WO2001084937A1 - Oxidoreductase mediated antimicrobial activity - Google Patents
Oxidoreductase mediated antimicrobial activity Download PDFInfo
- Publication number
- WO2001084937A1 WO2001084937A1 PCT/DK2001/000315 DK0100315W WO0184937A1 WO 2001084937 A1 WO2001084937 A1 WO 2001084937A1 DK 0100315 W DK0100315 W DK 0100315W WO 0184937 A1 WO0184937 A1 WO 0184937A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- composition according
- alkyl
- acyl
- composition
- laccase
- Prior art date
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Classifications
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N65/00—Biocides, pest repellants or attractants, or plant growth regulators containing material from algae, lichens, bryophyta, multi-cellular fungi or plants, or extracts thereof
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
- A01N63/50—Isolated enzymes; Isolated proteins
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N65/00—Biocides, pest repellants or attractants, or plant growth regulators containing material from algae, lichens, bryophyta, multi-cellular fungi or plants, or extracts thereof
- A01N65/08—Magnoliopsida [dicotyledons]
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N65/00—Biocides, pest repellants or attractants, or plant growth regulators containing material from algae, lichens, bryophyta, multi-cellular fungi or plants, or extracts thereof
- A01N65/08—Magnoliopsida [dicotyledons]
- A01N65/20—Fabaceae or Leguminosae [Pea or Legume family], e.g. pea, lentil, soybean, clover, acacia, honey locust, derris or millettia
Definitions
- the present invention relates to an enzymatic antimicrobial method for killing or inhibiting microbial cells or micro-organisms present, e.g., in laundry, on hard surfaces, in water systems, on skin, on teeth or on mucous membranes.
- the present invention also relates to the use of an enzymatic antimicrobial composition for preserving food products, cosmetics, paints, coatings, etc.
- WO94/04127 discloses stabilized dentifrice compositions which are capable of producing antimicrobially effective concentrations of hypothiocyanite ions.
- the compositions contain an oxidoreductase capable of producing hydrogen peroxide and a peroxidase enzyme capable of oxidizing thiocyanate ions normally present in saliva to antimicrobial hypothiocyanite ions.
- Suitable peroxidases include lactoperoxidase, myeloperoxidase, salivary peroxidase and chloroperoxidase.
- the object of the present invention is to provide an enhanced method for killing or inhibiting microbial cells.
- a method for killing or inhibiting microbial cells comprising treating said microbial cells with a phenol oxidizing enzyme system and an enhancing agent selected from the group consisting of:
- a and B are 6 membered aromatic rings, and may independently of each other be substituted with H, OH, C ⁇ . 8 -alkyl, acyl, SO 3 H, NO 2 , CN, CI, Br, F, NHR8, N(R8) 2 , OR9, C ⁇ - 8 -alkyl-OR9, or C ⁇ - 8 -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - 4 -alkyl or acyl.
- One or more carbon atoms of the aromatic rings of A, B, C, D, and E may independently of each other be substituted with N or S, thus rendering said aromatic ring a heterocyclic ring.
- the present invention relates to methods for killing or inhibiting microbial cells in laundry, in cosmetic products or on hard surfaces.
- the present invention relates to use of an enzymatic antimicrobial composition for cleaning of contact lenses, for cleaning of water systems, for presenting of paint, and in a cleaning-in-place system.
- the term "antimicrobial” is intended to mean that there is a bactericidal and/or a bacteriostatic and/or fungicidal and/or fungistatic effect and/or a virucidal effect and/or a sporicidal effect, wherein
- the term "bactericidal” is to be understood as capable of killing bacterial cells. Bactericidal activity is measured as a logarithmic reduction (log reduction) in the number of living cells or Colony Forming Units pr. ml (CFU/ml), e.g.
- 1 log reduction corresponds to a reduction in the number of living cells of Pseudomonas putida ATCC12633 from Y x 10 x CFU/M (CFU: Colony Forming Units; M: ml or g) to Y x 10 x"1 CFU/M, where X can be 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10 or 11 , and Y can be any number from 0 to 10.
- the number of living cells are to be determined as the number of Pseudomonas putida ATCC12633, which can grow on LB Agar (#0285, Merck, Germany) plates at 30°C.
- bacteriostatic is to be understood as capable of inhibiting bacterial growth, i.e. inhibiting growing bacterial cells.
- fungicidal is to be understood as capable of killing fungal cells.
- fungistatic is to be understood as capable of inhibiting fungal growth, i.e. inhibiting growing fungal cells.
- sporicidal is to be understood as capable of inactivating spores.
- microbial cells denotes bacterial or fungal cells
- microorganism denotes a fungus (including yeasts) or a bacterium.
- the term "inhibiting growth of microbial cells” is intended to mean that the cells are in the non-growing state, i.e., that they are not able to propagate.
- the "phenol oxidizing enzyme system” describes an enzyme possessing peroxidase activity together with a hydrogen peroxide source, or a laccase or laccase related enzyme together with oxygen.
- hard surface as used herein relates to any surface, which is essentially non-permeable for micro-organisms.
- hard surfaces are surfaces made from metal, e.g., stainless steel, plastics, rubber, board, glass, wood, paper, textile, concrete, rock, marble, gypsum and ceramic materials which optionally may be coated, e.g., with paint, enamel and the like.
- the hard surface can also be a process equipment, e.g., a cooling tower, an osmotic membrane, a water treatment plant, a dairy, a food processing plant, a chemical or pharmaceutical process plant. Accordingly, the composition according to the present invention is useful in a conventional cleaning-in-place (C-l-P) system. Enhancing agent
- the present invention relates to enhancing agents selected from the group consisting of:
- a and B are six membered aromatic rings, and may independently of each other be substituted with H, OH, d-s-alkyl, acyl, SO 3 H, NO 2 , CN, CI, Br, F, NHR8, N(R8) 2) OR9, Ci- 8 -alkyl-OR9, or C ⁇ - 8 -alkyl-OOR9; wherein R8, and R9 are H, C1-4- alkyl or acyl.
- a and B may independently of each other be substituted with H, OH, C ⁇ -alkyl, acyl, NO 2 , CI, Br, NHR8, N(R8) 2 , OR9, C ⁇ .
- substituents of A are independently of each other H, OH, Ci-s-alkyl, acyl, SO 3 H, NO 2 , CN, CI, Br, F, NHR8, N(R8) 2 , OR9, C ⁇ - 8 -alkyl-OR9, or C ⁇ -
- R8, and R9 are H, C ⁇ - 4 -alkyl or acyl.
- substituents of A are independently of each other H, OH, C ⁇ - -alkyl, acyl, NO 2 , CI, Br,
- R8, and R9 are H, C-i. 4 -alkyl or acyl.
- R8, and R9 are H, C-i. 4 -alkyl or acyl.
- the substituents of B are independently of each other H, OH, C ⁇ - 4 -alkyl, acyl, NO 2 , CI, Br,
- R1 , R2, R3, R4, and R5 of C are independently of each other H, OH, C ⁇ . 8 -alkyl, acyl, SO3H, NO 2 , CN, CI, Br, F, NHR8, N(R8) 2 , OR9, C ⁇ - 8 - alkyl-OR9, or C ⁇ - 8 -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - -alkyl or acyl.
- R1 , R2, R3, R4, and R5 of C are independently of each other H, OH, C1- 4 - alkyl, acyl, NO 2 , CI, Br, NHR8, N(R8) 2 , OR9, C ⁇ . 4 -alkyl-OR9, or C ⁇ - 4 -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - 4 -alkyl or acyl.
- R1 , R2, R3, R4, and R5 of D are independently of each other H, OH, C ⁇ - 8 -alkyl, acyl, SO3H, NO 2 , CN, CI, Br, F, NHR8, N(R8) 2 , OR9, C ⁇ - 8 - alkyl-OR9, or C ⁇ - 8 -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - -alkyl or acyl.
- R1 , R2, R3, R4, and R5 of D are independently of each other H, OH, C1- 4 - alkyl, acyl, NO 2 , CI, Br, NHR8, N(R8) 2) OR9, C ⁇ - 4 -alkyl-OR9, or C ⁇ - 4 -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - 4 -alkyl or acyl.
- R1 , R2, R3, R4, and R5 of E are independently of each other H, OH, Ci-s-alkyl, acyl, SO 3 H, NO 2 , CN, CI, Br, F, NHR8, N(R8) , OR9, C ⁇ - 8 -alkyl- OR9, or C ⁇ -8-alkyl-OOR9; wherein R8, and R9 are H, C ⁇ . 4 -alkyl or acyl.
- R1 , R2, R3, R4, and R5 of E are independently of each other H, OH, C ⁇ - 4 -alkyl, acyl, NO 2 , CI, Br, NHR8, N(R8) 2 , OR9, C ⁇ - 4 -alkyl-OR9, or C ⁇ - 4 -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - 4 -alkyl or acyl.
- R10, R11 , R12, R13, R14, R15, R16 and R17 of F are independently of each other H, OH, C ⁇ . 8 -alkyl, acyl, SO 3 H, NO 2 , CN, CI, Br, F, NHR8, N(R8) 2 , OR9, C ⁇ -8-alkyl-OR9, or C ⁇ - 8 -alkyl-OOR9; wherein R8, and R9 are H, Chalky! or acyl.
- R10, R11 , R12, R13, R14, R15, R16 and R17 of F are independently of each other H, OH, C ⁇ - 4 -alkyl, acyl, NO 2 , CI, Br, NHR8, N(R8) 2 , OR9, C ⁇ - 4 -alkyl-OR9, or C ⁇ - -alkyl-OOR9; wherein R8, and R9 are H, C ⁇ - 4 -alkyl or acyl.
- C ⁇ - n -alkyl wherein n can be from 1 through 8, as used herein, represent a branched or straight, saturated or unsaturated alkyl group having from one to the specified number of carbon atoms.
- Typical C ⁇ -6-alkyl groups include, but are not limited to, methyl, ethyl, ethenyl (vinyl), ⁇ -propyl, iso-propyl, propenyl, isopropenyl, butyl, iso-butyl, sec-butyl, terf-butyl, crotyl, methallyl, pentyl, iso-pentyl, prenyl, hexyl, iso-hexyl and the like.
- acyl refers to a monovalent substituent comprising a C- ⁇ -6-alkyl group linked through a carbonyl group; such as e.g. acetyl, propionyl, butyryl, isobutyryl, pivaloyl, valeryl, and the like.
- At least one of the substituents of A are H, preferably at least two of the substituents of A are H, more preferably at least three of the substituents of A are H, most preferably at least four of the substituents of A are H, in particular all the substituents of A are H.
- at least one of the substituents of B are H, preferably at least two of the substituents of B are H, more preferably at least three of the substituents of B are H, most preferably at least four of the substituents of B are H, in particular all the substituents of B are H.
- At least one of the substituents R1 , R2, R3, R4, and R5 of C are H, preferably at least two of the substituents R1 , R2, R3, R4, and R5 of C are H, more preferably at least three of the substituents R1 , R2, R3, R4, and R5 of C are H, most preferably at least four of the substituents R1 , R2, R3, R4, and R5 of C are H, in particular all the substituents R1 , R2, R3, R4, and R5 of C are H.
- At least one of the substituents R1 , R2, R3, R4, and R5 of D are H, preferably at least two of the substituents R1 , R2, R3, R4, and R5 of D are H, more preferably at least three of the substituents R1 , R2, R3, R4, and R5 of D are H, most preferably at least four of the substituents R1 , R2, R3, R4, and R5 of D are H, in particular all the substituents R1 , R2, R3, R4, and R5 of D are H.
- At least one of the substituents R1 , R2, R3, R4, and R5 of E are H, preferably at least two of the substituents R1 , R2, R3, R4, and R5 of E are H, more preferably at least three of the substituents R1 , R2, R3, R4, and R5 of E are H, most preferably at least four of the substituents R1 , R2, R3, R4, and R5 of E are H, in particular all the substituents R1 , R2, R3, R4, and R5 of E are H.
- At least one of the substituents R10, R11 , R12, R13, R14, R15, R16, and R17 of F are H, preferably at least two of the substituents R10, R11 , R12, R13, R14, R15, R16, and R17 of F are H, more preferably at least three of the substituents R10, R11 , R12, R13, R14, R15, R16, and R17 of F are H, more preferably at least four of the substituents R10, R11 , R12, R13, R14, R15, R16, and R17 of F are H, more preferably at least five of the substituents R10, R11 , R12, R13, R14, R15, R16, and R17 of F are H, more preferably at least seven of the substituents R10, R11 , R12, R13, R14, R15, R16, and R17 of F are H, most preferably at least six of the substituents R
- the enhancing agent is selected from the group consisting of: 4-aminophenol; p-Coumaric acid; 4,4'-Biphenol;
- Methylsyringate Propyl sinapate
- the enhancing agent of the invention may be present in concentrations of from
- 1 to 1000 ⁇ M preferably of from 5 to 500 ⁇ M, and more preferably from 10 to 200 ⁇ M.
- the source may be hydrogen peroxide or a hydrogen peroxide precursor for in situ production of hydrogen peroxide, e.g., percarbonate or perborate, or a hydrogen peroxide generating enzyme system, (e.g., an oxidase together with a substrate for the oxidase, e.g., an amino acid oxidase together with a suitable amino acid), or a peroxycarboxylic acid or a salt thereof.
- Hydrogen peroxide may be added at the beginning of or during the process, e.g., typically in an amount corresponding to levels of from 0.001-25 mM, preferably to levels of from 0.005-5 mM, and particularly to levels of from 0.01-1 mM.
- the phenol oxidizing enzyme requires molecular oxygen, molecular oxygen from the atmosphere will usually be present in sufficient quantity. If more O2 is needed, additional oxygen may be added.
- the enzyme of the phenol oxidizing enzyme may be an enzyme possessing peroxidase activity or a laccase or a laccase related enzyme.
- the enzyme of the invention may typically be present in concentrations of from 1 to 100000 ⁇ g enzyme protein per liter aqueous solution, preferably of from 5 to
- Compounds possessing peroxidase activity may be any peroxidase enzyme comprised by the enzyme classification (EC 1.11.1.7), or any fragment derived therefrom, exhibiting peroxidase activity.
- the peroxidase according to the invention is producible by plants (e.g. horseradish or soybean peroxidase) or micro-organisms such as fungi or bacteria.
- plants e.g. horseradish or soybean peroxidase
- micro-organisms such as fungi or bacteria.
- Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hyphomycetes, e.g., Fusarium, Humicola, Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia alii or Dreschlera halodes.
- DSM 2672 Fusarium oxysporum
- Humicola insolens Trichoderma resii
- Myrothecium verrucaria IFO 6113
- fungi include strains belonging to the subdivision Basidiomycotina, class Basidiomycetes, e.g., Coprinus, Phanerochaete, Coriolus or
- Coprinus cinereus f. microsporus IFO 8371
- Coprinus macrorhizus Phanerochaete chrysosporium (e.g. NA-12) or Trametes (previously called Polyporus), e.g., T. versicolor (e.g. PR4 28-A).
- fungi include strains belonging to the subdivision Zygomycotina, class Mycoraceae, e.g., Rhizopus or Mucor, in particular Mucor hiemalis.
- Some preferred bacteria include strains of the order Actinomycetales, e.g. Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
- Actinomycetales e.g. Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
- Rhodobacter sphaeroides Rhodomonas palustri, Streptococcus lactis, Pseudomonas purrocinia (ATCC 15958), Pseudomonas fluorescens (NRRL B-11) and Bacillus strains, e.g. Bacillus pumilus (ATCC 12905) and Bacillus stearothermophilus.
- bacteria include strains belonging to Myxococcus, e.g., M. virescens.
- the peroxidase may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said peroxidase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the peroxidase, in a culture medium under conditions permitting the expression of the peroxidase and recovering the peroxidase from the culture.
- a recombinantly produced peroxidase is a peroxidase derived from a Coprinus sp., in particular C. macrorhizus or C. cinereus according to WO 92/16634.
- compounds possessing peroxidase activity comprise peroxidase enzymes and peroxidase active fragments derived from cytochromes, haemoglobin or peroxidase enzymes.
- POXU peroxidase unit
- the reaction is followed for 60 seconds (15 seconds after mixing) by the change in absorbance at 418 nm, which should be in the range 0.15 to 0.30.
- laccases and laccase related enzymes comprise any laccase enzyme comprised by the enzyme classification (EC 1.10.3.2), any catechol oxidase enzyme comprised by the enzyme classification (EC 1.10.3.1 ), any bilirubin oxidase enzyme comprised by the enzyme classification (EC 1.3.3.5) or any monophenol monooxygenase enzyme comprised by the enzyme classification (EC 1.14.18.1).
- the above-mentioned enzymes may be microbial, i.e. derived from bacteria or fungi (including filamentous fungi and yeasts), or they may be derived from plants.
- Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinus, e.g., C. cinereus, C. comatus, C. friesii, and C. plicatilis, Psathyrel- la, e.g., P. condelleana, Panaeolus, e.g., P.
- papilionaceus Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Pycnoporus, e.g. P. cinnabarinus, Phlebia, e.g., P. radita (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2-238885).
- M. thermophila Schytalidium, e.g., S. thermophilum
- Polyporus e.g., P. pinsitus
- Pycnoporus e.g. P. cinnabarinus
- Phlebia e.g., P. radita (WO 92/01046)
- Coriolus e.g., C. hirsutus (JP 2-238885)
- Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
- a laccase derived from Coprinus, Myceliophthora, Polyporus, Pycnoporus, Scytalidium or Rhizoctonia is preferred; in particular a laccase derived from Coprinus cinereus, Myceliophthora thermophila, Polyporus pinsitus, Pycnoporus cinnabarinus, Scytalidium thermophilum or Rhizoctonia solani.
- the laccase or the laccase related enzyme may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said laccase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the laccase, in a culture medium under conditions permitting the expression of the laccase enzyme, and recovering the laccase from the culture.
- Laccase activity is determined from the oxidation of syringaldazin under aerobic conditions.
- the violet colour produced is photometered at 530 nm.
- the analytical conditions are 19 mM syringaldazin, 23 mM acetate buffer, pH 5.5, 30°C, 1 min. reaction time.
- LACU laccase unit
- LAMU Laccase Activity
- Laccase activity is determined from the oxidation of syringaldazin under aerobic conditions.
- the violet colour produced is photometered at 530 nm.
- the analytical conditions are 19 mM syringaldazin, 23 mM Tris/maleate buffer, pH 7.5, 30°C, 1 min. reaction time.
- LAMU laccase unit
- the present invention provides an enzymatic antimicrobial composition
- a phenol oxidizing enzyme system and an enhancing agent of a formula selected from group consisting of:
- the antimicrobial composition according to the invention may be formulated as a solid or a liquid.
- the composition When formulated as a liquid, the composition is typically an aqueous composition.
- the composition When formulated as a solid, the composition is typically a powder, a granulate, a paste or a gelled product.
- composition of the invention may further comprise auxiliary agents such as wetting agents, thickening agents, buffer, stabilisers, perfume, colourants, fillers and the like.
- Useful wetting agents are surfactants, i.e., non-ionic, anionic, amphoteric or zwitterionic surfactants.
- the composition of the invention may be a concentrated product or a ready-to- use product.
- the concentrated product is typically diluted with water to provide a medium having an effective antimicrobial activity, applied to the object to be disinfected or preserved, and allowed to react with the micro-organisms present.
- the optimum pH of such an aqueous composition is usually a compromise between the optimum stability and optimum activity of the enzyme in question.
- pH is in the range of pH 3 to 10.5 (such as pH 4 to 6 or pH 8 to 10), and in another aspect of the invention pH is in the range of pH 4 to 10, preferably pH 5 to 9, and more preferably pH 6 to 8.
- the present invention also provides a medical catheter comprising the composition of the invention.
- the present invention also provides a method for killing or inhibiting microbial cells comprising treating said microbial cells with the composition of the invention. Said treatment may be carried out with an effective amount of said composition.
- an “effective amount” is meant an amount suitable for obtaining the required antimicrobial effect in the chosen application; e.g. to reduce the number of living cells to 10%, 1% or less than 1%; or to prevent the number of living cells from doubling during 12 hours, 1 day, 5 days, 30 days or more than 30 days.
- the composition of the invention may be capable of reducing the number of living cells (killing) of E. coli (DSM1576) to less than 50% (preferably less than 75%, more preferably less than 90%, most preferably less than 95%, in particular at least 99%), when incubated 10 min. at 20°C in an aqueous solution containing 1 mg/L of the composition.
- the composition may also be capable of increasing the time before outgrowth (inhibition) of E. coli (DSM1576) at 25°C in a microbial growth substrate containing 1 mg/L of the composition by at least 5%, preferably at least 10%, more preferably at least 25%, most preferably at least 50%, and in particular at least 100%.
- composition of the invention may be incorporated into a detergent or cleaning composition typically comprising other enzyme types as well (see below).
- composition of the invention can also be used for inhibiting microorganisms present in laundry, by treating the laundry with a soaking, washing or rinsing liquor comprising an effective amount of the composition.
- composition used in the method of the present invention may be incorporated into e.g. water based paint, unprese ⁇ ted food, beverages, cosmetics, contact lens pro- ducts, food ingredients or anti-inflammatory product in an amount effective for killing or inhibiting growth of microbial cells.
- composition of the invention may be used as a preservation agent or a disinfection agent in water based paints (see below).
- composition according to the present invention may by useful as a disinfectant, e.g., in the treatment of acne, infections in the eye or the mouth, skin infections; in antiperspirants or deodorants; in foot bath salts; for cleaning and disinfection of contact lenses, hard surfaces, teeth (oral care), wounds, bruises and the like.
- a disinfectant e.g., in the treatment of acne, infections in the eye or the mouth, skin infections; in antiperspirants or deodorants; in foot bath salts; for cleaning and disinfection of contact lenses, hard surfaces, teeth (oral care), wounds, bruises and the like.
- composition of the present invention is useful for cleaning, disinfecting or inhibiting microbial growth on any hard surface.
- surfaces which may advantageously be contacted with the composition of the invention are surfaces of process equipment used, e.g., in dairies, chemical or pharmaceutical process plants, water sanitation systems, paper pulp processing plants, water treatment plants, and cooling towers.
- the composition of the invention may be used in an amount, which is effective for cleaning, disinfecting or inhibiting microbial growth on the surface in question.
- composition of the invention may be used for disinfecting and inhibiting microbial growth in paper and pulp processing plants.
- composition of the invention can advantageously be used in a cleaning-in-place (C.I.P.) system for cleaning of process equipment of any kind.
- C.I.P. cleaning-in-place
- the method of the invention may additionally be used for cleaning surfaces and cooking utensils in food processing plants and in any area in which food is prepared or served such as hospitals, nursing homes, restaurants, especially fast food restaurants, delicatessens and the like. It may also be used as an antimicrobial in food products and would be especially useful as a surface antimicrobial for cheese, fruits and vegetables and for food in salad bars.
- the composition of the present invention is also useful for microbial control of water lines, and for disinfection of water, in particular for disinfection of industrial water.
- composition of the present invention is also useful for treating medical catheters to kill or inhibit microbes present on the surface of said medical catheters.
- the composition of the invention can also be used for treating wounds.
- paint is construed as a substance comprising a solid coloring matter dissolved or dispersed in a liquid vehicle such as water, organic solvent and/or oils, which when spread over a surface, dries to leave a thin colored, decorative and/or protective coating.
- a liquid vehicle such as water, organic solvent and/or oils
- isothiazoliones such as 5-chlor-2-methyl-4-thia-zoli-3-on, has been added to the paint as biocides to inhibit/prevent microbial growth in the paint.
- the present invention provides a method for conservation of a paint comprising contacting said paint with a phenol oxidizing enzyme and an enhancing agent according to the invention. Further the invention provides a paint composition comprising a phenol oxidizing enzyme and an enhancing agent as described in the present invention.
- the paint is preferably a water based paint, i.e. the solids of the paint is dispersed in an aqueous solution.
- the paint may contain 0-20 % organic solvent, preferable 0-10%, e.g. 0-5%.
- the enzyme may be added to the paint in an amount of 0.0001-100 mg active enzyme protein per litre paint, preferably 0.001-10 mg/l, e.g. 0.01-5 mg/l, while the enhancing agent may be added in an amount of 10-500 ⁇ M, preferably 25-250 ⁇ M, e.g. 100 ⁇ M of the paint composition.
- the antimicrobial composition of the invention may be added to and thus become a component of a detergent composition.
- the detergent composition of the invention may for example be formulated as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre-treatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations.
- the invention provides a detergent additive comprising the antimicrobial composition of the invention.
- the detergent additive as well as the detergent composition may comprise one or more other enzymes such as a protease, a lipase, a cutinase, an amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase, e.g., a laccase, and/or a peroxidase.
- enzymes such as a protease, a lipase, a cutinase, an amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an
- the properties of the chosen enzyme(s) should be compatible with the selected detergent, (i.e. pH-optimum, compatibility with other enzymatic and non- enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
- proteases include those of animal, vegetable or microbial origin.
- the protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease.
- alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279).
- trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270 and WO 94/25583.
- Examples of useful proteases are the variants described in WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101 , 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274.
- Preferred commercially available protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, EsperaseTM, and KannaseTM (Novozymes A/S), MaxataseTM, MaxacaiTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
- Lipases Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (T.
- lanuginosus as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580
- a Pseudomonas lipase e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri (GB 1 ,372,034), P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), a Bacillus lipase, e.g.
- LipolaseTM and Lipo- lase UltraTM are preferred commercially available lipase enzymes.
- Amylases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, ⁇ -amylases obtained from Bacillus, e.g. a special strain of B. licheniformis, described in more detail in GB 1 ,296,839.
- amylases are the variants described in WO 94/02597, WO
- Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g.
- cellulases are the alkaline or neutral cellulases having colour care benefits.
- Examples of such cellulases are cellulases described in EP 0495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940.
- Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307 and PCT/DK98/00299.
- Peroxidases/Oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
- the detergent enzyme(s) may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all of these enzymes.
- a detergent additive of the invention i.e. a separate additive or a combined additive, can be formulated e.g. as a granulate, a liquid, a slurry, etc.
- Preferred detergent additive formulations are granulates, in particular non- dusting granulates, liquids, in particular stabilized liquids, or slurries.
- Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and 4,661,452 and may optionally be coated by methods known in the art.
- waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids.
- film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.
- Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods.
- Protected enzymes may be prepared according to the method disclosed in EP 238,216.
- the detergent composition of the invention may be in any convenient form, e.g., a bar, a tablet, a powder, a granule, a paste or a liquid.
- a liquid detergent may be aqueous, typically containing up to 70 % water and 0-30 % organic solvent, or non- aqueous.
- the detergent composition comprises one or more surfactants, which may be non-ionic including semi-polar and/or anionic and/or cationic and/or zwitterionic.
- the surfactants are typically present at a level of from 0.1 % to 60% by weight.
- the detergent When included therein the detergent will usually contain from about 1% to about 40% of an anionic surfactant such as linear alkylbenzenesulfonate, alpha- olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap.
- an anionic surfactant such as linear alkylbenzenesulfonate, alpha- olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap.
- the detergent When included therein the detergent will usually contain from about 0.2% to about 40% of a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl derivatives of glucosamine (“glucamides").
- a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl derivatives of glucosamine (“glucamides”).
- glucamides N-acyl N-alkyl derivatives of glucosamine
- the detergent may contain 0-65 % of a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst).
- a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst).
- the detergent may comprise one or more polymers.
- examples are carboxymethylcellulose, poly(vinylpyrrolidone), poly (ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid co- polymers.
- the detergent may contain a bleaching system, which may comprise a H2O2 source such as perborate or percarbonate, which may be combined with a peracid- forming bleach activator such as tetraacetylethylenediamine or nonanoyloxyben- zenesulfonate.
- a bleaching system may comprise peroxyacids of e.g. the amide, imide, or sulfone type.
- the enzyme(s) of the detergent composition of the invention may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708.
- the detergent may also contain other conventional detergent ingredients such as e.g.
- fabric conditioners including clays, foam boosters, suds suppressors, anti- corrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes.
- Table 1 Layout of master plate containing enhancing agent. Columns 1 and 2 contain 50mM HEPES buffer pH 7.0 and m1-m40 are numbered enhancing agents.
- Pseudomonas putida ATCC12633 was grown in a dilution series over night in LB medium and a late exponential culture was harvested by centrifugation (5 min @ 4000 RPM in a Microcentrifuge 154, Ole Dich, Denmark) and washed twice in 50 mM HEPES buffer pH 7.0. OD@490 was adjusted to 0.05 corresponding to approximately 10E5 cells/ml.
- Table 2 Layout of screenings plate. Only half of the 364 well plate is shown. Rows 3, 5, 7, 9, 11 contain enhancing agent only, whereas rows 4, 6, ⁇ , 10, 12 contain enhancing agent and laccase. Rows 1 and 2 are negative controls as well as a dilution series of cells are included in order to evaluate the amount of killing observed by the laccase / enhancing agent system. All assays were run in duplicate.
- LB Bouillon was from Merck, #0285. 25 g mix was added to 1000 ml water and then autoclaved.
- laccases used are described in: Myceliophthora thermophila (MtL) WO 95/33836 Rhizoctonia solani (RsL) WO 95/07986 Coprinus cinereus (CcL) WO 97/0 ⁇ 325 Polyporus pinsitus (PpL) WO 96/00290 - which is hereby incorporated by reference.
- Microtiter plates (96 well and 384 well plates) were obtained from Nalge Nunc International (Denmark). Enhancing agents were supplied as indicated in Table 3-6.
- Antimicrobial activity was determined on Pseudomonas putida (ATCC 12633), the cells were grown in Tryptone Soy Broth, TSB (Oxoid CM129) overnight, washed two times in sterile 0.9% saline and suspended in 50 mM HEPES buffer (Sigma H3375) at pH 7 to a cell concentration of approximately 10 6 CFU/ml.
- the mediators were added to the cell suspension to a final concentration of 50 ⁇ M, rCiP was added to the concentration 4 POXU/L and the enzyme reaction was started by addition of hydrogen peroxide to a final concentration of 0.5 mM.
- Antimicrobial activity was determined after 20 minutes incubation at 40°C, by a 10-fold dilution of the cell suspension into TSB substrate and incubation overnight. Antimicrobial activity was determined as logio reduction, thus a logio reduction of 2 corresponds to a kill of 99%.
Abstract
Description
Claims
Priority Applications (1)
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AU58223/01A AU5822301A (en) | 2000-05-08 | 2001-05-07 | Oxidoreductase mediated antimicrobial activity |
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DKPA200000755 | 2000-05-08 | ||
DKPA200000755 | 2000-05-08 |
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WO2001084937A1 true WO2001084937A1 (en) | 2001-11-15 |
WO2001084937A8 WO2001084937A8 (en) | 2001-12-13 |
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PCT/DK2001/000315 WO2001084937A1 (en) | 2000-05-08 | 2001-05-07 | Oxidoreductase mediated antimicrobial activity |
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WO (1) | WO2001084937A1 (en) |
Cited By (11)
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FR2826574A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
FR2826570A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
FR2826572A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
FR2826571A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
FR2826573A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
WO2003090542A1 (en) * | 2002-04-25 | 2003-11-06 | Novozymes A/S | Methods and compositions for killing spores |
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JP2008524243A (en) * | 2004-12-17 | 2008-07-10 | ザ・トラスティーズ・オブ・ザ・ユニバーシティ・オブ・ペンシルバニア | Stilbene derivatives and their use for binding and imaging amyloid plaques |
WO2010031408A2 (en) * | 2008-09-19 | 2010-03-25 | Aarhus Universitet | Gel compositions |
CN102219338A (en) * | 2011-04-15 | 2011-10-19 | 北京师范大学 | Method for removing organic contaminants in water through electrochemical oxidation and biological enzyme catalyzing |
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FR2826574A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
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FR2826572A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
FR2826571A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
FR2826573A1 (en) * | 2001-06-29 | 2003-01-03 | Oreal | COMPOSITIONS CONTAINING A HYDROXYDIPHENYL ETHER DERIVATIVE INHIBITING THE DEVELOPMENT OF BODY ODORS |
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WO2003002080A1 (en) * | 2001-06-29 | 2003-01-09 | L'oreal | Compositions containing a derivative of hydroxydiphenyl ether inhibiting the development of body odours |
WO2003090542A1 (en) * | 2002-04-25 | 2003-11-06 | Novozymes A/S | Methods and compositions for killing spores |
EP1623623A1 (en) * | 2003-05-13 | 2006-02-08 | Idemitsu Kosan Co., Ltd. | Antibacterial antiviral composition |
EP1623623A4 (en) * | 2003-05-13 | 2008-12-17 | Idemitsu Kosan Co | Antibacterial antiviral composition |
JP2008524243A (en) * | 2004-12-17 | 2008-07-10 | ザ・トラスティーズ・オブ・ザ・ユニバーシティ・オブ・ペンシルバニア | Stilbene derivatives and their use for binding and imaging amyloid plaques |
WO2010031408A2 (en) * | 2008-09-19 | 2010-03-25 | Aarhus Universitet | Gel compositions |
WO2010031408A3 (en) * | 2008-09-19 | 2010-07-22 | Aarhus Universitet | Gel compositions |
CN102219338A (en) * | 2011-04-15 | 2011-10-19 | 北京师范大学 | Method for removing organic contaminants in water through electrochemical oxidation and biological enzyme catalyzing |
CN106471112A (en) * | 2014-05-06 | 2017-03-01 | 美利肯公司 | Laundry care composition |
EP3140384A1 (en) * | 2014-05-06 | 2017-03-15 | Milliken & Company | Laundry care compositions |
US11530374B2 (en) | 2014-05-06 | 2022-12-20 | Milliken & Company | Laundry care compositions |
EP3140384B1 (en) * | 2014-05-06 | 2024-02-14 | Milliken & Company | Laundry care compositions |
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WO2001084937A8 (en) | 2001-12-13 |
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