sigma Aldrich, #P8250) was dissolved in 4.3 wt % water.

TABLE-US-00004 TABLE 4 enzyme peroxidase, solid: 0-17 mg/g resin water: 4.3 wt % mediator (ACAC): 0.12 mmol/g resin peroxide (Butanox M50):   2 wt %

TABLE-US-00005 TABLE 5 Results enzyme started to cure [h] [mg solid/g with without resin] mediator mediator 0.0 x x 0.4 x 167 2.0 65 65 3.0 49 49 4.0 42 42 7.0 24 49 9.0 18 17 13.0 15 15 17.0 7 15 x: “no curing”

[0086] The curing was observed visually and determined as described above.

[0087] The results show that with an increasing amount of enzyme the reaction time decreased. By addition of the mediator, the reaction time decreased further.

[0088] Variation of Water Concentration

[0089] The samples were prepared as described above (see sample preparation) using the amounts as described in table 6 followed by incubation in a Thermomixer comfort (Eppendorf) for 2, 24, 48 hours at 24° C. with closed lid. The enzyme (peroxidase, Sigma Aldrich, #P8250) was dissolved in various water concentrations.

TABLE-US-00006 TABLE 6 enzyme peroxidase, solid: 17 mg/g resin water: 4-10 wt % mediator (ACAC): 1.2 mmol/g resin peroxide (Butanox M-50): 2 wt %

TABLE-US-00007 TABLE 7 Results started to cure [min] water [wt %] with mediator without mediator 4 1440 1440 6 60 180 8 60 60 10 60 60

[0090] Curing was observed visually and determined as described above.

[0091] With increasing water content, the reaction time decreased. With addition of mediator, the reaction time decreased even further.

[0092] Variation of Peroxide Concentration

[0093] The samples were prepared as described above (see sample preparation) using the amounts as described in table 8 followed by incubation in a Thermomixer comfort (Eppendorf) for 2, 24, 48 hours at 24° C. with closed lid. The enzyme (peroxidase, Sigma Aldrich, #P8250) was dissolved in 10 wt % water.

TABLE-US-00008 TABLE 8 enzyme peroxidase, solid: 17 mg/g resin water: 10 wt % mediator (ACAC): 1.2 mmol/g resin peroxide (Butanox M-50): 0.2-6.0 wt %

TABLE-US-00009 TABLE 9 Results started to cure [min] peroxide [wt %] with mediator without mediator 0.2 60 120 1.0 36 36 2.0 36 500 4.0 300 1440 6.0 180 480

[0094] Curing was observed visually and determined as described above.

[0095] In general, lower peroxide concentrations showed shorter reaction times. The best result was achieved between 0.2 and 1.0 wt % peroxide.

[0096] Variation of Mediator Concentration

[0097] The samples were prepared as described above (see sample preparation) using the amounts as described in table 10 followed by incubation in a Thermomixer comfort (Eppendorf) for 2, 24, 48 hours at 24° C. with closed lid. The enzyme (peroxidase, Sigma Aldrich, #P8250) was dissolved in 10 wt % water.

TABLE-US-00010 TABLE 10 enzyme peroxidase, solid: 17 mg/g resin water: 10 wt % mediator (ACAC): 0.00-0.24 mmol/g resin peroxide (Butanox M-50):  1 wt %

TABLE-US-00011 TABLE 11 Results mediator [mmol/g started to visual evaluation resin] cure [min] after 2 h after 24 h after 48 h 0.00 0-36 3.0 2.0 1.7 0.01 0-36 3.3 1.7 1.3 0.06 0-36 2.3 1.3 1.3 0.12 0-36 2.7 1.7 1.3 0.24 0-36 3.0 2.0 1.7 1 = very good; 2 = good; 3 = satisfactory

[0098] Curing was observed visually and determined as described above.

[0099] Moreover, the hardness, thickness and homogeneity of the resin were assessed. The parameters were evaluated visually and additionally by poking the resin with a spatula. Subsequently, the criteria summarized in the table above were applied. 3 denotes for medium thick sample, which is soft to solid with residual liquid; 2 denotes for a thick sample, solid and with a lower content of residual liquid and 1 denotes for a thick sample, which is very solid with almost no residual liquid.

[0100] The best results were achieved between 0.01 and 0.06 mmol ACAC/g resin.

[0101] Increase of Water Concentration

[0102] The samples were prepared as described above (see sample preparation) using the amounts as described in table 12. The enzyme (peroxidase, Sigma Aldrich, #P8250) was dissolved in water concentrations between 10 and 20 w %.

TABLE-US-00012 TABLE 12 enzyme peroxidase, solid: 17 mg/g resin water: 10-20 wt % mediator (ACAC): 0.05 mmol/g resin peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00013 TABLE 13 Results Shore A after Shore A after water [wt %] gel-time [min] 24 h 48 h 10 22 71 80 15 0 66 76 20 50 47 78

[0103] The best result was reached with 10 wt % water content. With higher water concentrations, the gel-time increased and but the Shore A hardness of the final sample decreased.

[0104] Peroxidases from Various Suppliers

[0105] The samples were prepared as described above (see sample preparation) using the amounts as described in table 14. The enzymes were dissolved in 10 wt % water.

TABLE-US-00014 TABLE 14 enzyme peroxidase, solid: 17 mg/g resin water:  10 wt % mediator (ACAC): 0.5 mmol/g resin peroxide (Butanox M-50): 0.5 wt %

[0106] The activity of the enzyme was determined by using ABTS as substrate. 1 U stands for one unit which oxidizes 1.0 μmole of 2,2″-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) per minute at pH 5.0 at 25° C., measured at A=405 nm (Spark, Tecan).

TABLE-US-00015 TABLE 15 Results enzyme activity gel- Shore A Shore A article [U/mg time after after supplier number protein] [min] 24 h 48 h abcr AB348238 313 41 44 77 Alfa Aesar J60026 109 58 41 76 Amano Amano PO-3 652 11 83 85 Amresco 417 n/a 20 73 76 BBI 161451BBI 497 25 79 85 Solutions 161453BBI 443 81 48 77 161455BBI 412 133 52 87 161457BBI 256 32 44 66 Biosynth P-2000 236 92 33 71 Calzyme 100A0400 577 29 89 81 100A0600 519 16 81 89 Chemical CP9003-99-0- 291 15 42 76 Point BULK Creative PHAM-231 177 24 69 83 Enzymes Faizyme 16001 356 16 73 82 16002 348 19 68 77 16004 196 n/a 20 56 16005 169 n/a 20 58 Iris LS-1217 266 37 43 76 Biotech Proactive P113-0165 260 16 59 69 Molecular Research Sigma P8125 175 51 40 70 Aldrich P8250 325 18 80 91 P8375 427 14 77 84 TCI P0073 318 17 73 80 Chemicals

[0107] From the table it is visible, that all peroxidases showed a curing effect, irrespective of their origin from different commercial suppliers.

[0108] DMSO as Solvent

[0109] The samples were prepared as described above (see sample preparation) using the amounts as described in table 16. The enzyme (peroxidase, Sigma Aldrich, #P8250) was dissolved in various concentrations of water-DMSO mixtures. No mediator was used in this experiment.

TABLE-US-00016 TABLE 16 enzyme peroxidase, solid: 17 mg/g resin peroxide (Butanox M-50): 0.2 wt %

TABLE-US-00017 TABLE 17 Results water DMSO gel-time Shore A Shore A [wt %] [wt %] [min] after 24 h after 48 h 0 10 49 79 82 9 1 86 78 84 5 5 58 79 83 Without enzyme, no curing was detectable.

[0110] From the table it is visible that curing of the resin with peroxidase was also possible without any water and mediator in the system.

[0111] Curing with Various Resins and Peroxides

[0112] Experiments with Cobalt accelerator NL-49P (without enzyme) were performed as non-inventive control. The samples were prepared as described above (see sample preparation) using the amounts as described in table 18.

TABLE-US-00018 TABLE 18 NL- peroxide 49P gel-time Shore A Shore A resin peroxide [wt %] [wt %] [min] after 24 h after 48 h Palatal P 4-01 Butanox M- 2 1.0 7 88 96 50 Palatal P 4-01 Trigonox 1 0.5 16 90 93 44B Palatal A-410 Trigonox 1 0.5 10 90 94 44B Palatal A 400- Butanox M- 1 1.0 7 91 95 01 FC 50 Atlac Premium Butanox 2 2.0 13 85 91 100 LPT-IN

[0113] Experiments with Different Resins

[0114] The enzyme (peroxidase, BBI Solutions, #161451BBI) was dissolved in 10 wt % water.

TABLE-US-00019 TABLE 19 enzyme peroxidase, solid: 17 mg/g resin mediator (ACAC): 0.05 mmol/g resin Peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00020 TABLE 20 Results gel-time Shore A Shore A resin [min] after 24 h after 48 h Palatal P 4-01 19 70 82 Palatal A-410 10 75 89 Palatal A 400-01 FC  7 87 89 Derakane Momentum 411-350 18 85 94 Advalite VH-1223 39 29 33 Advalite ™ Vinyl hybrid 35060-00 n/a 24 37 Atlac Premium 100 n/a 65 77

[0115] With peroxidase, different resin systems based on unsaturated polyester, vinylester, or with acrylates or styrene as monomer could be cured.

[0116] For testing of different peroxides, Palatal P 4-01 as resin was used.

TABLE-US-00021 TABLE 21 Results Shore A gel-time Shore A after resin peroxide [min] after 24 h 48 h Palatal P 4-01 Butanox LPT- 31 88 87 IN Palatal P 4-01 Butanox M- 25 64 79 50VR Palatal P 4-01 Butanox M-50 19 70 82

[0117] With peroxidase, different peroxides could be used for curing of the resin system.

[0118] Variation of DMSO Concentration

[0119] The samples were prepared as described above (see sample preparation) using the amounts as described in table 22. The enzyme (peroxidase, Faizyme, #16001) was dissolved in various DMSO concentrations. 6-hydroxy-2-naphtoic acid was used as mediator.

TABLE-US-00022 TABLE 22 enzyme peroxidase, solid: 17 mg/g resin DMSO: 2.5-20 wt % mediator (6-hydroxy-2-naphtoic acid): 0.05 mmol/g resin peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00023 TABLE 23 Results DMSO gel-time Shore A Shore A Shore A [wt %] [min] after 2 h after 24 h after 48 h 2.5 36 20 83 87 5.0 4 85 97 98 7.5 5 90 97 97 10.0 5 89 97 97 15.0 4 73 94 95 20.0 6 66 90 90

[0120] The best result was reached with 7.5 wt % DMSO.

[0121] Variation of Enzyme Concentration with DMSO as Solvent

[0122] The samples were prepared as described above (see sample preparation) using the amounts as described in table 24. The enzyme (peroxidase, Faizyme, #16001) was dissolved in 7.5 wt % DMSO.

TABLE-US-00024 TABLE 24 enzyme peroxidase, solid: 0-10 mg/g resin DMSO: 7.5 wt % mediator (6-hydroxy-2-naphtoic 0.05 mmol/g acid): resin peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00025 TABLE 25 Results enzyme, solid gel-time Shore A Shore A Shore A [mg/g resin] [min] after 2 h after 24 h after 48 h 0.0 n/a x x x 2.5 271 x 71 87 5.0 30 59 91 92 7.5 16 67 94 95 10.0 10 77 97 96 x: no curing was detectable

[0123] The samples were prepared as described above (see sample preparation) using the amounts as described in table 26. Enzyme (peroxidase, Faizyme, #16001) was dissolved in 7.5 wt % DMSO.

TABLE-US-00026 TABLE 26 enzyme peroxidase, solid: 0-10 mg/g resin DMSO: 7.5 wt % mediator (6-hydroxy-2-naphtoic 0.1 mmol/g resin acid): peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00027 TABLE 27 Results enzyme, Shore A Shore A solid geltime after after [mg/g resin] [min] Shore A after 2 h 24 h 48 h 0.00 x x x x 0.25 1387 x x 0* 0.50 214 0 84 87 1.00 49 21 80 83 2.50 11 75 95 94 5.00 5 92 96 96 7.50 4 92 97 96 10.00 3 92 96 96 0*: Curing of sample was visible, but sample was too soft for measurement of Shore A hardness.

[0124] Also with DMSO, an increasing enzyme concentration lead to a decrease in gel-time and an increase in hardness.

[0125] Curing with H.sub.2O.sub.2 as Peroxide

[0126] The samples were prepared as described above (see sample preparation) using the amounts as described in table 28. The mediator 6-hydroxy-2-naphtoic acid and the enzyme (peroxidase, Faizyme, #16001) were dissolved in 10 wt % DMSO.

TABLE-US-00028 TABLE 28 enzyme peroxidase, solid: 10 mg/g resin water/DMSO: 10 wt % mediator (6-hydroxy-2- 0.05 mmol/g naphtoesäure/ACAC): resin peroxide (H.sub.2O.sub.2, 30%): 0.1-0.3 wt %

TABLE-US-00029 TABLE 29 Results H.sub.2O.sub.2 (30%) gel-time Shore A Shore A Shore A [wt %] [min] after 2 h after 24 h after 48 h 0.1 n/a x 52 88 0.3 n/a x  0* 68 0*: Curing of sample was visible, but sample was too soft for measurement of Shore A hardness. x: no curing was detectable

[0127] In the following, the enzyme was dissolved in 10 wt % water and ACAC was used as mediator.

TABLE-US-00030 TABLE 30 H.sub.2O.sub.2 (30%) gel-time Shore A Shore A Shore A after [wt %] [min] after 2 h after 24 h 48 h 0.6 n/a x 33 79

[0128] With both solvents (DMSO or water), curing of the resin with peroxidase and H.sub.2O.sub.2 was possible.

[0129] Curing of Thin Layers

[0130] The samples were prepared as described above (see sample preparation) using the amounts as described in table 30. The enzyme (peroxidase, Faizyme, #16001) was dissolved in 7.5 wt % DMSO.

TABLE-US-00031 TABLE 31 enzyme peroxidase, solid: 17 mg/g resin mediator (6-hydroxy-2-naphtoic acid): 0.05 mmol/g resin peroxide (Butanox M-50) 0.5 wt %

[0131] The mixture was transferred to a glass plate and spread with a doctor blade (300 μm). The curing was tested via scratching the resin with a spatula. Additionally, a non-inventive comparison example with cobalt instead of the enzyme and mediator was tested.

[0132] Comparable curing with peroxidase or cobalt was observed. As a result, also thin film curing was possible with peroxidase.

[0133] Curing with Catalases

[0134] To test if the enzyme catalase can also be suitably used in the curing resin systems, the following experiment was carried out with catalase instead of peroxidase. The enzyme was dissolved in 10 wt % water.

TABLE-US-00032 TABLE 32 enzyme catalase, solid: 17 mg/g resin water:  10 wt % mediator (ACAC): 0.5 mmol/g resin peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00033 TABLE 33 Results article gel-time Shore A Shore A origin supplier number [min] after 24 h after 48 h Bovine liver Sigma C40 >120 0* 0* 0*: Curing of sample was visible, but sample was too soft for measurement of Shore A hardness.

[0135] Enzyme was dissolved in 10 wt % in a mixture of DMSO and water (50:50).

TABLE-US-00034 TABLE 34 enzyme catalase, solid: 17 mg/g resin Dmso/water (50:50):  10 wt % peroxide (Butanox M-50): 0.5 wt %

TABLE-US-00035 TABLE 35 Results geltime Shore A Shore A Shore A origin supplier order no [min] after 2 h after 24 h after 48 h bovine liver Sigma C40 n/a x x  0* bovine liver Sigma E3289 n/a 0* 16 37 Aldrich 0*: Curing of sample was visible, but sample was too soft for measurement of Shore A hardness.

[0136] The tables show that the employment of catalase also leads to the curing of the resin.