WO1999047631A1 - Nettoyage enzymatique en bloc solide a controle electrolytique pour systemes de nettoyage sur place - Google Patents

Nettoyage enzymatique en bloc solide a controle electrolytique pour systemes de nettoyage sur place Download PDF

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Publication number
WO1999047631A1
WO1999047631A1 PCT/US1999/005748 US9905748W WO9947631A1 WO 1999047631 A1 WO1999047631 A1 WO 1999047631A1 US 9905748 W US9905748 W US 9905748W WO 9947631 A1 WO9947631 A1 WO 9947631A1
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WIPO (PCT)
Prior art keywords
enzyme
composition
detergent
cleaning
soil
Prior art date
Application number
PCT/US1999/005748
Other languages
English (en)
Inventor
G. Jason Wei
David M. Mcsherry
Bruce R. Cords
Original Assignee
Ecolab Inc.
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Filing date
Publication date
Application filed by Ecolab Inc. filed Critical Ecolab Inc.
Priority to CA002324002A priority Critical patent/CA2324002C/fr
Priority to AU30074/99A priority patent/AU745239B2/en
Priority to EP99911433A priority patent/EP1071738A1/fr
Priority to BRPI9908763-4A priority patent/BR9908763B1/pt
Priority to JP2000536814A priority patent/JP2002506921A/ja
Priority to NZ506738A priority patent/NZ506738A/xx
Publication of WO1999047631A1 publication Critical patent/WO1999047631A1/fr

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/02—Inorganic compounds ; Elemental compounds
    • C11D3/04—Water-soluble compounds
    • C11D3/046—Salts
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C7/00—Other dairy technology
    • A23C7/02—Chemical cleaning of dairy apparatus; Use of sterilisation methods therefor
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/0047—Detergents in the form of bars or tablets
    • C11D17/0065—Solid detergents containing builders
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/221—Mono, di- or trisaccharides or derivatives thereof
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38609—Protease or amylase in solid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/14—Hard surfaces
    • C11D2111/20—Industrial or commercial equipment, e.g. reactors, tubes or engines

Definitions

  • the invention relates to enzyme containing solid detergent compositions that can be used to remove food soil from typically food or foodstuff related manufacturing equipment or processing surfaces.
  • the invention relates to the use of said composition in a clean-in-place system. Further, the invention relates to the use of electrical conductivity to control the concentration of enzyme cleaner during cleaning operations.
  • Periodic cleaning and sanitizing in the food process industry is a regimen mandated by law and rigorously practiced to maintain the exceptionally high standards of food hygiene and shelf-life expected by today's consumer.
  • Residual food soil left on food contact equipment surfaces for prolonged periods, can harbor and nourish growth of opportunistic pathogen and food spoilage microorganisms that can contaminate foodstuffs processed in close proximity to the residual soil.
  • Insuring protection of the consumer, against potential health hazards associated with food borne pathogens and toxins and. maintaining the flavor, nutritional value and quality of the foodstuff requires diligent cleaning and soil removal from any surfaces of which contact the food product directly or are associated with the processing environment.
  • cleaning in the context of the care and maintenance of food preparation surfaces and equipment, refers to the treatment given all food product contact surfaces following each period of operation to substantially remove food soil residues including any residue that can harbor or nourish any harmful microorganism. Freedom from such residues, however, does not indicate perfectly clean equipment. Large populations of microorganisms may exist on food process surfaces even after visually successful cleaning.
  • the concept of cleanliness as applied in the food process plant is a continuum wherein absolute cleanliness is the 2 ideal goal always strived for; but, in practice, the cleanliness achieved is of lesser degree.
  • cleaning refers to an antimicrobial treatment applied to all surfaces after the cleaning is effected that reduces the microbial population to safe levels.
  • the critical objective of a cleaning and sanitizing treatment program, in any food process industry, is the reduction of microorganism populations on targeted surfaces to safe levels as established by public health ordinances or proven acceptable by practice. This effect is termed a “sanitized surface” or “sanitization”.
  • a sanitized surface is, by Environmental Protection Agency (EPA) regulation, a consequence of both an initial cleaning treatment followed with a sanitizing treatment.
  • a sanitizing treatment applied to a cleaned food contact surface must result in a reduction in population of at least 99.999% reduction (5 log order reduction) for a given microorganism.
  • Sanitizing treatment is defined by "Germicidal and Detergent Sanitizing Action of Disinfectants", Official Methods of Analysis of the Association of Official Analytical Chemists, paragraph 960.09 and applicable sections, 15th Edition, 1990 (EPA Guideline 91-2).
  • Sanitizing treatments applied to non-food contact surfaces in a food process facility must cause 99.9% reduction (3 log order reduction) for given microorganisms as defined by the "Non- Food Contact Sanitizer Method, Sanitizer Test" (for inanimate, non-food contact surfaces), created from EPA DIS/TSS- 10. 07 January '82. Although it is beyond the scope of this invention to discuss the chemistry of sanitizing treatments, the microbiological efficacy of these treatments is significantly reduced if the surface is not clean prior to sanitizing.
  • the presence of residual food soil can inhibit sanitizing treatments by acting as a physical barrier which shields microorganisms lying within the soil layer from the microbicide or by inactivating sanitizing treatments by direct chemical interaction which deactivates the killing mechanism of the microbicide.
  • sanitizing treatments by acting as a physical barrier which shields microorganisms lying within the soil layer from the microbicide or by inactivating sanitizing treatments by direct chemical interaction which deactivates the killing mechanism of the microbicide.
  • the major operational parameters of a cleaning treatment in a food process facility are mechanical work level, solution temperature, detergent composition and concentration, and contact time. Of course other variables such as equipment surface characteristics; soil composition, concentration, and condition; and water composition effect the cleaning treatment.
  • a major challenge of detergent development for the food process industry is the successful removal of soils that are resistant to conventional treatment and the 5 elimination of chemicals that are not compatible with food processing.
  • One such soil is protein, and one such chemical is chlorine or chlorine yielding compounds, which can be incorporated into detergent compounds or added separately to cleaning programs for protein removal.
  • Protein soil residues, often called protein films, occur in all food processing industries but the problem is greatest for the dairy industry, including milk and milk products producers, because dairy products are among the most perishable of major foodstuffs and any soil residues have serious quality consequences.
  • Proteins are biomolecules which occur in the cells, tissues and biological fluids of all living organisms. Proteins range in molecular weight from about 6000 (single protein chain) to several millions (protein chain complexes) and can simplistically be described as polyamides composed of covalently linked alpha amino acids. Of over 100 naturally occurring amino acids, only 20 are utilized in protein biosynthesis - their number and sequential order characterizing each protein.
  • the covalent bond that joins amino acids together in proteins is called a peptide bond and is formed by reaction between the alpha amino (-NH, "" ) protonated group of one amino acid and the alpha carboxyl (-COO ' ) group of another.
  • alpha amino ( -NH 2 ) groups and alpha carboxyl ( - COOH) groups are ionized at physiological pH with the protonated amino group bearing a positive charge and the deprotonated carboxyl group a negative charge.
  • a unique conformation or three-dimensional structure also must exist, which is determined by interactions between a polypeptide and its aqueous environment, and driven by such fundamental forces as ionic or electrostatic interactions; hydrophobic interactions; hydrogen and covalent bonding; and charge transfer interactions.
  • the complex three-dimensional structure of the protein macromolecule is that conformation which maximizes stability and minimizes the necessary energy to maintain.
  • four 6 levels of structure influence a protein's structure; three being intramolecular and existing in single polypeptide chains, and the fourth being intermolecular associations within a multi-chained molecule.
  • Principles of protein structure are available in modern biochemistry textbooks, for example: Biochemistry, Armstrong, F. B., 3rd edition, Oxford University Press, New York, 1989; or
  • proteins contain heterogeneous modules consisting of electrically charged (both negative and positive) regions, hydrophobic regions, and hydrophilic polar regions, analogous in character to similar areas on food processing equipment surfaces having trace soil residues.
  • the protein can thus interact with the hard surface in a variety of different ways, depending on the particular orientation exposed to the surface, the number of binding sites, and overall binding energies.
  • chlorinated detergent solutions in the food process industry is not without problems. Corrosion is a constant concern, as is degradation of polymeric gaskets, hoses, and appliances. Practice indicates that available chlorine concentrations must initially be at least 75, and preferably, 100 ppm for optimum protein film removal. At concentrations of available chlorine less than 50 ppm, protein soil build-up is enhanced by formation of insoluble, adhesive chloro-proteins (see “Cleanability of Milk-Filmed Stainless Steel by Chlorinated Detergent Solutions", Jensen. J.M.. Journal of Dairy Science. Vol. 53, No. 2, pp. 248-251 (1970). Chlorine concentrations are not easy to maintain or analytically discern in detersive solutions.
  • Chlorine has improved cleaning efficiency, and improved sanitation resulting in improved product quality. No safe and effective, lower cost alternative has been advanced by the detergent manufacturers.
  • Enzyme powders or granulates tended to segregate in these mechanical mixtures resulting in non-uniform, and hence undependable, product in use. Precautions had to be taken with packaging and in storage to protect the product from humidity which caused enzyme degradation. Dry powdered compositions are not as conveniently suited as liquids for rapid solubility or miscibility in cold and tepid waters nor functional as direct application products to soiled surfaces. For these reasons and for expanded applications, it became desirable to have liquid enzyme compositions.
  • Enzymes generally denature or degrade in an aqueous medium resulting in the serious reduction or complete loss of enzyme activity. This instability results from at least two mechanisms. Enzymes have three-dimensional protein structure which can be physically or chemically changed by other solution ingredients, such as surfactants and builders, causing loss of catalytic effect. Alternately when protease is present in the composition, the protease will cause proteolytic digestion of the other enzymes if they are not proteases: or of itself via a process called autolysis.
  • aqueous enzyme composition In order to market an aqueous enzyme composition, the enzyme must be stabilized so that it will retain its functional activity for prolonged periods of (shelf- life or storage) time. If a stabilized enzyme system is not employed, an excess of enzyme is generally required to compensate for expected loss.
  • enzymes are expensive and are in fact the most costly ingredients in a commercial detergent even though they are present in relatively minor amounts. Thus, it is no surprise that methods of stabilizing enzyme-containing, aqueous, liquid detergent compositions are extensively described in the patent literature. (See, Guilbert, U.S. Pat. No. 4,238,345).
  • the literature also includes enzyme compositions which contain high percentages of water, but the water or the enzyme or both are immobilized; or otherwise physically separated to prevent hydrolytic interaction.
  • an aqueous enzyme encapsulate formed by extrusion see U.S. Pat. No. 4,087,368 to Borrello issued May 2, 1978.
  • a gel-like aqueous based enzyme detergent see U.S. Patent No. 5,064,553 to Dixit et al. issued November 12, 1991.
  • a dual component, two-package composition wherein the enzyme is separated from the alkalies, builders and sequestrants. see U.S. Pat. No. 4.243,543 to Guilbert et al. issued January 6. 1981.
  • Weber may be employed as a laundry detergent, a laundry pre-soak, or as a general purpose cleaner for dairy and cheese making processing equipment.
  • the detergent solution of Weber generally has a pH in the range of 7.0 to 11.0.
  • the aforementioned prior teaching embodies high foam surfactants and fails to provide detergents which can be utilized in CIP cleaning systems.
  • Ciaccio U.S. Pat. No. 4,212.761 to Ciaccio issued July 15. 1980 discloses a neat or use solution composition containing a ratio of sodium carbonate and sodium bicarbonate, a surfactant, an alkaline protease, and optionally sodium tripolyphosphate.
  • the detergent solution of Ciaccio is used for cleaning dairy equipment including clean-in-place methods.
  • the pH of the use solution in Ciaccio ranges from 8.5 to 11.
  • no working examples of detergent concentrate embodiments are disclosed.
  • Ciaccio only asserts that the desirable detergent form would be as a premixed particulate not a solid block. From the ingredient ranges discussed, it becomes obvious to one skilled in the art that such compositions would be too wet, sticky, and mull-like in practice to be readily commercialized.
  • U.S. Pat. No. 5,064,561 to Rouillard issued November 12. 1991 discloses a two-part cleaning system for use in clean-in-place facilities.
  • Part one is a liquid concentrate consisting of a highly alkaline material (NaOH), defoamer, solubilizer or emulsifier, sequestrant and water.
  • Part two is a liquid concentrate containing an enzyme which is a protease generally present as a liquid or as a slurry within a non- 14 aqueous carrier which is ordinarily an alcohol, surfactant, polyol or mixture thereof.
  • Rouillard generally has a pH of about 9.5 to about 10.5.
  • Rouillard teaches the use of high alkaline materials; and, paradoxically, the optional use of buffers to stabilize the pH of the composition.
  • Rouillard's invention discloses compositions wherein unstable aqueous mixtures of inorganic salts and organic defoamer are necessarily coupled by inclusion of a solubilizer or emulsifier to maintain an isotropic liquid concentrate. Rouillard further teaches that the defoamer may not always be required if a liquid (the assumption of term is
  • aqueous, stabilized form of the enzyme is used in the second concentrate.
  • Esperase 8.0 SL is a proteolytic enzyme suspended in Tergitol 15-S-9, a high foam surfactant — hence the need for a defoamer and for a solubilizer or emulsifier. Rouillard still further discloses that proteolytic enzyme (Esperase 8.0 SL) of an by itself does not clean as effectively as a high alkaline, chlorinated detergent unless mixed with its cooperative alkaline concentrate.
  • CIP cleaning in place
  • U.S. Patent No. 4,858,449 issued to Lehn teaches the use of dispensers which dispense solid alkaline chemicals used in cleaning processes which control the quantity of chemical dispensed by periodically measuring the conductivity of the 15 concentrated chemical solution. This invention periodically measures the conductivity of the consorted solution in order to determine the amount of solution which has been dispensed. Various chemicals can be used as long as the solutions conductivity can be correlated with its concentration.
  • U.S. Patent No. 4,211,517, issued to Schmid discloses the use of measuring pH in order to determine the conductivity.
  • U.S. Patent No. 4,845,965, issued to Copeland et al discloses the use of a conductivity sensor which is used for controlling the dispensing of multiple alkaline cleaning solutions to one or more laundry machines using preferably a single delivery system.
  • the conductivity sensor is used to monitor the concentration of the concentrated detergent solution.
  • U.S. Patent No. 4,826.661, also issued to Copeland et al teaches the preparation of a concentrated cleaning solution by contacting a solid block cleaning composition with the dissolving liquid.
  • U.S. Patent No. 4,690,305 issued to Copeland et al discloses a washed chemical dispenser for dispensing a concentrated alkaline chemical solution by contacting a solid block with an aqueous liquid.
  • WO 97/02753 issued to Olsen, relates to an enzymatic method of clean in place self processing equipment, in particular, slaughter house process equipment.
  • the invention discloses a method of clean in place process equipment comprising circulating a solution comprising a protease and a lipase for a sufficient period of time to permit action of the enzymes.
  • WO 96/41859 relates to a liquid composition, in particular to a liquid detergent composition, comprising an enzyme and an improved enzyme stabilizer.
  • the enzyme stabilizers in this patent generally are phenyl boronic acid derivatives.
  • WO 93/21299 issued to Marshall, et al relates to a liquid automatic dishwashing detergent composition which is substantially free of chlorine bleach and silicate.
  • the automatic dishwashing composition contains enzyme, an enzyme stabilizing system and detergent surfactant or detergent builder.
  • WO 97/07190 issued to Rouillard, teaches the use of portion packed powdered low alkaline enzymatic detergents for cleaning milk lines at a dairy installation. 1 6
  • This invention discloses formulations comprising enzyme, borate. carbohydrate, etc. in a solid form. Further methods of manufacture and methods of use for compositional embodiments having application as detergents in the food process industry are disclosed. We have also discovered a method that controls enzyme concentration with conductivity. Said compositions are used in cleaning food soiled surfaces. The materials are made in concentrated form. The diluted concentrate when delivered to the targeted surfaces will provide cleaning. The concentrated product is a solid. The concentrate products being manufactured by any number of solid blending methods known to the art inclusive of casting, pour- molding, compressions-molding, extrusion-molding or similar shape - packaging operations. The preferred embodiment comprises the use of extrusion to create the solid block detergent. Said products being designed for clean-in-place (CIP) cleaning regimens in food process industries such as dairy plant and farm; fluid milk and processed milk by-product. More specifically, the present invention describes detergent compositions generally containing enzymes, surfactants and sequestrants.
  • CIP clean-in-place
  • the claimed compositions eliminate the need for high alkaline builders, axillary defoamers. corrosion inhibitors, and chlorine release agents. Accordingly the claimed compositions are safer to use and resulting effluent is friendly to the environment. When used, the claimed composition will continue to clean soiled food process equipment surfaces equal to or better than present, conventional chlorinated - high alkaline detergents.
  • the food processing units having at least some minimal film residue derived from the protein containing food product is contacted with a protease containing detergent composition of the invention.
  • the unit can be prerinsed with an aqueous rinse composition to remove gross food soil.
  • the protein residue on the food processing unit is contacted with a detergent of the invention for a sufficient period of time to remove the protein film. Any protease enzyme residue remaining on the surfaces of the unit or otherwise 17 within the food processing unit, can be denatured using a variety of techniques.
  • the food processing unit can be heated with a heat source comprising steam, hot water, etc.
  • the residual protease enzyme remaining in the food processing unit can be denatured by exposing the enzyme to an extreme pH. Typically, a pH greater than about 10, preferably greater than about 11 (alkaline pH) or less than 5, preferably less than about 4 (acid pH) is sufficient to denature the enzyme.
  • the protease can be denatured by exposing any residual protease enzyme to the effects of an oxidizing agent.
  • oxidizing agents that also have the benefit of acting as a food acceptable sanitizer include aqueous hydrogen peroxide, aqueous ozone containing compositions, aqueous peroxy acid compositions wherein the peroxy acid comprises a per C, . , 4 monocarboxylic or dicarboxylic acid composition.
  • hypochlorite. iodophors and interhalogen complexes ICl, ClBr, etc.
  • Denatured enzyme remaining in the system after the denaturing step can have little or no effect on any proteinaceous food.
  • the resulting product quality is unchanged.
  • Preferred foods treated in food processing units having a denaturing step following the cleaning step include milk and dairy products, beer and other fermented malt beverages, puddings, soups, yogurt, or any other liquid, thickened liquid, or semisolid protein containing food material.
  • the objectives of this product invention are thus to:
  • Figure 1 is a graphical representation of stability of residual enzyme activity data for various test formulations.
  • the invention comprises a use dilution, use-solution composition having exceptional detergency properties when applied as a cleaning treatment to food soiled equipment surfaces and having particular cleaning efficiency upon tenacious protein films.
  • Preferred embodiments of the invention provide cleaning performance superior to conventional high alkaline, chlorine containing detergents and is directed especially to the diary industry in which milk proteins are involved.
  • the present invention generally comprises in a low foaming solid or solid block formulation free of an alkaline metal hydroxide or a source of active chlorine:
  • a preferred concentrate embodiment of this invention is a detergent system which comprises a stabilized solid block detergent which is made by solidifying a liquid detergent premix with borate alone or together with other solidifying agents.
  • the premix contains a liquid protease enzyme source, an optional surfactant and a sequestrant.
  • the other said solidifying agents are selected from carbonates, bicarbonates, sulfates and urea.
  • the enzyme is stabilized by a borate salt, a carbohydrate composition or a combination thereof.
  • An important aspect is the use of borate for multiple functions: stabilization of the enzyme, solidification, alkalinity source and buffering agent (with a pK a of 9.1 ).
  • the solid enzyme containing detergents stabilized by the stabilizing compounds of the invention can be further enhanced using a borate stabilizing material.
  • a borate stabilizing material The combination of an alkali metal borate with the vicinal hydrocarbon stabilizer compositions of the invention produce enhanced stability.
  • Boric acid chemistry like many other chemistries is complex and contains many simple and complex compounds.
  • Mixtures of B(OH) 3 and B(OH) 4 " ' appear in classic buffer systems depending on pH.
  • Sodium borate, potassium borate, disodium tetraborate, disodium tetraborate pentahydrate. disodium tetraborate decahydrate, etc. can be used in the stabilized materials of the invention.
  • borate compounds alone and combined with a carbohydrate compounds having vicinal hydroxyl groups can act as stabilizing agents for the enzyme materials.
  • the alkali metal salts of boric acid or more complex borates oligomers of boric acid including both linear and cyclic borate materials
  • Preferred materials are species such as Na 2 O*B 4 O 7 *XH 2 O, disodium tetraborate pentahydrate, disodium tetraborate decahydrate, anhydrous borax, sodium pentaborate decahydrate, sodium metaborate octahydrate, sodium metaborate tetrahydrate and others can be prepared.
  • Borax decahydrate and borax pentahydrate are produced by extraction from dry-lake brines and other natural sources.
  • the enzyme stabilizer compositions of the invention can also include an organic C 4 compound with at least one vicinal hydroxide group corresponding to the following formula:
  • glycerin derivatives such as glycerin lower alkyl monoesters and ethers including glyceryl monostearate, glyceryl monooleate, glyceryl-monoethyl ether, glyceryl- diethyl ether, etc. 2.3-dihydroxybutyraldehyde, and other C 4+ organic compounds having vicinal hydroxyls.
  • One class of preferred stabilizers are the monosaccharides including aldotetrose, aldopentose, aldohexose, aldoheptose, aldooctose, ketotetrose, ketopentose, ketohexose, etc. compounds.
  • Such compounds include erythrose, ribose. glucose, mannose, galactose. isomers and derivatives thereof and other 20 similar monosaccharides.
  • disaccharides compounds including sucrose, lactose, cellobiose, maltose are useful.
  • the present invention related to a CIP system in which a stabilized enzyme is used to remove milk proteins from milk processing equipment. Further, the present invention relates to the use of electrolytic control to regulate the concentration of detergent within the system.
  • the benefits of the present invention include an ability to clean with enzymes. Consequently, the cleaning solution is less alkaline and uses less water. Because no chlorine is used, there are fewer problems with corrosiveness.
  • Enzymes are important and essential components of biological systems, their function being to catalyze and facilitate organic and inorganic reactions. For example, enzymes are essential to metabolic reactions occurring in animal and plant life.
  • the enzymes of this invention are simple proteins or conjugated proteins produced by living organisms and functioning as biochemical catalysts which, in detergent technology, degrade or alter one or more types of soil residues encountered on food process equipment surfaces thus removing the soil or making the soil more removable by the detergent-cleaning system. Both degradation and alteration of soil residues improve detergency by reducing the physicochemical forces which bind the soil to the surface being cleaned, i.e. the soil becomes more water soluble.
  • enzymes are referred to as simple proteins when they require only their protein structures for catalytic activity. Enzymes are described as conjugated proteins if they require a non-protein component for activity, termed cofactor, which is a metal or an organic biomolecule often referred to as a coenzyme. Cofactors are not involved in the catalytic events of enzyme function. Rather, their role seems to be one of maintaining the enzyme in an active configuration. As used herein, enzyme activity refers to the ability of an enzyme to perform the desired catalytic function of soil degradation or alteration; and, enzyme stability pertains to the ability of an enzyme to remain or to be maintained in the active state. 21 Enzymes are extremely effective catalysts.
  • Enzymes also have substrate (soil) specificity which determines the breadth of its catalytic effect. Some enzymes interact with only one specific substrate molecule (absolute specificity); whereas, other enzymes have broad specificity and catalyze reactions on a family of structurally similar molecules (group specificity).
  • Enzymes exhibit catalytic activity by virtue of three general characteristics: the formation of a noncovalent complex with the substrate, substrate specificity, and catalytic rate. Many compounds may bind to an enzyme, but only certain types will lead to subsequent reaction. The later are called substrates and satisfy the particular enzyme specificity requirement. Materials that bind but do not thereupon chemically react can affect the enzymatic reaction either in a positive or negative way. For example, unreacted species called inhibitors interrupt enzymatic activity. Enzymes which degrade or alter one or more types of soil, i.e. augment or aid the removal of soils from surfaces to be cleaned, are identified and can be grouped into six major classes on the basis of the types of chemical reactions which they catalyze in such degradation and alteration processes. These classes are (1) oxidoreductase: (2) transferase; (3) hydrolase; (4) lyase: (5) isomerase; and (6) ligase.
  • hydrolases catalyze the addition of water to the soil with which they interact and generally cause a degradation or breakdown of that soil residue. This breakdown of soil residue is of particular and practical importance in detergent 22 applications because soils adhering to surfaces are loosened and removed or rendered more easily removed by detersive action.
  • hydrolases are the most preferred class of enzymes for use in cleaning compositions.
  • Preferred hydrolases are esterases, carbohydrases, and proteases.
  • the most preferred hydrolase sub-class for the present invention is the proteases.
  • proteases catalyze the hydrolysis of the peptide bond linkage of amino acid polymers including peptides, polypeptides, proteins and related substances - generally protein complexes - such as casein which contains carbohydrate (glyco group) and phosphorus as integral parts of the protein and exists as distinct globular particles held together by calcium phosphate; or such as milk globulin which can be thought of as protein and lipid sandwiches that comprise the milk fat globule membrane.
  • Proteases thus cleave complex, macromolecular protein structures present in soil residues into simpler short chain molecules which are, of themselves, more readily desorbed from surfaces, solubilized or otherwise more easily removed by detersive solutions containing said proteases.
  • Proteases a sub-class of hydrolases, are further divided into three distinct subgroups which are grouped by the pH optima (i.e. optimum enzyme activity over a certain pH range). These three subgroups are the alkaline, neutral and acids proteases. These proteases can be derived from vegetable, animal or microorganism origin; but, preferably are of the latter origin which includes yeasts, molds and bacteria. More preferred are serine active, alkaline proteolytic enzymes of bacterial origin. Particularly preferred for embodiment in this invention are bacterial, serine active, alkaline proteolytic enzymes obtained from alkalophilic strains of Bacillus, especially from Bacillus subtilis and Bacillus licheniformis.
  • Proteolytic enzymes produced by chemically or genetically modified mutants are herein included by definition as are close structural enzyme variants.
  • These alkaline proteases are generally neither inhibited by metal chelating agents (sequestrants) and thiol poisons nor activated by metal ions or reducing agents. They all have relatively broad substrate specificities, are inhibited by diisopropylfluorophosphate (DFP), are all endopeptidases, generally have molecular weights in the range of 20,000 to 40,000, and are active in the pH 23 ranges of from about 6 to about 12; and, in the temperature range of from about
  • DFP diisopropylfluorophosphate
  • alkaline proteases examples include Alcalase
  • alkaline proteases are obtainable in liquid or dried form, are sold as raw aqueous solutions or in assorted purified, processed and compounded forms, and are comprised of about 2% to about 80% by weight active enzyme generally in combination with stabilizers, buffers, cofactors. impurities and inert vehicles.
  • the actual active enzyme content depends upon the method of manufacture and is not critical, assuming the detergent solution has the desired enzymatic activity.
  • the particular enzyme chosen for use in the process and products of this invention depends upon the conditions of final utility, including the physical product form, use pH, use temperature, and soil types to be degraded or altered. The enzyme can be chosen to provide optimum activity and stability for any given set of utility conditions. For example.
  • Purafect is a preferred alkaline protease for use in detergent compositions of this invention having application in lower temperature cleaning programs ⁇ from about 30°C to about 65°C; whereas, Esperase (R) is the alkaline protease of choice for higher temperature detersive solutions, from about 50°C to about 85°C.
  • the amount of commercial alkaline protease composite present in the final use-dilution, use-solution ranges from about 0.001 % ( 10 ppm) by weight of detersive solution to about 0.02% (200 ppm) by weight of solution of the commercial enzyme product, which typically contains 5-10 percent of active enzyme.
  • KNPU Kilo-Novo Protease Units
  • the activity of proteases present in the use-solution ranges from about 1 x 10° KNPU/gm solution to about 4 x 10 "3 KNPU/gm solution.
  • proteolytic enzymes may be incorporated into this invention. While various specific enzymes have been described above, it is to be understood that any protease which can confer the desired proteolytic activity to the composition may be used and this embodiment of this invention is not limited in any way by specific choice of proteolytic enzyme.
  • proteases it is also to be understood, and one skilled in the art will see from the above enumeration, that other enzymes which are well known in the art may also be used with the composition of the invention. Included are other hydrolases such as esterases, carboxylases and the like: and. other enzyme classes.
  • the enzyme or enzyme admixture may be incorporated into various non-liquid embodiments of the present invention as a coated, encapsulated, agglomerated, prilled or marumerized form.
  • the enzyme stabilizing system of the present invention consists of sodium borate, sucrose, milk or a combination thereof.
  • the enzyme stabilizer compositions of the invention include an organic C 4+ compound with at least one vicinal hydroxide group corresponding to the following formula:
  • glycerin derivatives such as glycerin lower alkyl monoesters and ethers including glyceryl monostearate, glyceryl monooleate, glyceryl-monoethyl ether, glyceryl- diethyl ether, etc. 2,3-dihydroxybutyraldehyde. and other C 4+ organic compounds having vicinal hydroxyls.
  • glycerin lower alkyl monoesters and ethers including glyceryl monostearate, glyceryl monooleate, glyceryl-monoethyl ether, glyceryl- diethyl ether, etc. 2,3-dihydroxybutyraldehyde. and other C 4+ organic compounds having vicinal hydroxyls.
  • One class of preferred reversion inhibitors are the monosaccharides including aldotetrose, aldopentose, aldohexose. aldohepto
  • aldooctose. ketotetrose, ketopentose, ketohexose, etc. compounds Such compounds include erythrose, ribose, glucose, mannose, galactose. isomers and derivatives thereof and other similar monosaccharides. Additionally, disaccharides compounds including sucrose, lactose, cellobiose, maltose are useful.
  • the stabilizer, solidification, etc. agent of the invention can include an alkali metal borate. 2 6
  • borate compounds and borate compounds, optionally combined with carbohydrate compounds having vicinal hydroxyl groups can act as stabilizing agents for the enzyme materials.
  • the alkali metal salts of boric acid or more complex borates (oligomers of boric acid including both linear and cyclic borate materials) can be used.
  • Preferred materials are species such as
  • Borax (anhydrous), borax decahydrate and borax pentahydrate are produced by extraction and drying from dry-lake brines and other natural sources.
  • surfactant or surfactant admixture of the present invention can be selected from water soluble or water dispersible nonionic, semi-polar nonionic, anionic, cationic, amphoteric. or zwitterionic surface-active agents; or any combination thereof.
  • the particular surfactant or surfactant mixture chosen for use in the process and products of this invention depends upon the conditions of final utility, including method of manufacture, physical product form, use pH, use temperature, foam control, and soil type.
  • Surfactants incorporated into the present invention must be enzyme compatible and free of enzymatically reactive species.
  • the surfactant should be free of peptide and glycosidic bonds respectively. Care should be taken in including cationic surfactants because some reportedly decrease enzyme effectiveness.
  • the preferred surfactant system of the invention is selected from nonionic or anionic species of surface-active agents, or mixtures of each or both types.
  • Nonionic 27 and anionic surfactants offer diverse and comprehensive commercial selection, low price; and, most important, excellent detersive effect ⁇ meaning surface wetting, soil penetration, soil removal from the surface being cleaned, and soil suspension in the detergent solution. This preference does not teach exclusion of utility for cationics, or for that sub-class of nonionic entitled semi-polar nonionics, or for those surface- active agents which are characterized by persistent cationic and anionic double ion behavior, thus differing from classical amphoteric, and which are classified as zwitterionic surfactants.
  • the most preferred surfactant system of the present invention is selected from nonionic or anionic surface-active agents, or mixtures of each or both types which impart low foam to the use-dilution, use solution of the detergent composition during application.
  • the surfactant or the individual surfactants participating within the surfactant mixture are of themselves low foaming within normal use concentrations and within expected operational application parameters of the detergent composition and cleaning program.
  • there is advantage to blending low foaming surfactants with higher foaming surfactants because the latter often impart superior detersive properties to the detergent composition.
  • Mixtures of low foam and high foam nonionics and mixtures of low foam nonionics and high foam anionics can be useful in the present invention if the foam profile of the combination is low foaming at normal use conditions.
  • foaming nonionics and anionics can be judiciously employed without departing from the spirit of this invention.
  • Particularly preferred concentrate embodiments of this invention are designed for clean-in-place (CIP) cleaning systems within food process facilities; and. most particularly for dairy farm and fluid milk and milk by-product producers.
  • CIP clean-in-place
  • 28 Foam is a major concern in these highly agitated, pump recirculation systems during the cleaning program. Excessive foam reduces flow rate, cavitates recirculation pumps, inhibits detersive solution contact with soiled surfaces, and prolongs drainage. Such occurrences during CIP operations adversely affect cleaning performance and sanitizing efficiencies.
  • the present invention permits incorporation of high concentrations of surfactant as compared to conventional chlorinated, high alkaline CIP and COP cleaners.
  • Certain preferred surfactant or surfactant mixtures of the invention are not generally physically compatible nor chemically stable with the alkalis and chlorine of convention. This major differentiation from the art necessitates not only careful foam profile analysis of surfactants being included into compositions of the invention; but, also demands critical scrutiny of their detersive properties of soil removal and suspension.
  • the present invention relies upon the surfactant system for gross soil removal from equipment surfaces and for soil suspension in the detersive solution.
  • Soil suspension is as important a surfactant property in CIP detersive systems as soil removal to prevent soil redeposition on 29 cleaned surfaces during recirculation and later re-use in CIP systems which save and re-employ the same detersive solution again for several cleaning cycles.
  • the concentration of surfactant or surfactant mixture useful in use- dilution, use solutions of the present invention ranges from about 0.002% (20 ppm) by weight to about 0.1 % ( 1000 ppm) by weight, preferably from about 0.005% (50 ppm) by weight to about 0.075% (750 ppm) by weight, and most preferably from about 0.008% (80 ppm) by weight to about 0.05% (500 ppm) by weight.
  • concentration of surfactant or surfactant mixture useful in the most preferred concentrated embodiment of the present invention ranges from about 5% by weight to about 75% by weight of the total formula weight percent of the enzyme containing composition.
  • Nonionic surfactants useful in the invention are generally characterized by the presence of an organic hydrophobic group and an organic hydrophilic group and are typically produced by the condensation of an organic aliphatic, alkyl aromatic or polyoxyalkylene hydrophobic compound with a hydrophilic alkaline oxide moiety which in common practice is ethylene oxide or a polyhydration product thereof, polyethylene glycol.
  • any hydrophobic compound having a hydroxyl, carboxyl. amino, or amido group with a reactive hydrogen atom can be condensed with ethylene oxide, or its polyhydration adducts, or its mixtures with alkoxylenes such as propylene oxide to form a nonionic surface- active agent.
  • hydrophilic polyoxyalkylene moiety which is condensed with any particular hydrophobic compound can be readily adjusted to yield a water dispersible or water soluble compound having the desired degree of balance between hydrophilic and hydrophobic properties.
  • Useful nonionic surfactants in the present invention include:
  • Block polyoxypropylene-polyoxyethylene polymeric compounds based upon propylene glycol, ethylene glycol, glycerol, trimethylolpropane, and 30 ethylenediamine as the initiator reactive hydrogen compound.
  • Examples of polymeric compounds made from a sequential propoxylation and ethoxylation of initiator are commercially available under the trade name Pluronic and Tetronic manufactured by BASF Corp.
  • Pluronic compounds are difunctional (two reactive hydrogens) compounds formed by condensing ethylene oxide with a hydrophobic base formed by the addition of propylene oxide to the two hydroxyl groups of propylene glycol. This hydrophobic portion of the molecule weighs from about 1,000 to about 4,000. Ethylene oxide is then added to sandwich this hydrophobe between hydrophilic groups, controlled by length to constitute from about 10% by weight to about 80% by weight of the final molecule.
  • Tetronic (R) compounds are tetra-functional block copolymers derived from the sequential addition of propylene oxide and ethylene oxide to ethylenediamine.
  • the molecular weight of the propylene oxide hydrotype ranges from about 500 to about 7,000; and, the hydrophile, ethylene oxide, is added to constitute from about 10% by weight to about 80% by weight of the molecule.
  • the alkyl group can. for example, be represented by diisobutylene, di-amyl, polymerized propylene. iso-octyl, nonyl, and di-nonyl. Examples of commercial compounds of this chemistry are available on the market under the trade name Igepal manufactured by Rhone-Poulenc and Triton manufactured by Union Carbide. 3.
  • the alcohol moiety can consist of mixtures of alcohols in the above delineated carbon range or it can consist of an alcohol having a specific number of carbon atoms within this range. Examples of
  • the acid moiety can consist of mixtures of acids in the above defined carbon atoms range or it can consist of an acid having a specific number of carbon atoms within the range. Examples of commercial compounds of this chemistry are available on the market under the trade name Nopalcol manufactured by Henkel Corporation and Lipopeg manufactured by Lipo Chemicals, Inc.
  • ester moieties In addition to ethoxylated carboxylic acids, commonly called polyethylene glycol esters, other alkanoic acid esters formed by reaction with glycerides, glycerin, and polyhydric (saccharide or sorbitan/sorbitol) alcohols have application in this invention for specialized embodiments, particularly indirect food additive applications. All of these ester moieties have one or more reactive hydrogen sites on their molecule which can undergo further acylation or ethylene oxide (alkoxide) addition to control the hydrophilicity of these substances. Care must be exercised when adding these fatty ester or acylated carbohydrates to compositions of the present invention containing amylase and/or lipase enzymes because of potential incompatibility.
  • nonionic low foaming surfactants include:
  • Tetraonic R surfactants are produced by BASF Corporation by the sequential addition of ethylene oxide and propylene oxide to ethylenediamine.
  • the hydrophobic portion of the molecule weighs from about 2, 100 to about 6,700 with the central hydrophile comprising 10% by weight to 80% by weight of the final molecule.
  • R is an alkyl group of 8 to 9 carbon atoms
  • A is an alkylene chain of 3 to 4 carbon atoms
  • n is an integer of 7 to 16
  • m is an integer of 1 to 10.
  • defoaming nonionic surfactants disclosed in U.S. Pat. No. 3,382,178 issued May 7 1968 to Lissant et al.. incorporated herein by reference, having the general formula Z[(OR) ⁇ OH] 2 wherein Z is alkoxylatable material.
  • R is a radical derived from an alkaline oxide which can be ethylene and propylene and n is an integer from, for example, 10 to 2,000 or more and z is an integer determined by the number of reactive oxyalkylatable groups.
  • conjugated polyoxyalkylene compounds described in U.S. Pat. No. 2,674,619, issued April 6, 1954 to Lundsted et al, incorporated herein by reference, having the formula Y[(C 3 H 6 O n (C 2 H 4 O) m H] x wherein Y is the residue of an organic compound having from about 2 to 6 carbon atoms and containing x reactive hydrogen atoms in which x has a value of at least about 2.
  • n has a value such that the molecular weight of the polyoxypropylene hydrophobic base is at least about 900 and m has value such that the oxyethylene content of the molecule is from about 10% to about 90% by weight.
  • Y Compounds falling within the scope of the definition for Y include, for example, propylene glycol, glycerine, pentaerythritol, trimethylolpropane, ethylenediamine and the like.
  • the oxypropylene chains optionally, but advantageously, contain small amounts of ethylene oxide and the oxyethylene chains also optionally, but advantageously, contain small amounts of propylene oxide.
  • Additional conjugated polyoxyalkylene surface-active agents which are advantageously used in the compositions of this invention correspond to the formula: P[(C 3 H 6 O) n (C 2 H 4 O) ir H] wherein P is the residue of an organic compound having from about 8 to 18 carbon atoms and containing x reactive hydrogen atoms in 34 which x has a value of 1 or 2, n has a value such that the molecular weight of the polyoxyethylene portion is at least about 44 and m has a value such that the oxypropylene content of the molecule is from about 10% to about 90% by weight.
  • the oxypropylene chains may contain optionally, but advantageously, small amounts of ethylene oxide and the oxyethylene chains may contain also optionally, but advantageously, small amounts of propylene oxide.
  • ® Surfonic is a registered trade name of Texaco Chemical Co
  • Plurafac is a registered trade name of BASF Corporation
  • the semi-polar type of nonionic surface active agents are another class of nonionic surfactant useful in compositions of the present invention.
  • semi-polar nonionics are high foamers and foam stabilizers which make their application in CIP systems limited.
  • semi-polar nonionics would have immediate utility.
  • the semi-polar nonionic surfactants include the amine oxides, phosphine oxides, sulfoxides and their alkoxylated derivatives.
  • Amine oxides are tertiary amine oxides corresponding to the general formula:
  • R 1 , R 2 , and R 3 may be aliphatic, aromatic, heterocyclic, alicyclic, or combinations thereof.
  • R 1 is an alkyl radical of from about 8 to about 24 carbon atoms
  • R 2 and R 3 are selected from the group consisting of alkyl or hydroxyalkyl of 1 -3 carbon atoms and mixtures thereof
  • R 4 is an alkaline or a hydroxyalkylene group containing 2 to 3 carbon atoms
  • n ranges from 0 to about 20.
  • Useful water soluble amine oxide surfactants are selected from the coconut or tallow alkyl di-(lower alkyl) amine oxides, specific examples of which are dodecvldimethylamine oxide, tridecyldimethylamine oxide, etradecyldimethylamine oxide, pentadecyldimethylamine oxide, hexadecyldimethylamine oxide, heptadecyldimethylamine oxide, octadecyldimethylaine oxide, dodecyldipropylamine oxide, tetradecyldipropylamine oxide, hexadecyldipropylamine oxide, tetradecyldibutylamine oxide, 3 6 octadecyldibutylamine oxide, bis(2-hydroxyethyl)dodecylamine oxide, bis(2- hydroxyethyl)-3-dodecoxy- 1 -hydroxypropylamine
  • Useful semi-polar nonionic surfactants also include the water soluble phosphine oxides having the following structure:
  • R' is an alkyl, alkenyl or hydroxyalkyl moiety ranging from 10 to about 24 carbon atoms in chain length; and, R 2 and R 3 are each alkyl moieties separately selected from alkyl or hydroxyalkyl groups containing 1 to 3 carbon atoms.
  • Examples of useful phosphine oxides include dimethyldecylphosphine oxide. dimethyltetradecylphosphine oxide, methylethyltetradecylphosphone oxide, dimethylhexadecylphosphine oxide, diethyl-2-hydroxyoctyldecylphosphine oxide, bis(2-hydroxyethyl)dodecylphosphine oxide, and bis(hydroxymethyl)tetradecylphosphine oxide.
  • Semi-polar nonionic surfactants useful herein also include the water soluble sulfoxide compounds which have the structure:
  • R 1 is an alkyl or hydroxyalkyl moiety of about 8 to about 28 carbon atoms, from 0 to about 5 ether linkages and from 0 to about 2 hydroxy 1 substituents; and R 2 is an 37 alkyl moiety consisting of alkyl and hydroxyalkyl groups having 1 to 3 carbon atoms.
  • sulfoxides include dodecyl methyl sulfoxide; 3- hydroxy tridecyl methyl sulfoxide; 3-mefhoxy tridecyl methyl sulfoxide; and 3- hydroxy-4-dodecoxybutyl methyl sulfoxide.
  • surface active substances which are categorized as anionics because the charge on the hydrophobe is negative; or surfactants in which the hydrophobic section of the molecule carries no charge unless the pH is elevated to neutrality or above (e.g. carboxylic acids).
  • Carboxylate. sulfonate. sulfate and phosphate are the polar (hydrophilic) solubilizing groups found in anionic surfactants.
  • cations counterions
  • sodium, lithium and potassium impart water solubility; ammonium and substituted ammonium ions provide both water and oil solubility; and, calcium, barium, and magnesium promote oil solubility.
  • anionics are excellent detersive surfactants and are therefore, favored additions to heavy duty detergent compositions.
  • anionics have high foam profiles which limit their use alone or at high concentration levels in cleaning systems such as CIP circuits that require strict foam control.
  • anionics are very useful additives to preferred compositions of the present invention; at low percentages or in cooperation with a low foaming nonionic or defoam agent for application in CIP and like foam controlled cleaning regimens; and, at higher concentrations in detergent compositions designed to yield foaming detersive solutions.
  • anionic surfactants are preferred ingredients in various embodiments of the present invention which incorporate foam for dispensing and utility -- for example, clinging foams used for general facility cleaning.
  • anionic surface active compounds are useful to impart special chemical or physical properties other than detergency within the composition.
  • Anionics can be employed as gelling agents or as part of a gelling or thickening system.
  • Anionics are excellent solubilizers and can be used for hydro tropic affect 38 and cloud point control.
  • Anionics can also serve as the solidifier for solid product forms of the invention, and so forth.
  • Alkylaryl sulfonates 3. Alkyl sulfonates
  • anionic surfactants may be incompatible with the enzymes incorporated into the present invention.
  • the acyl-amino acids and salts may be incompatible with proteolytic enzymes because of their peptide structure.
  • suitable synthetic, water soluble anionic detergent compounds are the ammonium and substituted ammonium (such as mono-, di- and triethanolamine) and alkali metal (such as sodium, lithium and potassium) salts of 39 the alkyl mononuclear aromatic sulfonates such as the alkyl benzene sulfonates containing from about 5 to about 18 carbon atoms in the alkyl group in a straight or branched chain, e.g., the salts of alkyl benzene sulfonates or of alkyl toluene, xylene.
  • alkyl naphthalene sulfonate diamyl naphthalene sulfonate, and dinonyl naphthalene sulfonate and alkoxylated derivatives.
  • Other anionic detergents are the olefin sulfonates, including long chain alkene sulfonates, long chain hydroxyalkane sulfonates or mixtures of alkenesulfonates and hydroxyalkane-sulfonates.
  • alkyl sulfates alkyl poly(ethyleneoxy) ether sulfates and aromatic poly(ethyleneoxy) sulfates such as the sulfates or condensation products of ethylene oxide and nonyl phenol (usually having 1 to 6 oxyethylene groups per molecule.
  • aromatic poly(ethyleneoxy) sulfates such as the sulfates or condensation products of ethylene oxide and nonyl phenol (usually having 1 to 6 oxyethylene groups per molecule.
  • the particular salts will be suitably selected depending upon the particular formulation and the needs therein.
  • the most preferred anionic surfactants for the most preferred embodiment of the invention are the linear or branched alkali metal mono and/or di-(C 6 . l4 )alkyl diphenyl oxide mono and/or disulfonates, commercially available from Dow
  • cationic surfactants may be synthesized from any combination of elements containing an "onium" structure RnX+Y- and could include compounds other than nitrogen (ammonium) such as phosphorus (phosphonium) and sulfur (sulfonium).
  • nitrogen containing compounds probably because synthetic routes to nitrogenous cationics are simple and straightforward and give high yields of product, e.g. they are less expensive.
  • Cationic surfactants refer to compounds containing at least one long carbon chain hydrophobic group and at least one positively charge nitrogen.
  • the long carbon chain group may be attached directly to the nitrogen atom by simple substitution; or more preferably indirectly by a bridging functional group or groups 4 0 in so-called interrupted alkylamines and amido amines which make the molecule more hydrophilic and hence more water dispersible. more easily water solubilized by co-surfactant mixtures, or water soluble.
  • additional primary, secondary or tertiary amino groups can be introduced or the amino nitrogen can be quaternized with low molecular weight alkyl groups, further, the nitrogen can be a member of branched or straight chain moiety of varying degrees of unsaturation; or, of a saturated or unsaturated heterocyclic ring.
  • cationic surfactants may contain complex linkages having more than one cationic nitrogen atom.
  • the surfactant compounds classified as amine oxides, amphoterics and zwitterions are themselves cationic in near neutral to acidic pH solutions and overlap surfactant classifications.
  • Polyoxyethylated cationic surfactants behave like nonionic surfactants in alkaline solution and like cationic surfactants in acidic solution.
  • the simplest cationic amines, amine salts and quaternary ammonium compounds can be schematically drawn thus:
  • R represents a long alkyl chain
  • R', R" and R'" may be either long alkyl chains or smaller alkyl or aryl groups or hydrogen and X represents an anion. Only the amine salts and quaternary ammonium compounds are of practical use in this invention because of water solubility.
  • cationics are specialty surfactants incorporated for specific effect; for example, detergency in compositions of or below neutral pH; antimicrobial efficacy; thickening or gelling in cooperation with other agents; and so forth.
  • the cationic surfactants useful in the compositions of the present invention have the formula R 1 m R 2 x Y L Z wherein each R 1 is an organic group containing a straight or branched alkyl or alkenyl group optionally substituted with up to three phenyl or hydroxy groups and optionally interrupted by up to four structures selected from the following group:
  • the R 1 groups may additionally contain up to 12 ethoxy groups, m is a number from 1 to 3. No more than one R 1 group in a molecule can have 16 or more carbon atoms when m is 2 or more than 12 carbon atoms when m is 3.
  • Each R 2 is an alkyl or hydroxyalkyl group containing from 1 to 4 carbon atoms or a benzyl group with no 42 more than one R 2 in a molecule being benzyl, and x is a number from 0 to 11. preferably from 0 to 6.
  • Y is selected from the group consisting of. but not limited to:
  • L is 1 or 2. with the Y groups being separated by a moiety selected from R 1 and R 2 analogs (preferably alkylene or alkenylene) having from 1 to about 22 carbon atoms and two free carbon single bonds when L is 2.
  • Z is a water soluble anion, such as a halide, sulfate, methylsulfate. hydroxide, or nitrate anion, particularly preferred being chloride, bromide, iodide, sulfate or methyl sulfate anions, in a number to give electrical neutrality of the cationic component.
  • Amphoteric surfactants contain both a basic and an acidic hydrophilic group and an organic hydrophobic group. These ionic entities may be any of anionic or cationic groups described in the preceding sections. A basic nitrogen and an acidic carboxylate group are the predominant functional groups, although in a few structures, sulfonate, sulfate, phosphonate or phosphate provide the negative charge.
  • Ampholytic surfactants can be broadly described as derivatives of aliphatic secondary and tertiary amines, in which the aliphatic radical may be straight chain or branched and wherein one of the aliphatic substituents contains from about 8 to 18 carbon atoms and one contains an anionic water solubilizing group, e.g., carboxy, sulfo, sulfato. phosphate or phosphono.
  • Amphoteric surfactants are subdivided into two major classes: (taken from "Surfactant Encyclopedia” Cosmetics & Toiletries.
  • 2-alkyl hydroxyethyl imidazoline is synthesized by condensation and ring closure of a long chain carboxylic acid (or a derivative) with dialkyl ethylenediamine.
  • Commercial amphoteric surfactants are derivatized by subsequent hydrolysis and ring-opening of the imidazoline ring by alkylation « for example with chloroacetic acid or ethyl acetate.
  • alkylation one or two carboxy-alkyl groups react to form a tertiary amine and an ether linkage with differing alkylating agents yielding different tertiary amines.
  • 4 4 Long chain imidazole derivatives having application in the present invention generally have the general formula:
  • R is an acyclic hydrophobic group containing from about 8 to 18 carbon atoms and M is a cation to neutralize the charge of the anion, generally sodium.
  • imidazoline-derived amphoterics include for example: Cocoamphopropionate, Cocoamphocarboxy-propionate. Cocoamphoglycinate. Cocoamphocarboxy-glycinate. Cocoamphopropyl-sulfonate, and Cocoamphocarboxy-propionic acid.
  • Betaines are a special class of amphoteric discussed in the section entitled, Zwitterion Surfactants.
  • N-alkylamino acid ampholytes having application in this invention include alkyl beta-amino dipropionates, RN(C 2 H 4 COOM) 2 and RNHC 2 H 4 COOM.
  • R is an acyclic hydrophobic group containing from about 8 to about 18 carbon atoms, and M is a cation to neutralize the charge of the anion.
  • amphoteric of special character termed a zwitterion.
  • amphoterics contain cationic and anionic groups which ionize to a nearly equal degree in the isoelectric region of the molecule and develop strong"inner-salt" attraction between positive-negative charge centers.
  • surfactant betaines do not exhibit strong cationic or anionic characters at pH extremes nor do they show reduced water solubility in their isoelectric range.
  • betaines are compatible with anionics.
  • Zwitterionic synthetic surfactants useful in the present invention can be broadly described as derivatives of aliphatic quaternary ammonium, phosphonium, and sulfonium compounds, in which the aliphatic radicals can be straight chain or branched, and wherein one of the aliphatic substituents contains from 8 to 18 carbon atoms and one contains an anionic water solubilizing group, e.g., carboxy, sulfonate, sulfate, phosphate, or phosphonate.
  • a general formula for these compounds is:
  • R 1 contains an alkyl, alkenyl, or hydroxyalkyl radical of from 8 to 18 carbon atoms having from 0 to 10 ethylene oxide moieties and from 0 to 1 glyceryl moiety;
  • Y is selected from the group consisting of nitrogen, phosphorus, and sulfur atoms;
  • R 2 is an alkyl or monohydroxy alkyl group containing 1 to 3 carbon atoms;
  • x is 1 when Y is a sulfur atom and 2 when Y is a nitrogen or phosphorus atom,
  • R 3 is an alkylene or hydroxy alkylene or hydroxy alkylene of from 1 to 4 carbon atoms and
  • Z 4 6 is a radical selected from the group consisting of caboxylate, sulfonate, sulfate, phosphonate, and phosphate groups.
  • Examples include: 4-[N,N-di(2-hydroxyethyl)-N-octadecylammonio]-butane- 1 -carboxylate;
  • the alkyl groups contained in said detergent surfactants can be straight or branched and saturated or unsaturated.
  • the nonionic and anionic surfactants enumerated above can be used singly or in combination in the practice and utility of the present invention.
  • the semi-polar nonionic, cationic, amphoteric and zwitterionic surfactants generally are employed in combination with nonionics or anionics.
  • the above examples are merely specific illustrations of the numerous surfactants which can find application within the scope of this invention.
  • the foregoing organic surfactant compounds can be formulated into any of the several commercially desirable composition forms of this invention having disclosed utility.
  • compositions are cleaning treatments for food soiled surfaces in concentrated form which, when dispensed or dissolved in water, properly diluted by a proportionating device, and delivered to the target surfaces as a solution, gel or foam will provide cleaning.
  • Said cleaning treatments consisting of one 4 7 product; or, involving a two product system wherein proportions of each are utilized.
  • Said product being concentrates of liquid or emulsion; solid, tablet, or encapsulate; powder or particulate; gel or paste; and slurry or mull.
  • Solidifying Agents are used in the claimed invention in order to convert the liquid detergent premix into a solid.
  • Borate can function as a solidifying agent within the present invention.
  • Additional solidifying agents can be drawn from the the group comprised of carbonates, bicarbonates, sulfates and urea.
  • the composition of the present invention generally comprises components known as chelating agents, builders or sequestrants.
  • sequestrants are those molecules capable of complexing or coordinating the metal ions commonly found in service water and thereby preventing the metal ions from interfering with the functioning of detersive components within the composition. Any number of sequestrants may be used in accordance with the invention.
  • Representative sequestrants include salts of amino carboxylic acids, phosphonic acid salts, water soluble acrylic polymers, among others.
  • the molecular weight (Mw) of these polymeric materials is about 200-8000, preferably 4000-6000.
  • the term "condensed phosphate " ' indicates a material having at least one group according to the formula:
  • empty bonds are directed to other phosphate groups, cations, etc. which can be part of a linear, condensed or cyclic phosphate composition.
  • Compounds with phosphate moieties useful as sequestrants are alkali metal condensed phosphates, cyclic phosphates, organo phosphonic acids and organo phosphonic acid salts.
  • Useful condensed phosphates include alkali metal 48 pyrophosphate.
  • an alkali metal polyphosphate such as sodium tripolyphosphate
  • organo phosphonic acids include, mono, di, tri and tetra-phosphonic acids which can also contain groups capable of forming anions under alkaline conditions such as carboxy, hydroxy, thio and the like.
  • the tendency of the condensed phosphate materials to revert can be controlled by using a condensed phosphate that reduces the impact of caustic and water on the sequestrant material. Such effects can be reduced by using an effective particle size sequestrant and by using barrier technologies.
  • the inorganic condensed phosphate can also be combined with an organic carboxylate, phosphonate, phosphonic acid or phosphonic acid salt.
  • the organic materials can aid in sequestering hardness ions in cleaning processes.
  • Suitable amino carboxylic acid chelating agents include N-hydroxyethyliminodiacetic acid, nitrilotriacetic acid (NT A), ethylenediaminetetraacetic acid (EDTA), N- hydroxyethyl-ethylenediaminetriacetic acid (HEDTA), and diethylenetriaminepentaacetic acid (DTPA).
  • these amino carboxylic acids are generally present in concentrations ranging from about 1 wt-% to 50 wt-%, preferably from about 2 wt-% to 45 wt-%, and most preferably from about 3 wt-% to 40 wt-%.
  • Suitable sequestrants include water soluble acrylic polymers having pendant -CO, "1 groups, used to condition the wash solutions under end use conditions.
  • Such polymers include polyacrylic acid, polymethacrylic acid, acrylic acid-methacrylic acid copolymers, acrylic acid-itaconic acid copolymers, hydrolyzed polyacrylamide. hydrolyzed methacrylamide, hydrolyzed acrylamide- methacrylamide copolymers, hydrolyzed polyacrylonitrile, hydrolyzed polymethacrylonitrile, hydrolyzed acrylonitrile methacrylonitrile copolymers, or mixtures thereof.
  • Water soluble salts or partial salts of these polymers such as their respective alkali metal (for example, sodium or potassium) or ammonium salts can also be used.
  • the number average molecular weight of the polymers is from about 4000 to about 12,000.
  • Preferred polymers include polyacrylic acid, the partial sodium salts of polyacrylic acid or sodium polyacrylate having an average molecular weight within the range of 4000 to 8000.
  • These acrylic polymers are generally 49 useful in concentrations ranging from about 0.5 wt-% to 20 wt-%, preferably from about 1 to 10. and most preferably from about 1 to 5.
  • phosphonic acids are 1 -hydroxy ethane- 1,1-diphosphonic acid; aminotri(methylenephosphonic acid); aminotri -(methylenephosphonate), sodium salt 2-hydroxy ethyl- iminobis(mefhylenephosphonic acid); diethylenetriaminepenta(methylenephosphonic acid);diethylene-triamine- penta(methylenephosphonate) sodium salt; hexamethylenediamine-
  • phosphonic acids or salts are present in a concentration ranging from about 0.25 to 25 wt-%, preferably from about 1 to 20 wt-%, and most preferably from about 1 to 18 wt-% based on the solid detergent.
  • the Figure shows data regarding the stability of the enzyme activity in the solid block materials. Each preparation should be compared to the enzyme control represented by the dashed line. Certain compositions. Examples 5, 6, 7, 8 and 9 all have superior enzyme activity stability when compared to the enzyme material alone. Such stability is present over twelve days under comparatively severe conditions.
  • the product is dissolved by spraying water in a solid dispenser and delivered to a sump or directly to use solution tank, from which the use solution is pumped to where cleaning is needed.
  • the use concentration is typically about 0.1 % in aqueous solution.
  • the pH 50 is about 9.0 to 10 and the temperature is between 130°F and 150°F (54.4 °C to 65.6
  • control over the concentration of the enzyme cleaner in the aqueous solution must be maintained.
  • the conductivity of the ionic species in the aqueous solution sodium, potassium, borate, etc. ions
  • a spray on dispenser can be used to deliver an aqueous concentrate to maintain the use solution at an appropriate concentration of enzyme surfactant and other components.
  • the conductivity of the use solution is measured using an electrical conductivity measurement means. As the conductivity of the use solution drops, typically the concentration of the enzyme, surfactant and other active ingredients in the use solution also is reduced proportionally.
  • the use solution can be replenished of enzyme surfactant and other actives by introducing an aqueous concentrate made by spraying water onto the solid block detergent of the invention for a period of time sufficient to dispense an adequate amount of the detergent into the use solution.
  • an aqueous concentrate made by spraying water onto the solid block detergent of the invention for a period of time sufficient to dispense an adequate amount of the detergent into the use solution.
  • the ionizable inorganic materials are also dispensed.
  • the concentration of the enzyme component and other surfactants and other ingredients can also be controlled quite closely.
  • the conductivity of the use solution is maintained between about 500 and 800 ⁇ siemens/cm to provide an adequate concentration of enzyme, surfactant and other active ingredients.
  • Electrolytic conductivity is defined as the electrical conductance of a unit cube of electrolytic solution. It is expressed in the same units as electrical conductivity, i.e.. reciprocal ohms per unit length. Most commonly we find conductivity units of:
  • Electrolytic conductivity is most often measured by placing electrodes in contact with the electrolytic solution which is contained in such a way that the measured electrical conductance between the electrodes can be related to the conductivity of the solution.
  • a conductivity cell commonly comprises an enclosure made of electrically insulating material such as glass or plastic which holds a portion of the solution and accommodates the two electrodes. The cell constant of such a device is then used to relate the measured electrical conductance between the electrodes to the actual electrolytic conductivity.
  • Two electrodes 1 centimeter square located on opposite interior faces of a hollow cube 1 centimeter on an edge would have a cell constant of 1/cm, and a measured conductance of 0.005 mhos/cm (0.5 siemens/meter) at 25°C.
  • Alternating current measurements greatly reduces these interfering factors, and finds wide use in such 52 measurements.
  • Properly designed inductive AC conductivity cells operated at appropriate alternating current frequencies obey Ohm's law since the current through the cell is proportional to the applied voltage and the conductivity of the electrolytic solution.
  • Alternating current Wheatstone bridges and conductance meters make up the most widely used instrumentation accepted for electrolytic conductivity measurements. Changes in solution temperature change bridge characteristics similarly, thereby allowing the bridge to remain balanced except for actual changes in solution concentration.
  • Conductivity meters generally apply a constant alternating voltage across the electrodes and respond to the resulting flow of current, which is proportional to the conductivity of the solution. Means of automatic temperature compensation are also included in such circuitry.
  • Measurements of electrolytic conductivity by means of electrical induction can be done without the use of contacting electrodes. Such measurements are made by inducing an alternating current in an electrolyte by use of a coil of wire. The magnitude of the induced current is proportional to the conductivity of the electrolyte. Current is caused to flow in a closed circular path through the electrolyte by a first coil of wire wound on a toroidal core of magnetic material. The magnitude of the current and hence the conductivity is measured by a second similar coil.
  • a typical laboratory-type DC conductivity cell which employs two platinized platinum electrodes contained in an open-bottom cylindrical chamber formed from pyrex glass.
  • This cell has a cell constant of 0.5/cm and is intended for use in measuring the conductivity of distilled water and other dilute solutions used in the laboratory. This kind of cell is dipped into an open-topped container containing the sample to be measured. Wide use is made in the laboratory of conductivity cells of this type in ascertaining water quality and in screening samples to be titrated or further analyzed by other means. A large variety of conductivity cells are available for use including DC and AC cells, electroless cells and others. Examples
  • Conductivity probes can be used to monitor the concentration of enzyme in washing solutions when dispensed from a spray on dispenser.
  • the use of an electrolyte material in the detergent can increase the conductivity of deionized water (at about 1 ⁇ S-cm "1 ) to an adequate conductivity or for typical service water from municipal utilities that can range from 100 to 300 ⁇ S-cm "1 . Since detergent materials are typically dispensed in city water, a substantial increase in conductivity is required to control enzyme concentration when dispensed in city water. Accordingly, a substantial difference in conductivity must be obtained from the dispensed material when compared to city water conductivity.
  • a minimum conductivity of the wash solution is greater than about 300 ⁇ semens/cm preferably greater than 400 ⁇ semens/cm, most preferably greater than 450 ⁇ semens/cm.
  • the process can efficiently operate at conductivities that range greater than 650 ⁇ semens/cm, greater than 700 ⁇ semens/cm or greater than 1000 ⁇ semens/cm.
  • the material can be dispensed even in the presence of substantial milk concentration, a soil that can coat electrode surfaces and reduce efficiency.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Molecular Biology (AREA)
  • Emergency Medicine (AREA)
  • Food Science & Technology (AREA)
  • Polymers & Plastics (AREA)
  • Inorganic Chemistry (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Dairy Products (AREA)

Abstract

L'invention concerne l'utilisation de compositions détergentes solides contenant une enzyme qui peuvent être utilisées pour enlever les taches de nourriture apparaissant sur des surfaces de traitement ou sur les installations de fabrication de produits alimentaires sans utiliser de corrosifs comme par exemple le chlore. L'invention concerne plus particulièrement l'élimination de protéines du lait d'un équipement de traitement quotidien. L'invention concerne en outre l'utilisation de ladite composition dans un système de nettoyage sur place dans lequel la conductivité électrique sert à contrôler la concentration de détergent dans le système. Bien que l'on puisse utiliser différentes enzymes, on utilise de préférence des protéases pour aider à enlever les protéines du lait de l'équipement de traitement. La protéase est stabilisée par l'ajout de borate de sodium, de saccharose, de lait ou de leur combinaison dans la solution. Le borate de sodium contribue également à la solidification, grâce à ses propriétés de tampon et de source d'alcalinité. Le borate de sodium permet l'utilisation d'un niveau élevé d'électrolyte pour le contrôle de la conductivité.
PCT/US1999/005748 1998-03-18 1999-03-16 Nettoyage enzymatique en bloc solide a controle electrolytique pour systemes de nettoyage sur place WO1999047631A1 (fr)

Priority Applications (6)

Application Number Priority Date Filing Date Title
CA002324002A CA2324002C (fr) 1998-03-18 1999-03-16 Nettoyage enzymatique en bloc solide a controle electrolytique pour systemes de nettoyage sur place
AU30074/99A AU745239B2 (en) 1998-03-18 1999-03-16 Solid block enzymatic cleaning with electrolytic control for clean-in-place systems
EP99911433A EP1071738A1 (fr) 1998-03-18 1999-03-16 Nettoyage enzymatique en bloc solide a controle electrolytique pour systemes de nettoyage sur place
BRPI9908763-4A BR9908763B1 (pt) 1998-03-18 1999-03-16 processo para dispensar uma composição de limpeza enzimática estabilizada em bloco sólido em um local de uso e composição de limpeza enzimática estabilizada em bloco sólido.
JP2000536814A JP2002506921A (ja) 1998-03-18 1999-03-16 現場清浄システム用の電気分解管理による固体ブロック酵素洗浄
NZ506738A NZ506738A (en) 1998-03-18 1999-03-16 Solid block enzymatic cleaning with electrolytic control for clean-in-place systems

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US4062898A 1998-03-18 1998-03-18
US09/040,628 1998-03-18

Publications (1)

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WO1999047631A1 true WO1999047631A1 (fr) 1999-09-23

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Country Link
EP (1) EP1071738A1 (fr)
JP (1) JP2002506921A (fr)
AR (2) AR018765A1 (fr)
AU (1) AU745239B2 (fr)
BR (1) BR9908763B1 (fr)
CA (1) CA2324002C (fr)
NZ (1) NZ506738A (fr)
WO (1) WO1999047631A1 (fr)
ZA (1) ZA200004593B (fr)

Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1679963A1 (fr) * 2003-10-24 2006-07-19 Novapharm Research (Australia) Pty. Limited Pastille utilisable dans un bac recepteur
US7494963B2 (en) 2004-08-11 2009-02-24 Delaval Holding Ab Non-chlorinated concentrated all-in-one acid detergent and method for using the same
US7569532B2 (en) 2000-06-29 2009-08-04 Ecolab Inc. Stable liquid enzyme compositions
US8999911B2 (en) 2011-11-04 2015-04-07 Bissell Homecare, Inc. Enzyme cleaning composition and method of use
EP2609187A4 (fr) * 2010-08-27 2017-04-26 Ecolab USA Inc. Utilisation de sucres dans une matrice de stabilisation et des compositions solides
US20190144784A1 (en) * 2017-11-14 2019-05-16 Ecolab Usa Inc Solid controlled release caustic detergent compositions
US11529588B2 (en) 2017-06-30 2022-12-20 Diversey, Inc. Membrane cleaning solution and method of accelerated membrane cleaning using the same
US11905493B2 (en) 2019-09-27 2024-02-20 Ecolab Usa Inc. Concentrated 2 in 1 dishmachine detergent and rinse aid

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20060293212A1 (en) * 2005-05-05 2006-12-28 Ecolab Inc. Stable solid compositions of spores, bacteria, fungi and/or enzyme
BR112020015170A2 (pt) 2018-01-26 2021-01-26 Ecolab Usa Inc. composições de tensoativo líquido solidificado e de limpeza sólida, e, método para limpar uma superfície
CA3089557A1 (fr) 2018-01-26 2019-08-01 Ecolab Usa Inc. Tensioactifs anioniques liquides solidifiants
KR20200110683A (ko) 2018-01-26 2020-09-24 에코랍 유에스에이 인코퍼레이티드 담체를 이용한 액체 아민 옥사이드, 베타인, 및/또는 설타인 계면활성제의 고체화

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4858449A (en) * 1986-01-09 1989-08-22 Ecolab Inc. Chemical solution dispenser apparatus and method of using
EP0501375A1 (fr) * 1991-02-28 1992-09-02 Kao Corporation Préparation solide enzymatique et procédé pour l'obtenir
GB2271120A (en) * 1992-09-30 1994-04-06 Unilever Plc Shaped detergent composition comprising mutant subtilisin
WO1996006910A2 (fr) * 1994-08-31 1996-03-07 Ecolab Inc. Composition de nettoyage amelioree contenant une enzyme proteolytique
WO1998054285A1 (fr) * 1997-05-30 1998-12-03 The Procter & Gamble Company Barre de lessive contenant une protease d'une plus grande stabilite

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4858449A (en) * 1986-01-09 1989-08-22 Ecolab Inc. Chemical solution dispenser apparatus and method of using
EP0501375A1 (fr) * 1991-02-28 1992-09-02 Kao Corporation Préparation solide enzymatique et procédé pour l'obtenir
GB2271120A (en) * 1992-09-30 1994-04-06 Unilever Plc Shaped detergent composition comprising mutant subtilisin
WO1996006910A2 (fr) * 1994-08-31 1996-03-07 Ecolab Inc. Composition de nettoyage amelioree contenant une enzyme proteolytique
WO1998054285A1 (fr) * 1997-05-30 1998-12-03 The Procter & Gamble Company Barre de lessive contenant une protease d'une plus grande stabilite

Cited By (14)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US7569532B2 (en) 2000-06-29 2009-08-04 Ecolab Inc. Stable liquid enzyme compositions
EP1679963A4 (fr) * 2003-10-24 2010-12-01 Novapharm Res Australia Pastille utilisable dans un bac recepteur
US8795740B2 (en) 2003-10-24 2014-08-05 Novapharm Research (Australia) Pty Ltd Drip tray tablet
EP1679963A1 (fr) * 2003-10-24 2006-07-19 Novapharm Research (Australia) Pty. Limited Pastille utilisable dans un bac recepteur
US7494963B2 (en) 2004-08-11 2009-02-24 Delaval Holding Ab Non-chlorinated concentrated all-in-one acid detergent and method for using the same
US7501027B2 (en) 2004-08-11 2009-03-10 Delaval Holding Ab Non-chlorinated concentrated all-in-one acid detergent and method for using the same
US9902924B2 (en) 2010-08-27 2018-02-27 Ecolab Usa Inc. Use of sugars in a stabilization matrix and solid compositions
EP2609187A4 (fr) * 2010-08-27 2017-04-26 Ecolab USA Inc. Utilisation de sucres dans une matrice de stabilisation et des compositions solides
US8999911B2 (en) 2011-11-04 2015-04-07 Bissell Homecare, Inc. Enzyme cleaning composition and method of use
US11529588B2 (en) 2017-06-30 2022-12-20 Diversey, Inc. Membrane cleaning solution and method of accelerated membrane cleaning using the same
US20190144784A1 (en) * 2017-11-14 2019-05-16 Ecolab Usa Inc Solid controlled release caustic detergent compositions
US10889783B2 (en) * 2017-11-14 2021-01-12 Ecolab Usa Inc. Solid controlled release caustic detergent compositions
US11932830B2 (en) 2017-11-14 2024-03-19 Ecolab Usa Inc. Solid controlled release caustic detergent compositions
US11905493B2 (en) 2019-09-27 2024-02-20 Ecolab Usa Inc. Concentrated 2 in 1 dishmachine detergent and rinse aid

Also Published As

Publication number Publication date
AU3007499A (en) 1999-10-11
ZA200004593B (en) 2002-03-27
BR9908763A (pt) 2000-12-05
EP1071738A1 (fr) 2001-01-31
AR022340A1 (es) 2002-09-04
BR9908763B1 (pt) 2010-05-18
AR018765A1 (es) 2001-12-12
NZ506738A (en) 2003-06-30
AU745239B2 (en) 2002-03-14
JP2002506921A (ja) 2002-03-05
CA2324002C (fr) 2008-10-07
CA2324002A1 (fr) 1999-09-23

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