GB2482164A - Cleaning composition - Google Patents
Cleaning composition Download PDFInfo
- Publication number
- GB2482164A GB2482164A GB1012302.4A GB201012302A GB2482164A GB 2482164 A GB2482164 A GB 2482164A GB 201012302 A GB201012302 A GB 201012302A GB 2482164 A GB2482164 A GB 2482164A
- Authority
- GB
- United Kingdom
- Prior art keywords
- parts
- composition
- water
- composition according
- enzyme
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 97
- 238000004140 cleaning Methods 0.000 title claims abstract description 29
- 102000004190 Enzymes Human genes 0.000 claims abstract description 27
- 108090000790 Enzymes Proteins 0.000 claims abstract description 27
- 229920005862 polyol Polymers 0.000 claims abstract description 19
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 19
- 150000001412 amines Chemical class 0.000 claims abstract description 18
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 claims abstract description 15
- 229910052796 boron Inorganic materials 0.000 claims abstract description 15
- 150000001875 compounds Chemical class 0.000 claims abstract description 15
- 150000003077 polyols Chemical class 0.000 claims abstract description 14
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims abstract description 13
- 108091005804 Peptidases Proteins 0.000 claims abstract description 12
- 239000004365 Protease Substances 0.000 claims abstract description 12
- -1 alkylene glycol polyols Chemical class 0.000 claims abstract description 11
- 159000000007 calcium salts Chemical class 0.000 claims abstract description 10
- 108010065511 Amylases Proteins 0.000 claims abstract description 9
- 102000013142 Amylases Human genes 0.000 claims abstract description 9
- 235000019418 amylase Nutrition 0.000 claims abstract description 9
- LYCAIKOWRPUZTN-UHFFFAOYSA-N ethylene glycol Natural products OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 claims abstract description 8
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 7
- 239000004382 Amylase Substances 0.000 claims abstract description 6
- 235000011187 glycerol Nutrition 0.000 claims abstract description 6
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 claims abstract description 5
- 239000004094 surface-active agent Substances 0.000 claims abstract description 5
- 210000004369 blood Anatomy 0.000 claims description 26
- 239000008280 blood Substances 0.000 claims description 26
- 239000012620 biological material Substances 0.000 claims description 14
- 238000000034 method Methods 0.000 claims description 12
- 108090000623 proteins and genes Proteins 0.000 claims description 11
- 230000007797 corrosion Effects 0.000 claims description 9
- 238000005260 corrosion Methods 0.000 claims description 9
- 102000004169 proteins and genes Human genes 0.000 claims description 9
- 239000003112 inhibitor Substances 0.000 claims description 7
- 238000001035 drying Methods 0.000 claims description 4
- 230000001954 sterilising effect Effects 0.000 claims description 3
- 238000013019 agitation Methods 0.000 claims description 2
- 210000003567 ascitic fluid Anatomy 0.000 claims description 2
- 210000000988 bone and bone Anatomy 0.000 claims description 2
- 210000001175 cerebrospinal fluid Anatomy 0.000 claims description 2
- 210000002939 cerumen Anatomy 0.000 claims description 2
- 210000003060 endolymph Anatomy 0.000 claims description 2
- 210000000416 exudates and transudate Anatomy 0.000 claims description 2
- 210000003608 fece Anatomy 0.000 claims description 2
- 239000012530 fluid Substances 0.000 claims description 2
- 210000004051 gastric juice Anatomy 0.000 claims description 2
- 239000002736 nonionic surfactant Substances 0.000 claims description 2
- 210000004049 perilymph Anatomy 0.000 claims description 2
- 210000004910 pleural fluid Anatomy 0.000 claims description 2
- 210000003296 saliva Anatomy 0.000 claims description 2
- 210000002374 sebum Anatomy 0.000 claims description 2
- 210000000582 semen Anatomy 0.000 claims description 2
- 210000004243 sweat Anatomy 0.000 claims description 2
- 238000002604 ultrasonography Methods 0.000 claims description 2
- 210000002700 urine Anatomy 0.000 claims description 2
- 238000009423 ventilation Methods 0.000 claims description 2
- 210000004916 vomit Anatomy 0.000 claims description 2
- 230000008673 vomiting Effects 0.000 claims description 2
- 229940088598 enzyme Drugs 0.000 description 22
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 13
- 239000003153 chemical reaction reagent Substances 0.000 description 10
- 238000010521 absorption reaction Methods 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 235000018102 proteins Nutrition 0.000 description 8
- 238000005406 washing Methods 0.000 description 8
- 239000002518 antifoaming agent Substances 0.000 description 7
- 229920001577 copolymer Polymers 0.000 description 7
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 6
- 102000035195 Peptidases Human genes 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 4
- 229940025131 amylases Drugs 0.000 description 4
- QRUDEWIWKLJBPS-UHFFFAOYSA-N benzotriazole Chemical compound C1=CC=C2N[N][N]C2=C1 QRUDEWIWKLJBPS-UHFFFAOYSA-N 0.000 description 4
- 239000012964 benzotriazole Substances 0.000 description 4
- 230000000052 comparative effect Effects 0.000 description 4
- 239000012141 concentrate Substances 0.000 description 4
- 238000005187 foaming Methods 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 4
- 239000004615 ingredient Substances 0.000 description 4
- 229920001296 polysiloxane Polymers 0.000 description 4
- 241000194108 Bacillus licheniformis Species 0.000 description 3
- 229910001369 Brass Inorganic materials 0.000 description 3
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 3
- 229920001400 block copolymer Polymers 0.000 description 3
- 239000010951 brass Substances 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 235000014113 dietary fatty acids Nutrition 0.000 description 3
- 229930195729 fatty acid Natural products 0.000 description 3
- 239000000194 fatty acid Substances 0.000 description 3
- 150000004665 fatty acids Chemical class 0.000 description 3
- 150000002222 fluorine compounds Chemical class 0.000 description 3
- 239000006260 foam Substances 0.000 description 3
- 229920005604 random copolymer Polymers 0.000 description 3
- 150000003839 salts Chemical group 0.000 description 3
- VXWBQOJISHAKKM-UHFFFAOYSA-N (4-formylphenyl)boronic acid Chemical compound OB(O)C1=CC=C(C=O)C=C1 VXWBQOJISHAKKM-UHFFFAOYSA-N 0.000 description 2
- CMGDVUCDZOBDNL-UHFFFAOYSA-N 4-methyl-2h-benzotriazole Chemical compound CC1=CC=CC2=NNN=C12 CMGDVUCDZOBDNL-UHFFFAOYSA-N 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 108091005658 Basic proteases Proteins 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- 102000005575 Cellulases Human genes 0.000 description 2
- 108010084185 Cellulases Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- 239000004367 Lipase Substances 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 150000001299 aldehydes Chemical class 0.000 description 2
- 125000000217 alkyl group Chemical group 0.000 description 2
- 108090000637 alpha-Amylases Proteins 0.000 description 2
- 102000004139 alpha-Amylases Human genes 0.000 description 2
- 229940024171 alpha-amylase Drugs 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 229910021538 borax Inorganic materials 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- ZCCIPPOKBCJFDN-UHFFFAOYSA-N calcium nitrate Chemical compound [Ca+2].[O-][N+]([O-])=O.[O-][N+]([O-])=O ZCCIPPOKBCJFDN-UHFFFAOYSA-N 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- UQGFMSUEHSUPRD-UHFFFAOYSA-N disodium;3,7-dioxido-2,4,6,8,9-pentaoxa-1,3,5,7-tetraborabicyclo[3.3.1]nonane Chemical compound [Na+].[Na+].O1B([O-])OB2OB([O-])OB1O2 UQGFMSUEHSUPRD-UHFFFAOYSA-N 0.000 description 2
- 239000012154 double-distilled water Substances 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 150000002334 glycols Chemical class 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- ZXEKIIBDNHEJCQ-UHFFFAOYSA-N isobutanol Chemical compound CC(C)CO ZXEKIIBDNHEJCQ-UHFFFAOYSA-N 0.000 description 2
- 235000019421 lipase Nutrition 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- YPFDHNVEDLHUCE-UHFFFAOYSA-N propane-1,3-diol Chemical compound OCCCO YPFDHNVEDLHUCE-UHFFFAOYSA-N 0.000 description 2
- 235000010339 sodium tetraborate Nutrition 0.000 description 2
- 239000004328 sodium tetraborate Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000003760 tallow Substances 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- JNYAEWCLZODPBN-JGWLITMVSA-N (2r,3r,4s)-2-[(1r)-1,2-dihydroxyethyl]oxolane-3,4-diol Chemical class OC[C@@H](O)[C@H]1OC[C@H](O)[C@H]1O JNYAEWCLZODPBN-JGWLITMVSA-N 0.000 description 1
- 125000001494 2-propynyl group Chemical group [H]C#CC([H])([H])* 0.000 description 1
- KFJDQPJLANOOOB-UHFFFAOYSA-N 2h-benzotriazole-4-carboxylic acid Chemical compound OC(=O)C1=CC=CC2=NNN=C12 KFJDQPJLANOOOB-UHFFFAOYSA-N 0.000 description 1
- 108091005508 Acid proteases Proteins 0.000 description 1
- 241001134780 Bacillus acidopullulyticus Species 0.000 description 1
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
- 241000193422 Bacillus lentus Species 0.000 description 1
- 241000194107 Bacillus megaterium Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 101710130006 Beta-glucanase Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- YASYEJJMZJALEJ-UHFFFAOYSA-N Citric acid monohydrate Chemical compound O.OC(=O)CC(O)(C(O)=O)CC(O)=O YASYEJJMZJALEJ-UHFFFAOYSA-N 0.000 description 1
- 206010011409 Cross infection Diseases 0.000 description 1
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 240000005979 Hordeum vulgare Species 0.000 description 1
- 235000007340 Hordeum vulgare Nutrition 0.000 description 1
- 229920001202 Inulin Polymers 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- GXCLVBGFBYZDAG-UHFFFAOYSA-N N-[2-(1H-indol-3-yl)ethyl]-N-methylprop-2-en-1-amine Chemical compound CN(CCC1=CNC2=C1C=CC=C2)CC=C GXCLVBGFBYZDAG-UHFFFAOYSA-N 0.000 description 1
- 206010029803 Nosocomial infection Diseases 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- ATTZFSUZZUNHBP-UHFFFAOYSA-N Piperonyl sulfoxide Chemical compound CCCCCCCCS(=O)C(C)CC1=CC=C2OCOC2=C1 ATTZFSUZZUNHBP-UHFFFAOYSA-N 0.000 description 1
- 108010059820 Polygalacturonase Proteins 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- GOOHAUXETOMSMM-UHFFFAOYSA-N Propylene oxide Chemical compound CC1CO1 GOOHAUXETOMSMM-UHFFFAOYSA-N 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- SLINHMUFWFWBMU-UHFFFAOYSA-N Triisopropanolamine Chemical compound CC(O)CN(CC(C)O)CC(C)O SLINHMUFWFWBMU-UHFFFAOYSA-N 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 150000001408 amides Chemical group 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 229940024606 amino acid Drugs 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 235000010338 boric acid Nutrition 0.000 description 1
- 125000005619 boric acid group Chemical class 0.000 description 1
- 150000001642 boronic acid derivatives Chemical class 0.000 description 1
- 125000005620 boronic acid group Chemical class 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 229910001622 calcium bromide Inorganic materials 0.000 description 1
- WGEFECGEFUFIQW-UHFFFAOYSA-L calcium dibromide Chemical compound [Ca+2].[Br-].[Br-] WGEFECGEFUFIQW-UHFFFAOYSA-L 0.000 description 1
- 108010089934 carbohydrase Proteins 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 229960004106 citric acid Drugs 0.000 description 1
- 229960002303 citric acid monohydrate Drugs 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 239000013530 defoamer Substances 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- XWBDWHCCBGMXKG-UHFFFAOYSA-N ethanamine;hydron;chloride Chemical compound Cl.CCN XWBDWHCCBGMXKG-UHFFFAOYSA-N 0.000 description 1
- UYMKPFRHYYNDTL-UHFFFAOYSA-N ethenamine Chemical compound NC=C UYMKPFRHYYNDTL-UHFFFAOYSA-N 0.000 description 1
- 108010093305 exopolygalacturonase Proteins 0.000 description 1
- 150000002191 fatty alcohols Chemical class 0.000 description 1
- 229930182478 glucoside Natural products 0.000 description 1
- 150000008131 glucosides Chemical class 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000005456 glyceride group Chemical class 0.000 description 1
- 150000002314 glycerols Chemical class 0.000 description 1
- 239000008233 hard water Substances 0.000 description 1
- 229940059442 hemicellulase Drugs 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 239000008240 homogeneous mixture Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-M hydroxide Chemical compound [OH-] XLYOFNOQVPJJNP-UHFFFAOYSA-M 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 229940029339 inulin Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 150000004682 monohydrates Chemical class 0.000 description 1
- ZBJVLWIYKOAYQH-UHFFFAOYSA-N naphthalen-2-yl 2-hydroxybenzoate Chemical compound OC1=CC=CC=C1C(=O)OC1=CC=C(C=CC=C2)C2=C1 ZBJVLWIYKOAYQH-UHFFFAOYSA-N 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 239000006174 pH buffer Substances 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- HXITXNWTGFUOAU-UHFFFAOYSA-N phenylboronic acid Chemical class OB(O)C1=CC=CC=C1 HXITXNWTGFUOAU-UHFFFAOYSA-N 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000223 polyglycerol Chemical class 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000008213 purified water Substances 0.000 description 1
- 150000003856 quaternary ammonium compounds Chemical class 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 239000002455 scale inhibitor Substances 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- DAJSVUQLFFJUSX-UHFFFAOYSA-M sodium;dodecane-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCS([O-])(=O)=O DAJSVUQLFFJUSX-UHFFFAOYSA-M 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 150000003445 sucroses Chemical class 0.000 description 1
- 108010075550 termamyl Proteins 0.000 description 1
- MDDUHVRJJAFRAU-YZNNVMRBSA-N tert-butyl-[(1r,3s,5z)-3-[tert-butyl(dimethyl)silyl]oxy-5-(2-diphenylphosphorylethylidene)-4-methylidenecyclohexyl]oxy-dimethylsilane Chemical compound C1[C@@H](O[Si](C)(C)C(C)(C)C)C[C@H](O[Si](C)(C)C(C)(C)C)C(=C)\C1=C/CP(=O)(C=1C=CC=CC=1)C1=CC=CC=C1 MDDUHVRJJAFRAU-YZNNVMRBSA-N 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38618—Protease or amylase in liquid compositions only
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38663—Stabilised liquid enzyme compositions
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L2202/00—Aspects relating to methods or apparatus for disinfecting or sterilising materials or objects
- A61L2202/20—Targets to be treated
- A61L2202/24—Medical instruments, e.g. endoscopes, catheters, sharps
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
- C11D2111/10—Objects to be cleaned
- C11D2111/14—Hard surfaces
- C11D2111/20—Industrial or commercial equipment, e.g. reactors, tubes or engines
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Abstract
An aqueous composition comprises: 0.01-15 parts bywt of enzyme, preferably protease and amylase; 0.01-10 parts by wt boron-containing compound; 0.01-10 parts by wt water-soluble calcium salt; 1-30 parts by wt polyol, preferably alkylene glycol polyols or glycerine; 1-15 parts by wt amine, preferably an alk anolamine; 2-30 parts by wt surfactant; water and has a pH of 8.1-8.3. The composition may be use for cleaning medical apparatus by placing it in a container and contacting with the composition.
Description
COMPOSITIONS SUITABLE FOR CLEANING MEDICAL DEVICES
This invention relates to compositions which are suitable for cleaning medical devices and to the use of such compositions.
Medical devices are often heavily contaminated with biological materials as a result of their use. Before re-use it is essential that the devices are properly cleaned and disinfected.
The nature and extent of contamination in the medical arena is far greater than that normally found in a domestic environment and the need for efficient cleaning is much greater. There is a risk of cross-infection to other patients whose immune systems may already compromised by illness, injury or the trauma of invasive medical procedures.
Typically the procedure for cleaning and disinfection of medical devices comprises washing to remove biological materials, rinsing, disinfection and drying.
GB 2,360,041 describes an aqueous composition having a pH of from about 7.0 to 8.0 suitable for cleaning medical devices. However it is desirable to improve the cleaning efficacy of the compositions described therein.
According to a first aspect of the present invention there is provided an aqueous composition comprising the following components: (i) 0.01 to 15 parts of enzyme; (ii) 0.01 to 10 parts of boron-containing compound; (iii) 0.01 to 10 parts of water-soluble calcium salt; (iv) 1 to 30 parts of polyol; (v) ito 15 parts of amine; (vi) 2 to 30 parts of surtactant; and (vii) water; wherein all parts are by weight and the composition has a pH of 8.1 to 8.9.
The number of parts of enzyme are calculated on a 100% solids basis.
For example, 6 parts of a 15% strength solution of enzyme would constitute 0.9 parts of enzyme The enzyme may be a single enzyme or a mixture comprising two or more enzymes.
The function of the enzyme is to break-down the biological material commonly encountered by the medical device. Typical biological materials include fat, blood, cerebrospinal fluid, cerumen, gastric juices, peritoneal fluid, pleural fluid, sebum, semen, sweat, vomit, saliva, tissue, bone, endolymph, perilymph, proteins, bodily exudates, discharges, urine and/or fecal matter.
The enzyme used in the composition depends to some extent on which biological materials the particular medical device will come into contact with.
Enzymes include, for example, amylases, lipases, cellulases and especially proteases.
Amylases are particularly useful for breaking down carbohydrate or starch-based biological materials into smaller sugar molecules.
Lipases are useful for breaking down oily, greasy and fatty biological materials.
Cellulases can provide general cleaning benefits.
Proteases are particularly useful for breaking down proteinaceous biological materials, reducing long proteins into smaller chains and amino acids.
As examples of proteases there may be mentioned serine, threonine, cysteine, aspartate, metallo-and glutamic acid proteases. Alkaline proteases are particularly useful in view of the pH of the composition.
Particularly useful proteases may be derived from the genus Bacillus, including the alkaline proteases derived from Bacillus subtilis, Bacillus lentus, and Bacillus licheniformis. Proteases derived from sources other than those mentioned above can also be used.
Various protease-containing solutions are commercially available.
Examples include those are under the trade names EverlaseTM 16L, SavinaseTM, including SavinaseTM 16.0 L, SavinaseTM Ultra, Savinase Ultra 16XL, LiquanaseTM or EsperaseTM from Novozymes or PurafectTM L, PurafectTM Ox, Purafect TMPrime L from Genencor.
Amylases may be obtained from any suitable source, for example barley malt, micro-organisms of the genus Bacillus such as Bacillus subtillis, Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus licheniformis especially containing a Bacillus sterothermophilus gene for alpha-amylase, Bacillus subtiis containing a Bacillus megaterium gene for alpha-amylase or Bacillus acidopullulyticus. Useful examples of such amylases are commercially available under the trade names PurastarTM SI, PurastarTM HP AmL from Genencor or StainzymeTM, DuramylTM, TermamylTM, Termamyl 300L Type DX, TermamylTM Ultra from Novozymes.
Optionally the enzyme comprises a further secondary enzyme, including but not limited to a pectinase, carbohydrase, beta-glucanase, hemicellulase, and/or a xylanase.
Preferably the enzyme comprises a protease and an amylase, preferably in a weight ratio of 1:4 to 4:1.
The composition preferably comprises 0.052 to 10 parts, more preferably 0.1 to 8 parts and especially 0.2 to 5 parts of enzyme.
The boron-containing compound may be a single boron-containing compound or a mixture comprising two or more boron-containing compounds.
Preferably the boron-containing compound is an organic borate.
The boron-containing compound is believed to stabilise the enzyme(s) of component (i). Preferred boron-containing compounds include boronic acids, boric acids, borates and polyborates in salt form and mixtures comprising two or more of the same (e.g. 2 to 4).
Examples of suitable boron-containing compounds include sodium tetraborate, aromatic borate esters, phenyl boronic acids and especially 4-formylphenyl boronic acid and salts thereof.
The composition preferably comprises 0.05 to 7.5 parts, more preferably 0.1 to 5 parts and especially 0.2 to 0.5 parts of boron-containing compound.
The water-soluble calcium salt may be a single water-soluble calcium salt or a mixture comprising two or more water-soluble calcium salts. The water-soluble calcium salt is also believed to stabilise the enzyme(s) of component (i).
Preferred water-soluble calcium salt include calcium chloride, calcium bromide, calcium nitrate, calcium acetate.
The composition preferably comprises 0.05 to 5 parts, more preferably 0.1 to 2 parts and especially 0.15 to 1 part of water-soluble calcium salt.
The polyol may be a single polyol or a mixture comprising two or more polyols.
Preferred polyols comprise two or more hydroxy groups, e.g. 2 to 5 hydroxy groups. Suitable polyols include alkylene glycol polyols and glycerine. Examples of alkylene glycol polyols include ethylene glycol, 1,2-propylene glycol and 1,3-propylene glycol. Especially preferred polyols are 1,2-propylene glycol and glycerine.
The composition preferably comprises 2 to 28 parts, more preferably 15 to parts of polyol.
The amine may be a single amine or a mixture comprising two or more amines. Preferred amines are alkanolamines.
The amine is useful for adjusting the pH of the composition into the range 8.1 to 8.9, either alone or in combination with another ingredient have a pH above 7. Furthermore, alkanolamines are also believed to enhance the cleaning ability of the composition.
Suitable amines include monoalkanolamines, dialkanolamines, trialkanolamines, and alkylalkanolamines such as alkyl-dialkanolamines, and dialkyl-monoalkanolamines. The alkanol and alkyl groups present in the alkanolamine are generally short to medium chain length, that is, from 1 to 10 carbons in length. Preferred alkanolamines are trialkanolamines, including triethanolamine or triisopropanolamine.
The amount of amine in the composition is generally selected such that the pH of the composition is 8.1 to 8.9. In practice this typically means ito 15 parts, preferably 3 to 10 parts of amine.
The surtactant may be a single surtactant or a mixture comprising two or more surfactant. Non-ionic surtactants are preferred.
Useful surtactants include, for example, those with hydroxyl, ether, amine oxide, phosphine oxide, sulphoxide, propargyl, ester or amide functionalities.
Among these, ethoxylates are especially useful, and these include, for instance, alcohol ethoxylates, mono alkanolamide ethoxylates, fatty amine ethoxylates, fatty acid ethoxylates, ethylene oxide/propylene oxide copolymers, and alkyl phenol ethoxylates. Further useful surfactants include multiple hydroxyl molecules, for example glucosides, glycerides, glycol esters, glycerol esters, polyglycerol esters and polyglycerides, polyglycosides, sorbitan esters and sorbitan ester ethoxylates and sucrose esters.
Desirably, the surtactant is a low foaming surtactant because this makes the composition particularly suitable for use in automated cleaning devices for medical instruments.
Commercially available low foaming surtactants include Amphoteric 400; AO-405; AO-455; TomadolTM 1-3 and 1-5; NonidetTM SF-3, SF-5 and RK-18; TomadyneTM 101 LF, 103 LF, 105 LF, 107 LF, 109 LF, 111 LF and 113 LF; all available from Tomah Products, Inc. These commercial products contain large quantities of water and the amounts included in the composition are calculated on the actual number of parts of the surtactant.
In a further embodiment, preferred surtactants are the ethylene oxide/propylene oxide copolymers, There are many possible variations within this class, with three main types being particularly preferred. The PluronicTM copolymers having the formulas (EO)n(PO)m(EO)n, where EO is ethylene oxide, P0 is propylene oxide and m and each n independently has a value of 1 to 20,000; the reverse PluronicTM copolymers having the formulas (P0)n(E0)m(P0)n, with the same abbreviations as above; and the corresponding E0/P0 copolymers having an alkyl end group on one or both ends. The copolymers above are represented as block copolymers, although random copolymers are also useful in the compositions according to the invention. It should be noted that even those copolymers commercialized as block copolymers will have some degree of randomness. Glycerol-based E0/P0 block mid random copolymers and ethylene amine-based block and random copolymers are also useful in the compositions according to the invention. Particularly preferred surtactants are available from Akzo Nobel under the trade name Berol, for example BerolTM LFG-61.
The amount of surtactant included in the composition is preferably 5 to 25 parts, more preferably 10 to 20 parts. Where the surtactant is obtained from a commercial source as an aqueous composition, the weight of the water and any other non-surtactant ingredients are ignored when calculating the number of parts of surtactant.
The composition optionally further comprises a defoaming agent, e.g. 0.1 to 5 parts by weight, in total, of defoarning agent(s). This can be useful when the composition is used in automated cleaning apparatus where excessive foam formation can be undesirable. When a defoarning agent is included in the composition one may use surtactants having a higher tendency to foam because the defoaming agent will suppress the foam formation.
Classes of defoaming agents include silicone, PEG and PPG defoaming agents. Silicone defoaming agents are available commercially, e.g. DF-400, DF- 403, DF-410 and DF-430 from Chemco Products, USA. Dow Corning also sell a range of defoaming agents, as well as GE Silicones, Air Products and Munzing.
Commercially available defoaming agents include the following from Clariant: AntimussolTM 3470 (mixture of N-alkyl isononanamide, butylpolyglycol, ethoxylate and a fluorine compound), AntimussolTM 3472 (a mixture of defoamer and a quaternary ammonium compound), AntimussolTM 4459 (an aqueous dispersion of a polysiloxane fatty acid derivative), AntimussolTM 4752 (a mixture of silicon and nitrogen containing substances and small amounts of a fluorine compound), AntimussolTM FN (a mixture of glycols, N-alkyl isononanamide and a fluorine compound), AntimussolTM TIP (a mixture of butoxethylphosphates and isobutanol 50 liquid) and AntimussolTM TW (a mixture of tallow fatty acid, tallow fatty alcohol and ethoxylate).
The compositions may include one or more further optional constituents or adjuvants. These include, inter a/ia, corrosion inhibitors and components which improve the aesthetic appeal of the composition. For example, materials which aid in reducing brass corrosion are particularly useful for preventing corrosion damage of any brass components in the objects to be cleaned by the compositions according to the invention. Triazole compounds are particularly useful brass corrosion inhibitors, e.g. tolyltriazole and salts thereof, tolyltriazole, benzotriazole, carboxybenzotriazole and mixtures comprising two or more of the same. Commercially available corrosion inhibitors include COBRATECTM TT100, COBRATECTM TT-50-S, COBRATECTM CBT, COBRATECTM CBT-E, COBRATECTM 99, COBRATECTM 928 and COBRATECTM 911S from PMC Specialties Group, Inc..
Thus in a preferred composition according to the first aspect of the present invention, the enzyme comprises a protease and an amylase, the boron containing compound is water-soluble, the polyol is an alkylene glycol polyols and/or glycerine, the amine is an alkanolamine, the surtactant is a non-ionic surtactant and the composition optionally further comprises a corrosion inhibitor.
Other adjuvants which may be incorporated into the composition include pH buffers, perfumes, biocides, pigments and dyes.
In a preferred embodiment the composition further comprises a peptide aldehyde stabilizing agent. Such agents are described in International patent publication No. WO 201 0/0550052 of Novozymes A/S. The amount of peptide aldehyde stabilizing agent used, when present, is preferably in the range 0.5 to 10 mg per bOg of composition.
The amount of water included in the composition may be varied across wide limits. For example, when the composition is a concentrate which is diluted before use the water content will typically be lower than in compositions actually used for cleaning medical devices. Concentrates are useful for efficient transportation of the composition. For concentrates, the typical water content is preferably 30 to 70 parts, more preferably 40 to 60 parts and especially 45 to 55 parts. Such concentrates may be diluted with water before use if desired, for example to provide a water content of 80 to 99.9 parts, preferably 90 to 99.85 parts and especially 97 to 99.8 parts. The water is preferably de-ionized or purified water.
The pH of the composition is preferably 8.1 to 8.9, especially pH 8.3 to 8.8.
The compositions may also be used generally for cleaning surfaces which come into contact with biological materials, e.g. the cleaning of hard surfaces, particularly metal surfaces, in the health care environment (e.g. hospitals, dental clinics and veterinary practices). Such surfaces include operating tables, trays, gurneys, instrument surfaces, equipment surfaces, etc. The types of medical devices which may be cleaned with the present composition are not particularly limited and include devices used in dental and veterinary procedures. Examples of medical devices include endoscopes, surgical instruments, operating room hand pieces, ventilation tubes and dental hand pieces.
The present invention also provides a method of cleaning a medical device or surface in a healthcare environment to remove biological materials therefrom comprising applying thereto a composition according to the first aspect of the present invention.
The process for cleaning a medical device preferably comprises the steps: a) placing a medical device contaminated with biological materials into a container; b) applying a composition according to the first aspect of the present invention to the device with agitation, shaking, ultra sound, as a jet of fluid or any combination thereof, thereby cleaning the device with the composition by applying alternating pressure to the container; c) optionally rinsing the device to remove at least some of the composition therefrom; d) optionally sterilising the device; and e) optionally drying the device.
In one embodiment step b) is performed at a temperature below 45°C, preferably below 4100.
In one embodiment the container is an alternating pressure resistant container. For example, an alternating pressure resistant container as described in International patent publication WO 2010/055121 of Novozymes NS may be used.
Preferably the rinsing and drying of steps c) and e) are performed, optionally in combination with sterilising step d).
The compositions of the present invention have good cleaning efficacy. As a result the invention compositions may be used for cleaning medical devices at temperature of, for example, 20 to 40°C. Furthermore, the compositions may display little foaming or corrosiveness compared to existing formulations on the market.
The invention will be further described in the following, non-limiting examples in which all parts are by weight. The Examples use the following ingredients: SokalanTM PA300L A dispersant having a 45% solids content.
DequestTM PB 11620 Carboxymethyl inulin, sodium salt solution, _________________________ having a 20% actives content (a scale inhibitor) Propylene glycol A polyol.
Triethanolamine, 80% An amine.
BerolTM LFG-61 A low foaming non-ionic surfactant having an _______________________ actives content of 95%.
Potassium hydroxide, 48% A pH adjusting agent.
Benzotriazole A corrosion inhibitor.
SavinaseTM Ultra 1 6XL An enzyme (protease from Novozymes).
TermamylTM 300L Type DX An enzyme (a-amylase of from Bacillus ________________________ licheniformis, from Novozymes).
Examples I to 4 and Comparative Examples CE1 to CE4 Stacie 1 -Preparation of Compositions The following compositions shown in Tables 1 and 2 were prepared by mixing the listed ingredients in demineralised water, and stirring to provide a homogenous mixture. The numbers in the tables relate to the number of parts by weight of the relevant component.
Table 1 -Examples
Component Example I Example 2 Example 3 Example 4 SavinaseTM Ultra 6.0 6.0 6.0 6.0 16XL7 ___________ ___________ ___________ ___________ TermamylTM 300L 3.6 3.6 3.6 3.6 Type DX7 __________ __________ __________ __________ Calcium chloride1 0.17 0.17 0.17 0.17 Propylene glycol 22.5 22.5 22.5 22.5 Triethanolamine2 8 8 8 8 BerolTM LFG-613 14.25 14.25 14.25 14.25 Citric acid 0.97 0.4 0.4 0.4 monohydrate ___________ ___________ ___________ ____________ SokalanTM PA3OCL 0.56 0.56 0.56 0.56 DequestTM PB 0.06 0.06 0.06 0.06 11620 __________ __________ __________ __________ Potassium --0.30 0.37 hydroxide ___________ ___________ ___________ ____________ Benzotriazole 0.5 0.5 0.5 0.5 Water to 100 parts to 100 parts to 100 parts to 100 parts pH @25°C 8.10 8.35 8.79 8.90 Table 2 -Comparative Examples Component Identity ________ CE2 CE3 CE46 SavinaseTM Ultra 16XL7 6.0 6.0 6.0 6.0 TermamylTM 300L Type DX7 3.6 3.6 3.6 3.6 Calcium chloride1 0.17 0.17 0.17 0.17 Propylene glycol 22.5 225 22.5 22.5 Triethanolamine2 8 8 8 8 BerolTM LFG-613 14.25 1425 14.25 14.25 Citric acid monohydrate 4.34 2.87 1.29 0.4 SokalanTM PA3OCL4 0.56 0.56 0.56 0.56 DequestTM PB 1162O 0.06 0.06 0.06 0.06 Potassium hydroxide ---0.40 Benzotriazole 0.5 0.5 0.5 0.5 Water to 100 to 100 to 100 to 100 _____________________________ parts parts parts parts pH @ 25°C 7.00 7.50 7.99 9.02 Notes to Tables 1 and 2: 1. The calcium chloride used was 0.5 parts of a 33% solution in water.
2. The triethanolamine used was 10 parts at 80% strength.
3. The surtactant used was 15 parts at 95% strength.
4. The SokalanTM PA3OCL used was 1.25 parts at 45% strength.
5. The DequestTM PB1 1620 used was 0.3 parts at 20% strength.
6. The composition of Comparative Example CE4 was unstable over time and a precipitate formed.
7. These commercial products are about 85% water. Therefore the number of parts of enzyme present is <15% of the figure shown in Tables 1 and 2, e.g. 6 parts of commercial product corresponds to less than 0.9 parts of enzyme and 3.6 parts corresponds to less than 0.54 parts of enzyme.
SavinaseTM Ultra 16XL also contains 4-formylphenyl boronic acid and therefore also provides the boron-containing compound.
The compositions described in Tables 1 and 2 were tested to evaluate their efficiency for dried blood removal. Dried blood was selected because it is particularly difficult to remove.
Stacie 2 -Use of the Compositions Sheep blood (10cm3) was re-activated by adding calcium chloride solution (0.25M, 300pl) and double distilled water (1 0cm3).
For the purpose of testing, instead of a medical device the re-activated blood (0.025 cm3) was applied to ash-free filter paper of size 4 cm2 and dried in an oven at 40°C for 1 hour to give a dried, blood-stained filter paper. The compositions described in Tables 1 and 2 (10cm3) were each diluted to 1 litre using artificial hard water with a hardness of 50°FH.
The diluted compositions were each poured into a thermostatic beaker (25 cm3) set to a temperature of 37°C. When the temperature of the diluted composition reached 37°C, the dried, blood-stained filter paper was added and left for exactly 5 minutes without mechanical action. This simulated the cleaning of a medical device. The filter paper with any remaining blood stain was then removed and the remaining composition, containing washed-off blood, was called the Filter Paper Washing.
Any blood remaining on the filter paper was extracted by bringing it in contact for 1 hour with a sodium dodecylsulphonate solution in water (2.5cm3 of a 1% solution) under constant stirring at 300 rpm. This gives what is referred to as the Residual Blood Solution.
Stacie 3 -Preparation of a Standard Curve to Calculate Blood Concentrations The concentration of blood was determined spectroscopically using a Hewlett Packard 8453 spectrophotometer by a method involving the measurement of absorption at 340nm, which corresponds to the wavelength absorbed by proteins typically found in blood after they have been derivatised with a reagent called OPA Reagent'.
Firstly, a standard curve was prepared by treating a range of known concentrations of protein (freshly prepared bovine serum albumin, fraction V) with OPA reagent. This curve was used subsequently to determine the concentration of protein (and by inference the concentration of blood) in various samples by comparing the absorption of the sample at 340nm (corrected as mentioned below) with the standard curve to reveal the corresponding protein concentration.
The OPA Reagent used to derivatise proteins had the following formulation: sodium tetraborate 2.012 g ortho-phtaldialdehyde 0.080 g NN-dimethylmercapto ethylammoniumchloride 0.200 g methanol 4 cm3 sodium dodecylsulphate 20% 5 cm3 double-distilled water to 100 cm3 In addition, a formulation called the Characteristic Reagent' was prepared having exactly the same formulation as the OPA Reagent except that the ortho-phtaldialdehyde and N,N-dimethylmercapto ethylarnmoniumchloride were omitted.
Stacie 4 -Use of the Standard Curve to Calculate Blood Concentrations As mentioned in Stage 3, the absorption at 340nm indicates the protein and therefore blood concentration in the Filter Paper Washing. However this absorption requires correction and such correction is performed as follows: Corrected absorbtion at 340nm = (Al-A2)-(B1-B2) wherein: Al is the absorption at 340nm of 1 part of OPA Reagent and 1 part of Filter Paper Washing; A2 is the absorption at 340nm of 1 part of Characteristic Reagent and 1 part of the Filter Paper Washing; Bl is the absorption at 340nm of 1 part of OPA Reagent and 1 part of the fresh, unused composition; and B2 is the absorption at 340nm of 1 part of Characteristic Reagent and 1 part of the fresh, unused composition used to wash the filter paper.
If the absorption values are too high, it is known by a person skilled in the art that one needs to make further dilution and take the dilution factor into account for the calculation.
The amount of blood present in the Filter Paper Washing ("wtFPW") was calculated by multiplying the blood concentration of the Filter Paper Washing by the volume of the Filter Paper Washing.
The blood concentration in the Residual Blood Solution was measured in an analogous manner. The amount of blood remaining on the filter paper after it had been washed ("wtRBS") was calculated by multiplying the blood concentration in the Residual Blood Solution by the volume of the Residual Blood Solution.
Stacie 5 -Calculation of Clean mci Efficiency The cleaning efficiency of the compositions of the invention was determined by the following calculation: Cleaning Efficiency = 100% X (wtFPW/(wtFPW + wtRBS)) Results The cleaning efficiency for the compositions described in the Examples and Comparative Examples ("CE") are shown in Table 3:
Table 3
Example pH Cleaning Efficiency CE1 7.00 541% CE2 7.50 598% CE3 7.99 639% 1 8.10 656% 2 8.35 6T4% 3 8.79 69i% 4 8.90 68A% CE4 9.02 Not measured (unstable) The results in Table 3 show that the cleaning efficiency for Examples 1 to 4 was significantly higher than for the Comparative Examples CE1 to CE3.
Claims (13)
- CLAIMS1. An aqueous composition comprising the following components: (i) 0.01 to 15 parts of enzyme; (ii) 0.01 to 10 parts of boron-containing compound; (iii) 0.01 to 10 parts of water-soluble calcium salt; (iv) 1 to 30 parts of polyol; (v) 1 to 15 partsof amine; (vi) 2 to 30 parts of surtactant; and (vii) water; wherein all parts are by weight and the composition has a pH of 8.1 to 8.9.
- 2. A composition according claim 1 having a pH of 8.3 to 8.8.
- 3. A composition according claim 1 or 2 which further comprises a corrosion inhibitor.
- 4. A composition according to any one of the preceding claims wherein the amine is an alkanolamine.
- 5. A composition according to any one of the preceding claims wherein the enzyme comprises a protease and an amylase.
- 6. A composition according to claim 1 or 2 wherein the enzyme comprises a protease and an amylase, the boron containing compound is water-soluble, the polyol is an alkylene glycol polyols and/or glycerine, the amine is an alkanolamine, the surfactant is a non-ionic surfactant and the composition optionally further comprises a corrosion inhibitor.
- 7. A composition according to claim 1 wherein the components are preferably present in the following range: (i) 0.2 to 5 parts of enzyme; (ii) 0.05 to 7.5 parts of boron-containing compound; (iii) 0.15 to 1 parts of water-soluble calcium salt; (iv) 15 to 25 parts of polyol; (v) 3 to 10 parts of amine; (vi) 10 to 20 parts of surfactant; and (vii) water; wherein all parts are by weight and the composition has a pH of 8.3 to 8.8.
- 8. A method of cleaning a medical device or surface in a healthcare environment to remove biological materials therefrom comprising applying thereto a composition according to any one of the preceding claims.
- 9. A process according to claim 8 for cleaning a medical device comprising the steps: a) placing a medical device contaminated with biological materials into a container; b) applying a composition according to the first aspect of the present invention to the device with agitation, shaking, ultra sound, as a jet of fluid or any combination thereof, thereby cleaning the device with the composition by applying alternating pressure to the container; c) optionally rinsing the device to remove at least some of the composition therefrom; d) optionally sterilising the device; and e) optionally drying the device.
- 10. A process according to claim 9 wherein step b) is performed at a temperature below 4500.
- 11. A process according to claim 9 or 10 wherein the container is an alternating pressure resistant container.
- 12. A process according to any one of claims 8 to 11 wherein the biological material comprises fat, blood, cerebrospinal fluid, cerumen, gastric juices, peritoneal fluid, pleural fluid, sebum, semen, sweat, vomit, saliva, tissue, bone, endolymph, perilymph, proteins, bodily exudates, discharges, urine and/or fecal matter.
- 13. A process according to any one of claims 8 to 12 wherein the medical device is an endoscope, surgical instrument, operating room hand piece, ventilation tube or dental hand piece.
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Cited By (6)
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EP2627752A1 (en) * | 2010-10-15 | 2013-08-21 | Realco SA | Product and method for the removal of biofilms |
WO2017129331A1 (en) * | 2016-01-28 | 2017-08-03 | Novozymes A/S | Method for cleaning a medical or dental instrument |
WO2017202442A1 (en) * | 2016-05-23 | 2017-11-30 | Ecolab Usa Inc. | Manual pre-cleaner and disinfectant for reprocessing of surgical instruments and flexible endoscopes |
EP3256564A4 (en) * | 2015-02-12 | 2018-04-25 | Whiteley Corporation Pty Ltd | Detergent for medical instrumentation |
WO2020052743A1 (en) * | 2018-09-11 | 2020-03-19 | Ecolab Usa Inc. | Phase stable and low foaming aqueous detergent compositions having a long time enzyme activity |
EP4234668A3 (en) * | 2018-04-27 | 2023-10-04 | The Procter & Gamble Company | Hard surface cleaners comprising carboxylated fructan |
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GB2360041A (en) * | 2000-03-11 | 2001-09-12 | Reckitt Benckiser Inc | Cleaning compositions containing enzymes |
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GB2360041A (en) * | 2000-03-11 | 2001-09-12 | Reckitt Benckiser Inc | Cleaning compositions containing enzymes |
Cited By (11)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP2627752A1 (en) * | 2010-10-15 | 2013-08-21 | Realco SA | Product and method for the removal of biofilms |
EP3256564A4 (en) * | 2015-02-12 | 2018-04-25 | Whiteley Corporation Pty Ltd | Detergent for medical instrumentation |
US10017719B2 (en) | 2015-02-12 | 2018-07-10 | Whiteley Corporation Pty. Ltd. | Detergent for medical instrumentation |
WO2017129331A1 (en) * | 2016-01-28 | 2017-08-03 | Novozymes A/S | Method for cleaning a medical or dental instrument |
CN108603146A (en) * | 2016-01-28 | 2018-09-28 | 诺维信公司 | Method for cleaning medical treatment or dental instruments |
US20190024022A1 (en) * | 2016-01-28 | 2019-01-24 | Novozymes A/S | Method for Cleaning a Medical or Dental Instrument |
EP3408366B1 (en) | 2016-01-28 | 2021-12-08 | Novozymes A/S | Method for cleaning a medical or dental instrument |
CN108603146B (en) * | 2016-01-28 | 2022-08-02 | 诺维信公司 | Method for cleaning a medical or dental instrument |
WO2017202442A1 (en) * | 2016-05-23 | 2017-11-30 | Ecolab Usa Inc. | Manual pre-cleaner and disinfectant for reprocessing of surgical instruments and flexible endoscopes |
EP4234668A3 (en) * | 2018-04-27 | 2023-10-04 | The Procter & Gamble Company | Hard surface cleaners comprising carboxylated fructan |
WO2020052743A1 (en) * | 2018-09-11 | 2020-03-19 | Ecolab Usa Inc. | Phase stable and low foaming aqueous detergent compositions having a long time enzyme activity |
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