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WO2003090797A1 - Compositions deodorantes - Google Patents

Compositions deodorantes Download PDF

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Publication number
WO2003090797A1
WO2003090797A1 PCT/DK2003/000270 DK0300270W WO03090797A1 WO 2003090797 A1 WO2003090797 A1 WO 2003090797A1 DK 0300270 W DK0300270 W DK 0300270W WO 03090797 A1 WO03090797 A1 WO 03090797A1
Authority
WO
WIPO (PCT)
Prior art keywords
laccase
locus
composition
enzyme
plant material
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.)
Ceased
Application number
PCT/DK2003/000270
Other languages
English (en)
Inventor
Kyoko Abe
Naoto Uyama
Hiromichi Sakaguchi
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novozymes AS
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Novozymes AS filed Critical Novozymes AS
Priority to US10/512,223 priority Critical patent/US20050147573A1/en
Priority to AU2003223922A priority patent/AU2003223922A1/en
Publication of WO2003090797A1 publication Critical patent/WO2003090797A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • 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
    • A61L9/00—Disinfection, sterilisation or deodorisation of air
    • A61L9/01—Deodorant 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
    • A61L9/00—Disinfection, sterilisation or deodorisation of air
    • A61L9/01—Deodorant compositions
    • A61L9/013—Deodorant compositions containing animal or plant extracts, or vegetable material

Definitions

  • the present invention relates to enzymatic methods and compositions capable of reducing odors from human, animal and industrial sources.
  • Various environmental odors are part of our daily life, such as refrigerator odors and odors from pets and domestic animals. Because some of these odors are unpleasant to humans, a wide variety of approaches have been proposed to eliminate these odors.
  • One such conventional deodorizing method is to adsorb the substance causing the offensive odor.
  • Activated carbon is an example of such an adsorbent.
  • the present invention provides such an alternative.
  • the present invention provides a deodorant composition
  • a deodorant composition comprising an enzymatic agent, an oxidizing agent, and shredded, sliced or crushed plant material which naturally contains one or more phenolic compounds.
  • the invention provides a method of reducing odor from a locus, comprising contacting the locus with the composition of the invention.
  • odor is intended to mean a bad smell as perceived by an average human being.
  • odorant means a substance yielding a bad smell (odor).
  • An odorant precursor is a substance which may be transformed into an odorant by e.g. biochemical reactions.
  • deodorant means a substance, which is capable of reducing odor.
  • the enzymatic agent of the invention comprises a phenol oxidizing enzyme and an oxidizing agent.
  • the enzymatic agent further comprises one or more other enzymatic activities, such as proteases, lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases and/or xylanases.
  • the phenol oxidizing enzyme is an enzyme or a compound exhibiting phenol oxidizing activity.
  • the phenol oxidizing enzyme may be a peroxidase or a compound exhibiting peroxidase activity, a laccase or a compound exhibiting laccase activity, a catechol oxidase (EC 1.10.3.1), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
  • the phenol oxidizing enzyme of the invention may typically be present in concentrations of from 1 to 10000 microgram enzyme protein per liter aqueous solution, preferably of from 5 to 2000 microgram enzyme protein per liter aqueous solution, more preferably of from 5 to 1000 microgram enzyme protein per liter aqueous solution, and most preferably of from 1 to 500 microgram enzyme protein per liter aqueous solution.
  • phenol oxidizing enzyme variants e.g. produced by recombinant techniques are included within the meaning of the term "phenol oxidizing enzyme”.
  • Compounds exhibiting laccase activity may be any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom, exhibiting laccase activity.
  • Preferred laccase enzymes and/or compounds exhibiting laccase activity are enzyr ies of microbial origin.
  • the enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts).
  • 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 7. versicolor, Rhizoctonia, e.g., R. solani, Cop nus, e.g., C. cinereus, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P.
  • papilionaceus Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radita (WO 92/01046), or 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, Scytalidium or Rhizoctonia is preferred; in particular a laccase derived from Coprinus cinereus, Myceliophthora thermophila, Polyporus pinsitus, 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.
  • LACU Laccase Activity
  • Laccase activity (particularly suitable for Polyporus laccases) may be 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 may be determined from the oxidation of syringaldazin under aerobic conditions.
  • the violet colour produced is measured 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
  • Compounds exhibiting 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.
  • compounds exhibiting peroxidase activity comprise peroxidase enzymes and peroxidase active fragments derived from cytochromes, haemoglobin or peroxidase enzymes.
  • the peroxidase employed in the composition of the invention is producible by plants (e.g. horseradish or soybean peroxidase) or microorganisms such as fungi or bacteria.
  • Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hyphomycetes, e.g., Fusarium, Humicola, T choderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma res/7, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia alii or Dreschlera
  • fungi include strains belonging to the subdivision Basidiomycotina, class Basidiomycetes, e.g., Coprinus, Phanerochaete, Coriolus or Trametes, in particular 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.
  • 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.
  • Bacillus pumilus ATCC 12905
  • Bacillus stearothermophilus Rhodobacter sphaeroides
  • Rhodomonas palustri Streptococcus lactis
  • Pseudomonas purrocinia ATCC 15958
  • Pseudomonas fluorescens NRRL B-11 .
  • Further preferred 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.
  • POXU peroxidase unit
  • ABTS 2,2'-azino-bis(3- ethylbenzothiazoline-6-sulfonate)
  • the phenol oxidizing enzyme requires a source of hydrogen peroxide as an oxidizing agent to exhibit phenol oxidizing activity (e.g. peroxidase activity)
  • the source may be hydrogen peroxide or a hydrogen peroxide precursor for in situ production of hydrogen peroxide. Any solid entity which liberates upon dissolution a peroxide which is useable by the phenol oxidizing enzyme can serve as the source of hydrogen peroxide.
  • Compounds which yield hydrogen peroxide upon dissolution in water or an appropriate aqueous based medium include but are not limited to metal peroxides, percarbonates, persulphates, perphosphates, peroxyacids, alkyperoxides, acylperoxides, peroxyesters, urea peroxide, perborates and peroxycarboxylic acids or salts thereof.
  • Any compound which generates a peroxide that the phenol oxidizing enzyme can use to exhibit phenol oxidizing activity is an acceptable source of hydrogen peroxide for this invention; this includes a large number of compounds as one skilled in the art will recognize. Mixtures of two or more of these substances can also be used.
  • Another source of hydrogen peroxide is a hydrogen peroxide generating enzyme system, such as an oxidase together with a substrate for the oxidase.
  • oxidase and substrate comprise, but are not limited to, amino acid oxidase (see e.g. US 6,248,575) and a suitable amino acid, glucose oxidase (see e.g. WO 95/29996) and glucose, lactate oxidase and lactate, galactose oxidase (see e.g. WO 00/50606) and galactose, and aldose oxidase (see e.g. WO 99/31990) and a suitable aldose.
  • the source of 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 mM to 25 mM, preferably to levels of from 0.005 mM to 5 mM, and particularly to levels of from 0.01 to 1 mM.
  • the source of oxygen may be oxygen from the atmosphere or an oxygen precursor for in situ production of oxygen. Oxygen from the atmosphere will usually be present in sufficient quantity. If more O 2 is needed, additional oxygen may be added, e.g. as pressurized atmospheric air or as pure pressurized O 2 .
  • Plant material in the context of the present invention is any shredded, sliced, cut or crushed plant items.
  • the plant material may be provided on the basis of frozen materials, heat treated materials (such as tea or coffee residues), fresh materials, fermented materials, or provided in any other form known in the art.
  • the extract may contain the plant material, e.g. the plant material may be mashed, pulped or homogenized.
  • the plant material may be obtainable from e.g. fruits, vegetables, cereals, leaves, wood or any other plant items.
  • Useful fruits comprise, but are not limited to, pomes and seed fruits (apples, pears, etc.), grapes, tomatoes, citrus (orange, lemon, lime, mandarin), prunes, cherries, black currants, red currants, raspberries, strawberries, cranberries, pineapple, and any other tropical fruit.
  • Useful vegetables comprise, but are not limited to, potatoes, carrots, celery, and onions.
  • Useful cereals comprise, but are not limited to, wheat and maize.
  • Useful leaves comprise, but are not limited to, tea leaves (e.g. green tea leaves). The tea leaves may be residues from a tea brewing process.
  • the plant material may also comprise a mixture of plant items from the same plant, or more than one plant material from different plants.
  • the plant material may have been extracted with hot water, such as a tea leaf residue.
  • Hot water means water with a temperature in the range of 60-120 degrees Celsius, preferably in the range of 70-110 degrees Celsius, more preferable in the range of 80-100 degrees
  • the plant material of the invention naturally contains one or more phenolic compounds.
  • phenolic compounds include, but are not limited to, lignin, lignosulfonic acid, humic acid, nitrohumic acid, tannin, catechin, gallic acid, urishiol, hesperidin, guaiachol, 4-methyl-guaiachol, 4-ethyl-guaiachol hinokitiol.
  • compositions comprising:
  • an enzymatic agent comprising a phenol oxidizing enzyme and an oxidizing agent; and - shredded, sliced or crushed plant material which naturally contains one or more phenolic compounds.
  • the deodorant composition may be formulated in the form of a slurry, a suspension, a paste, a solid or a dry product formulation.
  • the dry product formulation may subsequently be re-hydrated to form an active composition usable in the method of the invention.
  • composition When the composition is formulated as a dry formulation, the components may be mixed, arranged in discrete layers or packaged separately.
  • all components may be mixed together, e.g. as a powder.
  • 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, amphotehc 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 odor reducing activity, applied to the locus to be deodorized, and allowed to react with the odorants or odorant precursors present.
  • the present invention provides a method of reducing odor from a locus, comprising contacting the locus with: - an enzymatic agent comprising a phenol oxidizing enzyme and an oxidizing agent; and - shredded, sliced or crushed plant material which naturally contains one or more phenolic compounds.
  • the locus may be contacted with the composition of the invention by immersing the locus in an aqueous formulation of the composition (e.g. a suspension), by spraying the locus with the composition, by coating the locus with the composition using e.g. a cloth, a brush, a shovel, or the like.
  • the composition may also be mixed with objects containing odorants.
  • the locus is contacted with the composition in such a way that the odorants of the locus can react with the composition. Any method of applying the composition to a locus, which results in reducing the odor from the locus, is an acceptable method of application. The skilled person will easily recognize such methods.
  • the locus is contacted with the composition at between 5 and 80 degrees Celsius, preferably between 10 and 50 degrees Celsius, more preferably between 15 and 40 degrees Celsius, and most preferably at room temperature.
  • the locus is contacted with the composition at between pH 2 and pH 10, preferably at between pH 3.5 and pH 9, more preferably between pH 5 and pH 9.
  • the phenol oxidizing enzyme and the oxidizing agent are a laccase and a source of oxygen, or a peroxidase and a source of hydrogen peroxide.
  • the method of the invention may be capable of reducing the odor from a locus to less than 80% (preferably less than 50%, more preferably less than 30%, most preferably less than 20%, and in particular less than 10%) after 2 days at 20 degrees Celsius and 60-90% relative humidity, compared to an identical surface which has not been subjected to the method of the invention.
  • Evaluation of odor Odor may be evaluated by a trained sensory panel of at least 5 persons.
  • the odor intensity is indicated on a scale from 0 to 10 where 0 equals 'no odor' and 10 equals 'very strong odor'. All evaluations are performed twice, and average values are calculated.
  • bad smelling compounds are often volatile compounds, such as methyl mercaptan
  • traditional analysis methods such as gas chromatography and gas detection tubes, may be used to detect and quantify these compounds.
  • Chemicals used as buffers and substrates were commercial products of at least reagent grade.
  • Enzyme Myceliophthora thermophila laccase, activity: 276 LAMU/g (disclosed in patent application WO9533836 and available from Novozymes A S, Denmark).
  • Tea Green Tea (dry form), brand name "maccha iri ryokucha” (ITO EN, Ltd., Japan).
  • Gas sampling pump kit GV-100S (Gastec Corporation)
  • Gas detection tube No. 71 H, methyl mercaptan (Gastec Corporation)
  • Methyl mercaptan, sodium salt, approx. 15% in water was diluted with water in a ratio of 1 :100.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Epidemiology (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Botany (AREA)
  • Zoology (AREA)
  • Cosmetics (AREA)
  • Disinfection, Sterilisation Or Deodorisation Of Air (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

La présente invention concerne des procédés et des compositions permettant de réduire l'odeur d'un site par mise en contact du site avec un agent enzymatique, un agent oxydant et un matériau végétal écrasé, tranché ou déchiqueté contenant naturellement un ou plusieurs composés phénoliques.
PCT/DK2003/000270 2002-04-24 2003-04-24 Compositions deodorantes Ceased WO2003090797A1 (fr)

Priority Applications (2)

Application Number Priority Date Filing Date Title
US10/512,223 US20050147573A1 (en) 2003-04-24 2003-04-24 Deodorant compositions
AU2003223922A AU2003223922A1 (en) 2002-04-24 2003-04-24 Deodorant compositions

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DKPA200200613 2002-04-24
DKPA200200613 2002-04-24

Publications (1)

Publication Number Publication Date
WO2003090797A1 true WO2003090797A1 (fr) 2003-11-06

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ID=29265858

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Application Number Title Priority Date Filing Date
PCT/DK2003/000270 Ceased WO2003090797A1 (fr) 2002-04-24 2003-04-24 Compositions deodorantes

Country Status (3)

Country Link
CN (1) CN1662264A (fr)
AU (1) AU2003223922A1 (fr)
WO (1) WO2003090797A1 (fr)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20130085270A1 (en) * 2010-06-09 2013-04-04 Kao Corporation Manufacturing method for polyphenol composition
CN108611331A (zh) * 2018-05-10 2018-10-02 中国科学院过程工程研究所 一种茶叶全生物量综合利用的方法

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2196208A4 (fr) * 2007-09-26 2010-09-22 Takasago Perfumery Co Ltd Extrait végétal et son utilisation
CN112156645B (zh) * 2020-09-23 2021-04-27 柳州市宝净科技有限公司 一种复合生物酶除臭剂及其制备方法

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5804170A (en) * 1995-07-31 1998-09-08 Takasago Koryo Kogyo Kabushiki Kaisha (Takasago International Corporation) Deodorant composition
EP1064956A2 (fr) * 1999-06-24 2001-01-03 Takasago International Corporation Articles hygiéniques désodorisants
US6294161B1 (en) * 1997-01-30 2001-09-25 Takasago International Corporation Deodorant composition

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5804170A (en) * 1995-07-31 1998-09-08 Takasago Koryo Kogyo Kabushiki Kaisha (Takasago International Corporation) Deodorant composition
US6294161B1 (en) * 1997-01-30 2001-09-25 Takasago International Corporation Deodorant composition
EP1064956A2 (fr) * 1999-06-24 2001-01-03 Takasago International Corporation Articles hygiéniques désodorisants

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20130085270A1 (en) * 2010-06-09 2013-04-04 Kao Corporation Manufacturing method for polyphenol composition
US9079933B2 (en) * 2010-06-09 2015-07-14 Kao Corporation Manufacturing method for polyphenol composition
US9688712B2 (en) 2010-06-09 2017-06-27 Kao Corporation Manufacturing method for polyphenol composition
CN108611331A (zh) * 2018-05-10 2018-10-02 中国科学院过程工程研究所 一种茶叶全生物量综合利用的方法
CN108611331B (zh) * 2018-05-10 2021-07-20 中国科学院过程工程研究所 一种茶叶全生物量综合利用的方法

Also Published As

Publication number Publication date
CN1662264A (zh) 2005-08-31
AU2003223922A1 (en) 2003-11-10

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