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WO2000016740A1 - Compositions pour soins d'hygiene personnelle contenant les enzymes subtilisine liees a des substrats insolubles dans l'eau - Google Patents

Compositions pour soins d'hygiene personnelle contenant les enzymes subtilisine liees a des substrats insolubles dans l'eau Download PDF

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Publication number
WO2000016740A1
WO2000016740A1 PCT/US1999/021062 US9921062W WO0016740A1 WO 2000016740 A1 WO2000016740 A1 WO 2000016740A1 US 9921062 W US9921062 W US 9921062W WO 0016740 A1 WO0016740 A1 WO 0016740A1
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WO
WIPO (PCT)
Prior art keywords
personal care
substrate
composition according
wipe composition
enzymes
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/US1999/021062
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English (en)
Inventor
David John Weisgerber
Andrew Campbell Allcock
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Procter and Gamble Co
Original Assignee
Procter and Gamble Co
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Filing date
Publication date
Application filed by Procter and Gamble Co filed Critical Procter and Gamble Co
Priority to EP99969327A priority Critical patent/EP1115376A1/fr
Priority to JP2000573701A priority patent/JP2002526434A/ja
Priority to CA002345127A priority patent/CA2345127A1/fr
Priority to AU60388/99A priority patent/AU743760B2/en
Priority to KR1020017003665A priority patent/KR20010075285A/ko
Priority to BR9914026-8A priority patent/BR9914026A/pt
Publication of WO2000016740A1 publication Critical patent/WO2000016740A1/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
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/02—Cosmetics or similar toiletry preparations characterised by special physical form
    • A61K8/0208—Tissues; Wipes; Patches
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/02—Cosmetics or similar toiletry preparations characterised by special physical form
    • A61K8/0212—Face masks
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/65—Collagen; Gelatin; Keratin; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/66—Enzymes
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/72—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds
    • A61K8/73—Polysaccharides
    • A61K8/731—Cellulose; Quaternized cellulose derivatives
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/72—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds
    • A61K8/81—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds obtained by reactions involving only carbon-to-carbon unsaturated bonds
    • A61K8/817—Compositions of homopolymers or copolymers of compounds having one or more unsaturated aliphatic radicals, each having only one carbon-to-carbon double bond, and at least one being terminated by a single or double bond to nitrogen or by a heterocyclic ring containing nitrogen; Compositions or derivatives of such polymers, e.g. vinylimidazol, vinylcaprolactame, allylamines (Polyquaternium 6)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A61Q19/10—Washing or bathing preparations
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
    • A61K2800/57—Compounds covalently linked to a(n inert) carrier molecule, e.g. conjugates, pro-fragrances
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/80—Process related aspects concerning the preparation of the cosmetic composition or the storage or application thereof
    • A61K2800/94—Involves covalent bonding to the substrate

Definitions

  • the present invention relates to personal care compositions compnsing singularly substituted subti sin enzymes bound to the wipe substrate
  • Embodiments of the personal care compositions include a personal care wipe and a personal care skm mask.
  • the compositions provide improved cleansing and skin conditioning due to the activity of the active proteins, with minimized risk of allergic reaction to the active protein by the user.
  • Enzymes are proteins which react with a compound, or substrate, to break down that compound. Enzymes are divided into numerous classes based on the class of substrate they react upon. Each class of enzyme generally catalyzes the severing of different chemical bonds resulting in the specific selection of activity.
  • the hpase class of enzymes are known for their ability to hydrolyze ester bonds created between, but not limited to, hydrocarbons and polyalcohol backbone substrates. Examples of these substrates are mono-, di-, and triglycende polyglycerol esters.
  • the protease class of enzymes are known for their ability to hydrolyze proteins.
  • Naturally occurring and bio- engmeered protease enzymes are incorporated into household cleaning detergents to hydrolyze protemaceous dirt and stains, into personal care products to remove dirt and dead skin, into oral cleansing products to facilitate plaque removal in the mouth, and into medicines to affect undesired proteins m the body.
  • allergic responses to active proteins can be minimized by limiting the selection of those proteins used in products to those of human origin. While this approach minimizes allergenicity problems, it is not a complete solution since it is often not possible to find such an active protein which also has the activity properties desired.
  • a third proposition for decreasing allergenicity is through epitope mapping and alteration of the protein amino acid sequence to deliver a protein with reduced allergenicity This approach usually requires a large investment of development time and money.
  • the U. S. Patent Application, Serial Number 08/903,298 discloses the use of enzymes modified by the addition of twin polyethylene glycol polymer moieties to reduce allergenicity while delivering high enzymatic activity.
  • the modified enzyme therein is used in combination with a fibrous substrate m a wipe application.
  • the modified enzymes are not attached to the substrate. Reduced allergenicty is achieved via the modification of the enzyme.
  • U. S. Patent Application, Serial Number 09/088,912 disclosed polyme ⁇ c chemical modification of subtilism enzymes at one or more of three specific epitope regions which was found to mask the lmmunogenic determinants of the enzyme. Another approach to reduce the allergenicity of active proteins has been by granulating, coating or dissolving the active proteins to avoid their becoming airborne.
  • U.S. Patent 4,556,554 (Calvo) discloses cosmetic compositions which comp ⁇ se enzymes which have been immobilized by attachment to particles of polyme ⁇ c support. The particles with attached enzymes are dispersed in the cosmetic vehicle Upon application of the vehicle to the skm, the enzyme is released from the support and is therefore reactivated. Methods such as this address consumer exposure to airborne proteins, however they still leave the substantial nsks associated with extended tissue contact with the released enzyme which are deposited on the skin.
  • the present invention relates to personal care compositions compnsing a water insoluble substrate, a plurality of singularly substituted subtilism BPN' enzyme va ⁇ ants and a binding means, permanently attaching each of the enzymes to the substrate, wherein the personal care compositions comprise from about 0.01 ⁇ g/cm 2 to about 1000 ⁇ g/cm 2 of the enzyme on the substrate.
  • compositions of the present invention comprise subtilism BPN' enzymes and de ⁇ vatives modified by a single substitution of a cysteine ammo acid group permanently bound to a water insoluble substrate.
  • the compositions provide a convenient means to utilize the specialized activity of subtilism BPN' enzyme and its de ⁇ vatives, where the enzymes are bound to the substrate, thereby minimizing any risk of allergic reaction.
  • Preferred embodiments of the compositions are highly efficacious for cleaning sweat, sebum, dead skm cells, fats and oils from the skin and for moisturizing of the skm.
  • the enzymes may be brought into contact with the skm for use, allowing them to act on the surface Then as the wipe or mask is removed all of the enzymes are lifted from the skm surface, and removed and disposed of with the used wipe, thereby eliminating the risk of aeroso zation and extended dermal exposure.
  • the active protein reacts with the compounds it has specific reactivity for while in contact with the skin and none remain on the skm after use to stimulate the immune system and subsequently form antibodies responsible for allergic reaction
  • amino acid sequence refers to a specific configuration of the amino acids comprising a protein
  • amino acids comprising a protein
  • mutation refers to the genetic alteration of an organism, which in turn alters the amino acid sequence of the enzyme produced by that organism.
  • the mutation of an organism has been often found to alter the properties of the enzyme.
  • wild-type refers to an enzyme produced by unmutated hosts.
  • variant means an enzyme having an ammo acid sequence which differs from that of the wild-type enzyme due to the genetic mutation of the host producing that enzyme.
  • the products of the present invention comprise a water insoluble substrate.
  • water insoluble is meant that the substrate does not dissolve m or readily break apart upon immersion in water.
  • the water insoluble substrate is the implement or vehicle for delivering the active proteins of the present invention to the skin to be cleansed and moisturized, and for removing substantially all of the proteins from the skm.
  • a wide variety of materials can be used as the substrate.
  • the following nonlimitmg characteristics are desirable- (i) sufficient wet strength for use, (n) sufficient abrasivity, (in) sufficient loft and porosity, (IV) sufficient thickness, and (v) approp ⁇ ate size.
  • Nonlimitmg examples of suitable insoluble substrates which meet the above criteria include nonwoven substrates, woven substrates, hydroentangled substrates, air entangled substrates, natural sponges, synthetic sponges, polyme ⁇ c netted meshes, and the like
  • Preferred embodiments employ nonwoven substrates since they are economical and readily available m a variety of materials
  • nonwoven is meant that the layer is comprised of fibers which are not woven into a fabnc but rather are formed into a sheet, mat, or pad layer
  • the fibers can either be random (1 e., randomly aligned) or they can be carded (1 e combed to be oriented m primarily one direction).
  • the nonwoven substrate can be composed of a combination of layers of random and carded fibers.
  • Nonwoven substrates may be comprised of a va ⁇ ety of mate ⁇ als both natural and synthetic.
  • natural is meant that the materials are derived from plants, animals, insects or byproducts of plants, animals, and insects
  • synthetic is meant that the materials are obtained primarily from various man-made materials or from natural materials which have been further altered
  • the conventional base starting material is usually a fibrous web compnsing any of the common synthetic or natural textile-length fibers, or mixtures thereof.
  • Nonlimitmg examples of natural mate ⁇ als useful in the present invention are silk fibers, keratin fibers and cellulosic fibers.
  • Nonlimitmg examples of keratin fibers include those selected from the group consisting of wool fibers, camel hair fibers, and the like.
  • Nonlimitmg examples of cellulosic fibers include those selected from the group consisting of wood pulp fibers, cotton fibers, hemp fibers, jute fibers, flax fibers, and mixtures thereof.
  • Nonlimitmg examples of synthetic mate ⁇ als useful in the present invention include those selected from the group consisting of acetate fibers, acrylic fibers, cellulose ester fibers, modacryhc fibers, polyamide fibers, polyester fibers, polyolefin fibers, polyvmyl alcohol fibers, rayon fibers, polyurethane foam, and mixtures thereof.
  • acrylics such as ac ⁇ lan, creslan, and the acrylonit ⁇ le-based fiber, orlon
  • cellulose ester fibers such as cellulose acetate, amel, and accelerator
  • polyamides such as nylons (e.g., nylon 6, nylon 66, nylon 610, and the like)
  • polyesters such as fortrel, kodel, and the polyethylene terephthalate fiber, dacron
  • polyolefins such as polypropylene, polyethylene
  • polyvmyl acetate fibers polyurethane foams and mixtures thereof.
  • Nonwoven substrates made from natural materials consist of webs or sheets most commonly formed on a fine wire screen from a liquid suspension of the fibers. See C A Hampel et al., The Encyclopedia of Chemistry, third edition, 1973, pp 793-795 (1973); The Encyclopedia Americana, vol 21, pp 376-383 (1984), and G.A. Smook, Handbook of Pulp and Paper Technologies, Technical Association for the Pulp and Paper Industry (1986), which are incorporated by reference herein in their entirety.
  • Substrates made from natural materials useful the present invention can be obtained from a wide variety of commercial sources
  • suitable commercially available paper layers useful herein include Airtex®, an embossed airlaid cellulosic layer having a base weight of about 71 gsy, available from James River, Green Bay, WI, and Walkisoft®, an embossed airlaid cellulosic having a base weight of about 75 gsy, available from Walkisoft U.S.A., Mount Holly, NC.
  • nonwoven substrates are well known m the art.
  • these nonwoven substrates can be made by air-laymg, water-laying, meltblowmg, coforming, spunbondmg, or carding processes in which the fibers or filaments are first cut to desired lengths from long strands, passed into a water or air stream, and then deposited onto a screen through which the fiber-laden air or water is passed.
  • the resulting layer regardless of its method of production or composition, is then subjected to at least one of several types of bonding operations to anchor the individual fibers together to form a self-sustaining web.
  • the nonwoven layer can be prepared by a vanety of processes including hydroentanglement, thermally bonding or thermo-bonding, and combinations of these processes.
  • the substrates of the present invention can consist of a single layer or multiple layers.
  • a multilayered substrate can include films and other nonf ⁇ brous mate ⁇ als.
  • Nonwoven substrates made from synthetic mate ⁇ als useful in the present invention can also be obtained from a wide variety of commercial sources.
  • suitable nonwoven layer materials useful herein include HEF 40-047, an apertured hydroentangled material containing about 50% rayon and 50% polyester, and having a basis weight of about 43 grams per square yard (gsy), available from Veratec, Inc., Walpole, MA; HEF 140-102, an apertured hydroentangled material containing about 50% rayon and 50% polyester, and having a basis weight of about 56 gsy, available from Veratec, Inc., Walpole, MA; Novonet® 149-616, a thermo-bonded grid patterned material containing about 100% polypropylene, and having a basis weight of about 50 gsy, available from Veratec, Inc., Walpole, MA; Novonet® 149-801, a thermo-bonded grid patterned material containing about 69% rayon, about 25% polypropylene, and about 6% cotton, and having a basis weight of about 75 gsy,
  • Walpole, MA Novonet® 149-191 , a thermo-bonded grid patterned material containing about 69% rayon, about 25% polypropylene, and about 6% cotton, and having a basis weight of about 100 gsy, available from Veratec, Inc. Walpole, MA; HEF Nubtex® 149-801, a nubbed, apertured hydroentangled material, containing about 100% polyester, and having a basis weight of about 70 gsy, available from Veratec, Inc.
  • the water insoluble substrate can be a polyme ⁇ c mesh sponge as desc ⁇ bed in European Patent No. EP 702550 Al published March 27, 1996, incorporated by reference herein in its entirety.
  • the polymeric sponge comprises a plurality of plies of an extruded tubular netting mesh prepared from a strong flexible polymer, such as addition polymers of olefin monomers and polyamides of polycarboxyhc acids. Although these polymeric sponges are designed to be used in conjunction with a liquid cleanser, these types of sponges can be used as the water insoluble substrate in the present invention.
  • the substrate can be made into a wide variety of shapes and forms including flat pads, thick pads, thm sheets, ball-shaped implements, irregularly shaped implements, and having sizes ranging from a surface area of about a square inch to about hundreds of square inches.
  • the exact size will depend upon the desired use and product characteristics Especially convenient are square, circular, rectangular, or oval pads having a surface area of from about 1 m 2 to about 144 m 2 , preferably from about 10 2 to about 120 in 2 , and more preferably from about 30 m 2 to about 80 in 2 , and a thickness of from about 1 mil to about 500 mil, preferably from about 5 mil to about 250 mil, and more preferably from about 10 mil to about 100 mil.
  • the water insoluble substrates of the present invention can comprise two or more layers, each having different textures and abrasiveness.
  • the differing textures can result from the use of different combinations of mate ⁇ als or from the use of different manufacturing processes or a combination thereof.
  • a dual textured substrate can be made to provide the advantage of having a more abrasive side for exfoliation and a softer, absorbent side for gentle cleansing
  • separate layers of the substrate can be manufactured to have different colors, thereby helping the user to further distinguish the surfaces.
  • An essential component of the present invention is a plurality of singularly substituted subtilism BPN' enzymes (hereinafter referred to as Protease G).
  • the Protease G is present on the surface of the water insoluble substrate at a level ranging from about 0.01 ⁇ g/cm 2 to about 1000 ⁇ g/cm 2 , preferably from about 0.05 ⁇ g/cm 2 to about 100 ⁇ g/cm 2 , and most preferably from about 0.1 ⁇ g/cm 2 to about 10 ⁇ g/cm 2 .
  • protease enzymes are classified under the Enzyme Classification number E.C 3 4 (Carboxy c Ester Hydrolases) in accordance with the Recommendations (1992) of the International Union of Biochemistry and Molecular Biology (IUBMB).
  • E.C 3 4 Carboxy c Ester Hydrolases
  • Related proteases are also described in PCT publications: WO 95/30010 published November 9, 1995 by The Procter & Gamble Company; WO 95/30011 published November 9, 1995 by The Procter & Gamble Company; WO 95/29979 published November 9, 1995 by The Procter & Gamble Company.
  • Subtilism enzymes are protease enzymes which are naturally produced by Bacillus alcalophilus, Bacillus amyloliquefaciens , Bacillus amylosaccharicus, Bacillus hcheniformis , Bacillus lentus and Bacillus subtihs microorganisms.
  • Bacillus alcalophilus Bacillus amyloliquefaciens
  • Bacillus amylosaccharicus Bacillus hcheniformis
  • Bacillus lentus Bacillus subtihs microorganisms.
  • subtilism enzyme is BPN'.
  • the wild-type BPN' from Bacillus amyloliquefaciens is characte ⁇ zed by the ammo acid sequence:
  • Protease B Additional va ⁇ ants of BPN', heretoforth referred to as "Protease B", are disclosed by Genencor International, Inc. (San Francisco, California) European Patent EP-B-251,446 (granted December 28, 1994 and published January 7, 1988) as characte ⁇ zed by the wild-type BPN' amino acid with the mutations in one or more of the following ammo acids.
  • protease D Another BPN' va ⁇ ant protease, hereafter referred to as "Protease D" is desc ⁇ bed m WO 95/10615 published Ap ⁇ l 20, 1995 by Genencor International as characterized by the wild-type BPN' ammo acid with mutation to position Asn76, in combination with mutations in one or more other ammo acid positions selected from the group consisting of Asp99, Ser 101, Gin 103, Tyr 104, Serl05, Ilel07, Asnl09, Asnl23, Leul26, Glyl27, Glyl28, Leul35, Glul56, Glyl66, Glul95, Aspl97, Ser204, Gln206, Pro210, Ala216, Tyr217, Asn218, Met222, Ser260, Lys265, and/or Ala274
  • Protease F Another BPN' va ⁇ ant protease, hereafter referred to as "Protease F" is described U.S. Patent Number 4,760,025, issued to Estell, et al. on July 26, 1988 as characterized by the wild- type BPN' amino acid with mutation to one or more ammo acid positions selected from the group consisting of Asp32, Ser33, H ⁇ s64, Tyrl04, Asnl55, Glul56, Glyl66, Glyl69, Phel89, Tyr217, and Met222.
  • the enzyme used in the personal care compositions of the present invention comprises any of the BPN' enzymes and their vanants listed above with a singular substitution or insertion of a cysteine amino acid in the amino acid sequence.
  • Cysteine is the most preferred substituting amino acid for substitution in the desired epitope region since it does not occur in wild-type subtilism BPN' or its derivatives.
  • the substituted or inserted amino acid provides a moiety suitable for attachment to the substrate of the present invention at a specific site within the enzyme.
  • the substitution or insertion should be made at a position in an epitope region which falls at a point in the protein away from the active site of the protein.
  • this active site is spacially defined by the tnad Asn32, H ⁇ s64, and Ser 221.
  • a cysteine is substituted at a point away from that triad.
  • Preferable epitope regions for substitution are the of Aspl40-Vall50 and Ala230-Leu250 region Non-limiting examples of possible cysteine substitutions at either Serl45, Asn 240 or Ser249. Cysteine is the most preferred substituting amino acid for substitution in the desired epitope region since it does not occur in wild-type subtilism BPN' or its de ⁇ vatives.
  • binding means include any physical or chemical method of permanently binding an active protein to a substrate. Many such means are known in the art.
  • Physical Entrapment One means of binding the active protein of the present invention to the substrate is to physically trap the protein within the body of the substrate.
  • a preferred means of entrapment is to seal the protein in a coating on the surface of the substrate. Any adhesive or polymeric known m the art may be used to seal the protein to the substrate.
  • a preferred coating is poly-2- hydroxyethyl acrylate which is formed by the separate application of 2-hydroxyethyl acrylate monomer and an iron (II) sulfate heptahydrate initiator.
  • a solution of either a) active protein and adhesive or b) active protein and a monomer/mitiator combination is uniformly sprayed onto the surface of the substrate A second coating of adhesive or monomer/mitiator or a separate initiator may be required to achieve sufficient binding.
  • the substrate is then dried to allow the polymer to set.
  • the substrate is then fully rinsed to remove any free protein. Protein Tethered to Polymeric Gel Coating on Substrate
  • the protein may be bound to the substrate by a chemical tether bound to a polyme ⁇ c coating on the substrate.
  • the protein is bonded to a polymenc tether which is covalently attached to the polymer coating.
  • a polymeric tether is Polyethylene glycol (PEG)- Maleimide, sold by Shearwater Polymers, Inc.
  • PEG-Maleimide must be used with a cysteine amino acid, therefore it may be used when the active protein is Protease G.
  • PEG-Maleimide may also be used in conjunction with a poly-2 -hydroxyethyl acrylate coating.
  • a generic structure of a preferred acrylate-PEG-Maleimide tether can be represented by the formula:
  • cysteine containing protein tethered to a polymeric coating on the wipe substrate comprises a PEG-Maleimid covalently bonded to a polyethyleneimine coating by N-hydroxysuccimmide, as represented by the formula:
  • Binding means comprising tethered proteins are preferred over physical entrapment since tethered proteins are more mobile and are less covered by the polymer coating, both of which provide more activity of the proteins.
  • Another means for binding the protein of the present invention is a covalent link to an activated site on the surface.
  • the substrate is preferrablv a cellulosic material.
  • the chemical link can be any di-functional compound which will react with the substrate and the protein.
  • the preferred chemical link is ethylenediamine/N- ⁇ - maleimidobutyryloxysuccimmide ester (GMBS).
  • a generic structure of a preferred e hylenediamme/GMBS linkage can be represented by the formula:
  • Yet another means for binding the active protein to the substrate of the personal care wipe of the present invention is a polyme ⁇ c tether covalently bonded to an activated site on the surface of the substrate.
  • the preferred tether is ethylenediamme/polyethylene glycol-Maleimide.
  • a generic structure of a directly bonded ethylenediamine/PEG-Maleimide tether can be represented by the formula:
  • the wipe compositions of the present invention can comprise a wide range of optional ingredients.
  • Nonlimitmg examples of functional classes of ingredients are described at page 537 of this reference.
  • abrasives examples include: abrasives, anti-acne agents, anticaking agents, anti-microbial agents, antioxidants, binders, biological additives, bulking agents, chelat g agents, chemical additives, colorants, cosmetic astringents, cosmetic biocides, denaturants, drug astringents, emulsifiers, external analgesics, film formers, fragrance components, humectants, mildness enhancers (cationic and nonio c polymers, co-surfactants, lipid moisturizers, hydrocarbon oils, sihcone oils, waxes), opacifymg agents, plasticizers, preservatives, propellants, reducing agents, skm bleaching agents, skin-conditioning agents (emollient, humectants, miscellaneous, and occlusive), skin protectants, solvents, foam boosters, hydrotropes, solubilizmg agents, stabilizers, suspending agents, sunscreen agents, surfactants
  • the personal care compositions of the present invention are useful for personal cleansing, cosmetic skin treatment, and or skm conditioning
  • the present invention may take the form of a personal care wipe or a personal care skin mask.
  • the wipe is used to expose the area to be cleansed to the active enzymes for a relatively short period of time.
  • the wipe is contacted with or wiped skin which needs treatment and then removed.
  • Typical quantities of the present wipes useful for cleansing range from about 1 to about 4 wipes per use, preferably from about 1 to about 2 wipes per use.
  • the skin mask is used to expose the area to be treated for a relatively longer period of time.
  • Typical quantities of the present skm masks useful for cleansing range from about 1 to about 2 masks per use, preferably 1 mask per use.
  • Soak rayon/PET sheets m an aqueous 10% (w/v) NaOH solution for 10-15 minutes with shaking on auto-shaker, using lmL solution per 1 cm 2 sheet Wash sheets three times with deiomzed water under suction, with approximately 1ml water per cm 2 sheet each wash Wash sheets five times with acetone under suction. Allow sheets to soak in acetone for 1 minute between washes. React sheets in a 10% (w/v) p-toluenesulfonyl chloride in acetone solution for 25-30 minutes with shaking (-1 ml/cm 2 ).
  • Rinse sheets 3 times with acetone under suction to remove excess p-toluenesulfonyl chloride React sheets in 2.2M ethylenediamine in acetone solution, pH 13-14, for 2 hours with shaking. Rinse sheets 3 times with acetone under suction to remove excess EDA. Rinse sheets 5 times with dry N,N-d ⁇ methylformam ⁇ de (DMF) under suction. Allow sheets to soak in DMF for 1 minute between washes. React sheets in 10% (w/v) N-7-male ⁇ m ⁇ dobutyryloxysuccm ⁇ m ⁇ de ester (GMBS) overnight with shaking ( ⁇ 1 ml/cm 2 ).
  • GMBS N-7-male ⁇ m ⁇ dobutyryloxysuccm ⁇ m ⁇ de ester
  • EXAMPLE 5 Protease G Covalently Linked to Coated Implement Surface via Polymer Tether Soak rayon/PET sheets in 500 ppm bath of polyethyleneim e for 1 hour with shaking at room temperature ( ⁇ l-2ml/cm 2 sheet). Rinse rayon/PET sheets in 2 successive 0.2M sodium borate buffer, pH 12, baths (-5-10 ml/cm 2 ). Rinse sheets in 2 successive 0.2M sodium borate buffer, pH 8.5, baths. React sheets in 5 mg/mL NHS-PEG 34 oo-Maleimide m 0.2M sodium borate buffer, pH 8.5, with shaking at room temperature for 1 hour.
  • a personal care wipe composition product is prepared as follows: Ingredients Weight Percent Example 6 Example 7 Example 8 Example 9
  • a hydroapertured, nonwoven substrate having a basis weight of about 60 gsy comprising 50% rayon and 50% polyester approximately 6 in. by 7.6 in. and a thickness of about 20 mil having a bound active protein per Examples 1-7.
  • the Phase A ingredients are mixed at room temperature to form a dispersion and heated with stir ⁇ ng to 65°C.
  • the Phase B ingredients are mixed in a separate suitable vessel and heated to 65°C. Once the temperatures are the same, the Phase B ingredients are mixed into the vessel containing the Phase A ingredients and then cooled to 45°C.
  • the Phase C ingredients are then mixed together m a separate vessel at room temperature.
  • the Phase C mixture is added into the vessel containing the combination of Phases A and B at room temperature. 1.5 grams of the resulting solution is sprayed onto each substrate. Alternatively, the substrate can be dipped into the resulting solution. The treated substrate is then dried in an oven to constant weight.
  • the treated substrate is d ⁇ ed in a convection oven at 45°C to constant weight.
  • other substrates such as woven substrates, hydroentangled substrates, natural sponges, synthetic sponges, or polyme ⁇ c netted meshes.
  • Alternative embodiments may be in the from of person care skm masks.
  • a personal care wipe is prepared as follows
  • a hydroapertured, nonwoven substrate having a basis weight of about 60 gsy comprising 50% rayon and 50% polyester approximately 6 in. by 7.6 m. and a thickness of about 20 mil having a bound active protein per Examples 1-7.
  • the Phase A ingredients are mixed at room temperature to form a dispersion and heated with stir ⁇ ng to 65°C.
  • the Phase B ingredients are mixed in a separate suitable vessel and heated to 65°C. Once the temperatures are the same, the Phase B ingredients are mixed into the vessel containing the Phase A ingredients and then cooled to 45°C.
  • the Phase C mixture is added into the vessel containing the combination of Phases A and B at room temperature. 1.5 grams of the resulting solution is sprayed onto each substrate. Alternatively, the substrate can be dipped into the resulting solution. The treated substrate is then dried in an oven to constant weight. Alternatively, the treated substrate is dned m a convection oven at 45 °C to constant weight.
  • substrates such as woven substrates, hydroentangled substrates, natural sponges, synthetic sponges, or polymeric netted meshes.
  • Alternative embodiments may be in the from of person care skm masks.
  • a hydroapertured, nonwoven substrate having a basis weight of about 60 gsy comprising 50% rayon and 50% polyester approximately 6 in. by 7.6 m. and a thickness of about 20 mil having a bound active protein per Examples 1-7.
  • the Phase A ingredients are mixed at room temperature to form a dispersion and heated with stirring to 65°C.
  • the Phase B ingredients are mixed in a separate suitable vessel and heated to 65°C. Once the temperatures are the same, the Phase B ingredients are mixed into the vessel containing the Phase A ingredients and then cooled to 45°C.
  • the Phase C ingredients are then mixed together m a separate vessel at room temperature.
  • the Phase C mixture is added into the vessel containing the combination of Phases A and B at room temperature. 1.5 grams of the resulting solution is sprayed each substrate.
  • the subsfrate can be dipped into the solution.
  • the treated substrate is then dned in an oven to constant weight.
  • the treated substrate is dried in a convection oven at about 45°C to constant weight.
  • substrates such as woven substrates, hydroentangled substrates, natural sponges, synthetic sponges, or polymenc netted meshes.
  • Alternative embodiments may be m the from of person care skin masks.
  • a hydroapertured, nonwoven substrate having a basis weight of about 60 gsy compnsing 50% rayon and 50% polyester approximately 6 in. by 7.6 in. and a thickness of about 20 mil having a bound active protein according to Examples 1-7.
  • the Phase A ingredients are mixed at room temperature to form a dispersion and heated with stirring to 65°C.
  • the Phase B ingredients are mixed m a separate suitable vessel and heated to 65°C. Once the temperatures are the same, the Phase B ingredients are mixed into the vessel containing the Phase A ingredients and then cooled to 45°C.
  • the Phase C mixture is added into the vessel containing the combination of Phases A and B at room temperature. 1.5 grams of the resulting solution is sprayed onto each substrate. Alternatively, the substrate can be dipped into the solution. The treated substrate is then dried in an oven to constant weight. Alternatively, the treated substrate is dried in a convection oven at about 45°C to constant weight.
  • subsfrates such as woven substrates, hydroentangled substrates, natural sponges, synthetic sponges, or polymeric netted meshes.
  • Alternative embodiments may be in the from of person care skin masks.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Birds (AREA)
  • Epidemiology (AREA)
  • Dermatology (AREA)
  • Engineering & Computer Science (AREA)
  • Biomedical Technology (AREA)
  • Cosmetics (AREA)
  • Detergent Compositions (AREA)
  • Coating Of Shaped Articles Made Of Macromolecular Substances (AREA)
  • Chemical Or Physical Treatment Of Fibers (AREA)
  • Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)

Abstract

La présente invention porte sur des compositions pour soins d'hygiène personnelle comprenant un substrat insoluble dans l'eau, une pluralité d'enzymes Proteases G et un élément de liaison fixant en permanence chacune des enzymes au substrat. Les compositions pour soins d'hygiène personnelle comprennent d'environ 0,01 νg/cm2 à environ 1000 νg/cm2 de l'enzyme sur le substrat.
PCT/US1999/021062 1998-09-22 1999-09-14 Compositions pour soins d'hygiene personnelle contenant les enzymes subtilisine liees a des substrats insolubles dans l'eau Ceased WO2000016740A1 (fr)

Priority Applications (6)

Application Number Priority Date Filing Date Title
EP99969327A EP1115376A1 (fr) 1998-09-22 1999-09-14 Compositions pour soins d'hygiene personnelle contenant les enzymes subtilisine liees a des substrats insolubles dans l'eau
JP2000573701A JP2002526434A (ja) 1998-09-22 1999-09-14 水不溶性基質と結合したサブチリシン酵素を含有するパーソナルケア組成物
CA002345127A CA2345127A1 (fr) 1998-09-22 1999-09-14 Compositions pour soins d'hygiene personnelle contenant les enzymes subtilisine liees a des substrats insolubles dans l'eau
AU60388/99A AU743760B2 (en) 1998-09-22 1999-09-14 Personal care compositions containing subtilisin enzymes bound to water insoluble substrates
KR1020017003665A KR20010075285A (ko) 1998-09-22 1999-09-14 수불용성 기재에 결합된 서브틸리신 효소를 함유하는 신체케어 조성물
BR9914026-8A BR9914026A (pt) 1998-09-22 1999-09-14 Composição de esfregão e de máscara da pele de tratamento pessoal e processo para aperfeiçoar a condição da pele

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US10140598P 1998-09-22 1998-09-22
US60/101,405 1998-09-22

Publications (1)

Publication Number Publication Date
WO2000016740A1 true WO2000016740A1 (fr) 2000-03-30

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Country Status (8)

Country Link
EP (1) EP1115376A1 (fr)
JP (1) JP2002526434A (fr)
KR (1) KR20010075285A (fr)
CN (1) CN1319002A (fr)
AU (1) AU743760B2 (fr)
BR (1) BR9914026A (fr)
CA (1) CA2345127A1 (fr)
WO (1) WO2000016740A1 (fr)

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2002092050A3 (fr) * 2001-05-14 2003-11-06 Unilever Plc Lingette de nettoyage humide
GB2396297A (en) * 2002-12-18 2004-06-23 Coletica A cosmetic or dermopharmaceutical composition comprising an enzyme which is insoluble in an aqueous medium, as well as its uses
US6992054B2 (en) 2001-05-14 2006-01-31 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Damp cleansing wipe
WO2008058989A1 (fr) * 2006-11-17 2008-05-22 Unilever Plc Procédé de dérivation des cheveux avec un réactif de polyéthylèneglycol
WO2014067933A1 (fr) * 2012-10-31 2014-05-08 C-Lecta Gmbh Préparation de support bioactif pour une sécurité améliorée dans les produits de soin et les aliments

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR100507960B1 (ko) * 2002-10-22 2005-08-19 (주)나노팜 피부 각질 제거용 조성물, 이의 제조방법, 및 이를 포함하는 세안조성물
KR100558751B1 (ko) * 2004-10-18 2006-03-14 주식회사 태평양 피부보습용 화장료 조성물

Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4556554A (en) * 1981-06-01 1985-12-03 Germaine Monteil Cosmetiques Corp. Immobilized enzymes
EP0365160A2 (fr) * 1988-10-18 1990-04-25 Scott Paper Company Tissus mouillés
WO1995029979A1 (fr) * 1994-05-02 1995-11-09 The Procter & Gamble Company Compositions de lessive pour textiles contenant des variants de subtilisine bpn'
WO1995030010A1 (fr) * 1994-05-02 1995-11-09 The Procter & Gamble Company Variants de la subtilisine bpn' a adsorption reduite et hydrolyse accrue
WO1995030011A2 (fr) * 1994-05-02 1995-11-09 The Procter & Gamble Company Variants de subtilisine 309 a adsorption reduite et a hydrolyse accrue
US5538732A (en) * 1994-04-12 1996-07-23 Creative Products Resource, Inc. Medicated applicator sheet for topical drug delivery
WO1996030576A1 (fr) * 1995-03-31 1996-10-03 Kimberly-Clark Worldwide, Inc. Lingettes pre-humidifiees, jetables, notamment dans les toilettes, et biodegradables
WO1997024427A1 (fr) * 1995-12-29 1997-07-10 The Procter & Gamble Company Compositions detergentes contenant des enzymes immobilisees

Patent Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4556554A (en) * 1981-06-01 1985-12-03 Germaine Monteil Cosmetiques Corp. Immobilized enzymes
EP0365160A2 (fr) * 1988-10-18 1990-04-25 Scott Paper Company Tissus mouillés
US5538732A (en) * 1994-04-12 1996-07-23 Creative Products Resource, Inc. Medicated applicator sheet for topical drug delivery
WO1995029979A1 (fr) * 1994-05-02 1995-11-09 The Procter & Gamble Company Compositions de lessive pour textiles contenant des variants de subtilisine bpn'
WO1995030010A1 (fr) * 1994-05-02 1995-11-09 The Procter & Gamble Company Variants de la subtilisine bpn' a adsorption reduite et hydrolyse accrue
WO1995030011A2 (fr) * 1994-05-02 1995-11-09 The Procter & Gamble Company Variants de subtilisine 309 a adsorption reduite et a hydrolyse accrue
WO1996030576A1 (fr) * 1995-03-31 1996-10-03 Kimberly-Clark Worldwide, Inc. Lingettes pre-humidifiees, jetables, notamment dans les toilettes, et biodegradables
WO1997024427A1 (fr) * 1995-12-29 1997-07-10 The Procter & Gamble Company Compositions detergentes contenant des enzymes immobilisees

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2002092050A3 (fr) * 2001-05-14 2003-11-06 Unilever Plc Lingette de nettoyage humide
US6992054B2 (en) 2001-05-14 2006-01-31 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Damp cleansing wipe
GB2396297A (en) * 2002-12-18 2004-06-23 Coletica A cosmetic or dermopharmaceutical composition comprising an enzyme which is insoluble in an aqueous medium, as well as its uses
GB2396297B (en) * 2002-12-18 2005-08-31 Coletica A cosmetic or dermopharmaceutical composition comprising an enzyme which is insoluble in an aqueous medium, as well as its uses.
WO2008058989A1 (fr) * 2006-11-17 2008-05-22 Unilever Plc Procédé de dérivation des cheveux avec un réactif de polyéthylèneglycol
WO2014067933A1 (fr) * 2012-10-31 2014-05-08 C-Lecta Gmbh Préparation de support bioactif pour une sécurité améliorée dans les produits de soin et les aliments

Also Published As

Publication number Publication date
CA2345127A1 (fr) 2000-03-30
JP2002526434A (ja) 2002-08-20
EP1115376A1 (fr) 2001-07-18
AU743760B2 (en) 2002-02-07
BR9914026A (pt) 2001-07-03
KR20010075285A (ko) 2001-08-09
CN1319002A (zh) 2001-10-24
AU6038899A (en) 2000-04-10

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