MXPA00009136A - Solid block enzymatic cleaning with electrolytic control for clean-in-place systems - Google Patents
Solid block enzymatic cleaning with electrolytic control for clean-in-place systemsInfo
- Publication number
- MXPA00009136A MXPA00009136A MXPA/A/2000/009136A MXPA00009136A MXPA00009136A MX PA00009136 A MXPA00009136 A MX PA00009136A MX PA00009136 A MXPA00009136 A MX PA00009136A MX PA00009136 A MXPA00009136 A MX PA00009136A
- Authority
- MX
- Mexico
- Prior art keywords
- enzyme
- cleaning
- further characterized
- composition
- detergent
- Prior art date
Links
- 239000007787 solid Substances 0.000 title claims abstract description 38
- 238000004140 cleaning Methods 0.000 title claims description 131
- 230000002255 enzymatic Effects 0.000 title claims description 22
- 239000000203 mixture Substances 0.000 claims abstract description 171
- 102000004190 Enzymes Human genes 0.000 claims abstract description 158
- 108090000790 Enzymes Proteins 0.000 claims abstract description 158
- 239000003599 detergent Substances 0.000 claims abstract description 118
- 108091005771 Peptidases Proteins 0.000 claims abstract description 38
- 239000004365 Protease Substances 0.000 claims abstract description 29
- 239000000460 chlorine Substances 0.000 claims abstract description 25
- 229910052801 chlorine Inorganic materials 0.000 claims abstract description 25
- ZAMOUSCENKQFHK-UHFFFAOYSA-N chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 claims abstract description 25
- 102000033147 ERVK-25 Human genes 0.000 claims abstract description 21
- 235000013365 dairy product Nutrition 0.000 claims abstract description 21
- 235000010339 sodium tetraborate Nutrition 0.000 claims abstract description 11
- 239000003792 electrolyte Substances 0.000 claims abstract description 9
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- CZMRCDWAGMRECN-GDQSFJPYSA-N Sucrose Natural products O([C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](CO)O1)[C@@]1(CO)[C@H](O)[C@@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-GDQSFJPYSA-N 0.000 claims abstract description 5
- 239000005720 sucrose Substances 0.000 claims abstract description 5
- 239000004094 surface-active agent Substances 0.000 claims description 72
- -1 alkali metal borate Chemical class 0.000 claims description 56
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 49
- 239000003795 chemical substances by application Substances 0.000 claims description 25
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- IAYPIBMASNFSPL-UHFFFAOYSA-N oxane Chemical group C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 16
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- 108091005650 Basic proteases Proteins 0.000 description 14
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Abstract
Disclosed is the use of enzyme containing solid detergent compositions that can be used to remove food soil from typically food or foodstuff related manufacturing equipment or processing surfaces without the use of corrosives such as chlorine. In particular, the invention relates to the removal of milk proteins from dairy processing equipment. The invention further relates to the use of said composition in a clean-in-place system in which electrical conductivity is used to control the concentration of detergent within the system. Although various enzymes can be used, the preferred embodiment of the invention uses proteases to assist in removing the milk proteins from the processing equipment. The protease is stabilized by including sodium borate, sucrose, milk or the combination thereof in the use solution. The sodium borate also functions as an aid to solidification, as a buffering agent and also functions as an alkalinity source. It is the sodium borate which permits the use of a high level of electrolyte for conductivity control.
Description
ENZYMATIC CLEANER IN SOLID BLOCK, WITH ELECROLYTIC CONTROL, FOR CLEANING SYSTEMS ON THE SITE
FIELD OF THE INVENTION
The invention relates to solid detergent compositions containing enzyme, which can be used to remove food dirt from manufacturing equipment or processing surfaces, related to food. The invention relates to the use of said composition in an on-site cleaning system. In addition, the invention relates to the use of electrical conductivity to control the concentration of enzymatic cleaner during cleaning operations.
BACKGROUND OF THE INVENTION
Regular cleaning and sanitation in the food processing industry is a regime mandated by law and rigorously practiced to maintain exceptionally high hygiene standards in food, and the shelf life expected by current consumers. The residual dirt of food, which remains on the surfaces of the equipment that are in contact with food for prolonged periods, can accommodate and nourish the development of opportunistic pathogenic microorganisms that spoil food, which can contaminate processed food materials. next to residual dirt. Guaranteeing protection for the consumer against potential health damages associated with pathogens that live in food and with toxins, and maintaining the flavor, nutritional value and quality of the food, requires diligent cleaning and removal of dirt from any surfaces that are in contact with the food product, directly, or that are associated with the processing environment. The term "clean", in the context of the care and maintenance of surfaces and equipment for preparing food, refers to the treatment given to all surfaces that are in contact with the food produced, after each period of operation, to substantially eliminate food dirt residues, including any residue that may harbor or nourish any harmful microorganism. However, being free of such waste does not indicate a perfectly clean equipment. Large populations of microorganisms may exist on processing surfaces, even after visually satisfactory cleaning. The concept of cleanliness, as it is applied in the food processing plant, is a continuum in which absolute cleanliness is the ideal goal for which one always fights; but in practice, I achieved cleanliness is of a lower grade. The term "sanitize" refers to an antimicrobial treatment applied to all surfaces after cleaning is performed, which reduces the microbial population to safe levels. The critical objective of a cleaning and sanitation treatment program, in any food processing industry, is the reduction of microorganism populations on target surfaces, to safe levels, which are established by public health regulations, or approved by the practice. This effect is called "sanitized surface" or "sanitization". A sanitized surface, according to the regulations of the Environmental Protection Agency of the United States, a consequence of both an initial cleansing treatment and a sanitizing treatment that comes later. A sanitizing treatment, applied to a surface in contact with the food, clean, should result in a reduction in the population of at least 99.999% reduction (a reduction of 5 logarithmic orders) for a given microorganism. Sanitation 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, 15a. edition, 1990 (Guidelines 91-2 of the EPA). Sanitizing treatments applied to surfaces that are not in contact with food, in a food processing facility, must cause a 99.9% reduction (reduction of three logarithmic orders) for a given microorganism, as defined in the Non-Food Contact Sanitizer Method. Sanitizer Test (for inanimate surfaces, not in contact with food), created by EPA DIS / TSS-10.07, January 1982. Although it is beyond the scope of this invention to discuss the chemistry of sanitizing treatments, it is reduced the microbiological efficacy of these treatments if the surface is not cleaned before sanitizing. The presence of residual food dirt can inhibit the sanitizing treatments by acting as a physical barrier that protects the microorganisms that remain inside the dirt layer, against the microbicide, or by inactivating the sanitizing treatments by direct chemical interaction that deactivates the microbicide exterminating mechanism. Thus, the more perishable the food, the more effective the cleaning treatment should be. Cleaning technology in the food processing industry has traditionally been empirical. There was a need for cleaning treatments before a fundamental understanding of the mechanism of deposition and removal of dirt was developed. Due to the quality of the food and public health pressures, the food processing industry has reached a high standard of cleanliness and hygienic practices. This has not been achieved without large outlay, and there is considerable interest in a more efficient and less expensive technology. As knowledge about soils, the role of cleaning chemicals and the effects of cleaning procedures increased; and as improvements in plant design and food processing equipment became apparent, methodically improved the cost effectiveness and capacity of cleaning treatments, ie, cleaning products and procedures, to eliminate the final vestiges of waste. The consequence for the food processing industry and for the public translates into progressively higher standards. The search for ever more efficient and low cost cleaning treatments, coupled with the growing demand for friendly and environmentally compatible cleaning chemicals, has resulted in an increasing number of investigations that have significantly increased the understanding of deposition and elimination processes. , by means of a theoretical treatment, instead of by empirical experimentation. Many modes of improvement can occur, including improved chemicals, or efficiency in the formulation and simplification of the process, etc. See, for example: Theory and Practice of Hard-Surface Cleaning, Jennings, W. G., Advances in Food Research, volume 14, pages 325-455 (1965); or Forces in Detergency, Harris, J.S., Soap and Chemical Specialties, volume 37 (5), part I, pages 68-71 and 125; volume 37 (6), part II, pages 50-52; volume 37 (7), part III, pages 53-55; volume 37 (8), part IV, pages 61-62, 104, 106; part V, pages 61-64 (1961), or Physico-chemical aspects of hard-surface cleaning. Soil removal mechanisms, Koopal, L. K., Neth. Milk Dairy J., 39, pages 127-154 (1985). These studies confirm that the deposition of dirt on a surface and the sequential transitions of the adherence of dirt to the surface (adsorption), removal of dirt from the surface and suspension of dirt in a cleaning solution, can be described in terms of Well-established, generally accepted concepts of colloidal chemistry and surface chemistry. The meaning of this association is that there are now predictive tools that help the design of chemical cleaning compounds optimized for specific soils or formulated to solve other deficiencies in the cleaning program. The precepts suggest that it is difficult to maintain a clean surface; that energy is released (entropy increases) during the deposition of dirt, which favors the physico-chemical stability, that is, a dirty surface is a preferred condition by nature or more stable. To reverse this process and clean the surface, energy must necessarily be provided. In normal practice, this energy takes the form of mechanical and thermal energies, carried to the dirty surface. The chemical additives (detergents) for the cleaning solution (usually water) reduce the amount of energy required to reverse the energy-favored fouling process. Thus, the definition of detergent (Definition of the Word "Detergent", Bourne, MC and Jennings, WG, The Journal of the American Oil Chemists' Society, 40, page 212 (1963)) is "any substance that, alone or in a mixture, reduce the work necessary for a cleaning process ". Simply use the detergents because they facilitate cleaning. It follows that the word "detergency" "is understood, then, to mean the cleaning or removal of a dirt from a substrate, by means of a liquid medium". The elimination of dirt can not be considered as a spontaneous process, because the kinetics of dirt removal requires a finite period. The longer the cleaning solution is in contact with the dirt deposited, the more dirt is removed, up to a practical limit. The final vestiges of dirt become increasingly difficult to remove. In the last stage of the dirt removal process, cleaning involves resolving the very strong adhesive force between the surface of the dirt and the substrate, instead of the weaker coherent forces from dirt to dirt; and eventually a state of equilibrium is reached when the redeposition of the dirt occurs at the same speed as the removal of dirt. Thus, the main operating parameters of a cleaning treatment in a food processing plant are at the level of mechanical work, temperature of the solution, composition and concentration of the detergent, and contact time. Of course other variables, such as the characteristics of the equipment surface, the composition of the dirt, the concentration and the condition, as well as the effect of the aqueous composition, affect the cleaning treatment. However, these factors can not be controlled and, consequently, must be compensated, as necessary. The food processing industry has come to rely more on the efficiency of detergents than to compensate for design or functional deficiencies in their cleaning programs. This is not meant to suggest that the industry has not faced these factors; in fact, the cleaning processes have changed considerably during the last years, due to the technological advances in the food processing equipment and the development of specialized cleaning equipment. The modern food processing industries have revolutionized their cleaning processes through on-site cleaning (CIP, acronym for its English designation: Cleaning-ln-Place), and automation. A major challenge in the development of detergents for the food processing industry is the satisfactory elimination of soils that are resistant to conventional treatment and the elimination of chemicals that are not compatible with food processing. One of these soils is protein, and one of those chemicals is chlorine or chlorine-producing compounds, which can be incorporated into detergent compounds or added separately to cleaning programs for the removal of the protein. Protein dirt residues, often referred to as protein films, occur in all food processing industries; but the problem is greater in the dairy industry, including milk producers and producers of dairy products, because dairy products are among the most perishable of the main food materials, and any dirt residues have serious consequences on the quality . That such protein dirt residues are common in the dairy industry and fluid milk byproducts, including dairy farms, is not surprising, because the protein constitutes approximately 27% of the milk's natural solids. (Milk Components and Their Characteristics, Harper, W. J. in Dairy Technology and Engineering (compilers Harper, W. J. and Hall, C. W.), pages 18-19.The AVI Pubiishing Company, Westport, 1976). Proteins are biomolecules that occur in the cells, tissues and biological fluids of all living animals. Proteins vary in molecular weight from about 6000 (a single protein chain) to several million (protein chain complexes) and can be described simplistically as polyamides composed of covalently linked alpha-amino acids. Of more than 100 amino acids that occur in nature, only 20 are used in the biosynthesis of the protein; characterizing its number and sequential order to each protein. The covalent binding that binds amino acids together in proteins is called peptide binding, and is formed by the reaction between the alpha-amino (-NH3") protonated group of an amino acid and the alpha-carboxyl group (-COO") of another amino acid. These reactions occur in solution; and alpha-amino groups (-NH2) and alpha-carboxyl groups (-COOH) are ionized at physiological pH, with the protonated amino group carrying a positive charge and the deprotonated carboxyl group, a negative charge. Polypeptides alone do not constitute a biologically functional protein. There must also be a unique or single conformation or a three-dimensional structure, which is determined by the interactions between a polypeptide and its aqueous environment, and activated by fundamental forces such as ionic or electrostatic interactions, hydrophobic interactions, hydrogen bonds and covalent , and load transfer interactions. The complex three-dimensional structure of the protein macromolecule is the conformation that maximizes stability and minimizes the energy needed to maintain it. In fact, four levels of structure influence a protein structure: three are intramolecular, which exist in the individual polypeptide chains, and the fourth being the intermolecular associations within a molecule of several chains. The principles of protein structure are available in modern biochemistry textbooks, for example: Biochemistry, by Armstrong, F. B., 3a. edition, Oxford University Press, New York, 1989; or Physical Biochemistry, by Freifelder, D., 2a. Edition, W. H. Eruman Company, San Francisco, 1982; o Principles of Protein Structure, Schuitz, GE and Schumer, RH, Sprlnger-Verlag, Berlin, 1979. Protein interactions with surfaces have been studied for decades, focusing primarily on blood-plasma-serum applications and, More recently, the emphasis has been on the so-called biocompatibility field-biomaterials, or medical device implants. This work characterized the solid surface-protein solution interface, and developed a variety of new concepts and new experimental tools for research. Two compilations of this literature are: Principles of Protein Adsorption, in Surface and Interf acial Aspects of Biomedical Polymers, Andrade, J. D. (editor Andrade, J. D.), volume 2, pages 1-80, Plenum Press, New York, 1985; and Protein Adsorption and Materials Biocompatibility: A tutorial Review and Suggested Hypothesis, Andrade, JD and Hlady, V .. Advances in Polymer Science, volume 79, pages 1-63, Springer-Verlag, Berlin-Heidelberg, 1986. A growing source of Information on protein adsorption is present in the current literature, which deals specifically with soils. Studies have established that the same intrinsic interactions and associations within the protein molecule, which are responsible for the three-dimensional structure, also attract and bind proteins to surfaces. Due to their size and complex structure, the proteins contain heterogeneous modules consisting of regions with electrical charge (both negative and positive), hydrophobic regions and hydrophilic polar regions, of analogous nature to similar areas on the surface of food processing equipment that they have traces of residual dirt. In that way the protein can 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 the binding energies in general. Because biological fluids, such as slurry, are complex mixtures, the kinetics of the protein adsorption process is confused, by the concurrent events that occur at interfacial surfaces, within the solution in general and on the surfaces of the equipment. Temperature, pH, populations and protein concentrations and the presence of other inorganic and organic portions have an effect on the dynamics of speed. However, in general, there is a general consensus that protein adsorption is rapid, reversible and is randomly arranged at fractional surface coverage of less than 50%; and the speed is controlled by mass transport, that is, all the adsorption and desorption processes depend on the transportation of the global solute to and from the interface. When the coverage exceeds 50%, a surface ordering is developed and, given a sufficient contact time, the adsorbed proteins undergo changes in conformation and orientation, in order to optimally elevate the interfacial interactions and the stability of the system. Proteins adsorbed less than at the optimal point undergo desorption or change by larger proteins, which have more binding sites. The speed of the process is limited by the surface reaction (controlled mass action). By increasing the residence time, the adsorption of the protein becomes irreversible. Some representative articles that describe the studies of food dirt deposition are: Fouling of Heating Surfaces - Chemical Reaction Fouling Due to Milk, Sandu, C. and Lund, D. in Fouling and Cleaning in Food Processing (Editors Lund, D. , Plett, E. and Sandu, C), pages 122-67, University of Wisconsin-Madison Duplicating Extension, Madison, 1985; and Model Studies of Food Fouling, Gotham, SM, Fryer, PJ and Pritchard, AM, in Fouling and Cleaning in Food Processing, (Kessier editors, H: B. and Lund, DB), pages 1-13, Druckerei Walch, Augsburg , 1989; and Fouling of Milk Proteins and Salts - Reduction of Fouling by Technological Measures, Kessier, H. B., ibid., pages 37-45. The theory suggests that the irreversible adsorption of the protein begins as a tenacious monomolecular layer, tightly bound by interfacial protein-surface forces. Polycaps and protein are then deposited with repeated exposure, linked by coherent protein-protein forces; each layer being progressively weaker in the binding energy, as the distance from the original surface of the substrate increases. Experimental observation and practical experience in milk processing facilities confirms that several dirt-cleaning cycles generally occur before the protein films are visually discernable on the surfaces, manifested by a light blue-brown to dark blue-black discoloration . A precise analytical confirmation can be made by a simple qualitative test of the surface, using the Coomassie bright blue dye, which exists in two color forms: red and blue; quickly turning red to blue when it makes contact with a protein. This protein-dye complex has a high coefficient of extension, which affects the great sensitivity in both the qualitative and quantitative measurement of the protein (see The use of Coomassie Brilliant Blue G250 Perchloric Acid Solution for Staining in Electrophoresis and Isoelectric Focusing on Polyacrylamide Gels, Reisner, AH, Nemes, P. and Bucholtz, C: Analytical Biochemistry, volume 64, pages 509-516 (1975), and A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, Bradford, MM, Analytical Biochemistry, volume 72, pages 248-254 (1976)). As additional layers of protein deposit are deposited one on top of the other, a maximum thickness is probably reached, above which the coherent protein-protein binding forces can be overcome by mechanical, thermal and detergent energies, supplied to the dirt by the program cleaning. This would explain the results of elution experiments, in which surfaces previously contaminated with milk and cleaned, are subjected to a second cleaning process that has greater mechanical, thermal and detergent energies, which can release more protein. However, practical observations have suggested that protein films remain under extreme conditions of the cleanup program.Researchers who have carried out soil removal experiments in the 1950s, with the new concept of recirculating cleaning (called site cleaning or CIP, covering different methodologies) observed the occurrence of protein films on surfaces of the milk processing equipment. Subsequently it was found that the addition of hypochlorite to the CIP alkaline detergent compounds helped to remove the protein film; and this technology has been used until now by suppliers of cleaning compounds for the food processing industry in general. (For example, see Effect of Added Hypochlorite on Detergent Activity of Alkaline Solutions in Recirculation Cleaning, MacGregor, DR Elliker, PR and Richardson GA, Jnl. Of Milk &Food Technology, volume 17, pages 136-138 (1954); Further Studies on In-Place Cleaning, Kauf Ann, OW Andrews, RH and Tracy, PH, Journal of Dairy Science, Volume 38, No. 4, 371-379 (1955), and Formation and Removal of an Iridiscent Discoloration in Cleaned-ln -Plate Pipelines, Kaufmann, OW and Tracy, PH Ibid., Volume 42, pages 1883-1885 (1959) Chlorine degrades the protein by oxidative division and hydrolysis of the peptide ligation, which breaks down large protein molecules into small chains of peptides The conformational structure of the protein disintegrates, dramatically decreasing the binding energies and effecting the desorption of the surface, followed by solubilization or suspension in the cleaning solution.
The use of chlorinated detergent solutions in the food processing industry is not without problems. Corrosion is a constant concern, as is the degradation of polymeric packaging, hoses and artifacts made of polymers. The practice indicates that the available chlorine concentrations should initially be at least 75 ppm and, preferably, 100 ppm for optimal removal of the protein film. At concentrations of available chlorine of less than 50 ppm, the accumulation of protein dirt is increased by the formation of insoluble, adhesive chloro-proteins (see
Cleanability of Milk-Filmed Stainless Steel by Chlorinated Detergent Solutions, Jensen, J.M., Journal of Dairy Science, Volume 53, No. 2, pages 248-251 (1970). It is not easy to maintain chlorine concentrations or discern them analytically in detergent solutions. The dissipation of available chlorine by dirt residues has been well established; and chlorine can form unstable chloramino derivatives with proteins, which are titrated as available chlorine. The effectiveness of chlorine on the elimination of protein dirt decreases as the temperature and pH of the solution decrease; affecting the lower temperatures the reaction rate, and favoring the lower pH the additional chlorinated portions. These problems associated with the use and applications of chlorine releasing agents in the food processing industry have been known and tolerated for decades. Chlorine has improved cleaning efficiency and improved sanitization, resulting in improved product quality. No safe and effective and lower cost alternative has been obtained by detergent manufacturers. However, a new consideration may force change in both the food processing industry and detergent manufacturers: the growing public concern about the impacts of chlorine and organochlorines on health and the environment. Whatever the merits of scientific evidence regarding carcinogenicity, there is little argument that organohalogen compounds are persistent and bioaccumulative; and that many of these compounds have major non-carcinogenic effects on health: endocrine, immunological and neurological problems, mainly in the offspring of exposed humans and exposed wildlife, at extremely low levels of exposure. Therefore, it is prudent for the food processing industry and its detergent suppliers to focus on finding alternatives for the use of chlorine releasing agents in cleaning compositions. There is a substantial need for a release agent of the protein film, which does not contain chlorine, for the detergent compositions having applications in the food processing industry, and which have the versatility to remedy the problems described so far and which remain unresolved nowadays.
Although enzymes were discovered as early as 1830 and their importance triggered intense studies by biochemists, the public record of research into enzyme applications in detergents first occurred in 1915, when German Patent No. 283,923 (May 4) was issued. O. Rohm, founder of Rohm & Haas, for the application of pancreatic enzymes to laundry products. E. Jaag of the Swiss firm Gebrueder Schnyder further developed this concept of the detergent with enzymes during the course of 30 years of work; and in 1959 he introduced to the market a laundry product, Bio 40, which contained a bacterial protease, which had considerable advantages over pancreatic trypsin. However, this bacterial protease was not yet sufficiently stable at the pH of 9-10, of normal use, and had marginal activity on typical spots. Several more years of research went by until, in the mid-sixties, bacterial alkaline proteases, which had all the stability at the necessary pH, and the necessary characteristics of reactivity with the soils, for detergent applications, were commercial. While the use of enzymes in detergent compositions existed previously (see, for example, U.S. Patent No. 1,882,279 to Frelinghuysen, issued October 11, 1932), laundry detergents containing enzyme, on a large commercial scale, they first appeared in the United States market during 1966. Since that time an increasingly narrowly focused number of patents have been issued and reference articles have been published describing detergent compositions containing alkaline protease or mixtures of classes and subclasses of enzymes, generally of proteases, carbohydrases and esterases. The vast majority of these patents are for the purpose of enzyme applications in laundry detergent compositions for consumers, for the pre-soaking or washing cycle, and automatic dishwashing detergents for consumers. A severe examination of this universe of patents describes the evolution of the development of the formula in these product categories, from simple powders containing alkaline protease (see, for example, US Pat. No. 3,451,935 to Roald and co-inventors, issued on 24 June 1969) to more complex granular compositions containing multiple enzymes (see, for example, US Patent No. 3,519,570 to McCarty, issued July 7, 1970); to liquid compositions containing enzyme. The progression from dry to liquid detergent compositions, which contain enzymes, was a natural consequence of the problems inherent with the dry powder forms. Enzyme powders or enzyme granules tend to segregate in these mechanical mixtures, resulting in disuniformity and, therefore, unreliable products in their use. Precautions should be taken with packaging and storage to protect the product against moisture, which caused degradation of the enzyme. Dry powder compositions are not as conveniently suited as liquids for rapid solubility or miscibility in cold or warm water, nor functional as products of direct application to dirty surfaces. For those reasons, and for expanded applications, it became convenient to have liquid enzyme compositions. Economic considerations and also processing considerations suggest the use of water in liquid enzyme compositions. However, there have also been problems inherent in formulating the enzymes in aqueous compositions. Enzymes are generally denatured or degraded in a harassing environment, which results in a serious reduction in, or complete loss of, enzymatic activity. Instability is the result of two mechanisms, at least. The enzymes have a three-dimensional protein structure, which can be changed physically or chemically by other ingredients of the solution, such as surfactants and builders, causing loss of the catalytic effect. Alternatively, when protease is present in the composition, the protease will cause the proteolytic digestion of the other enzymes, if they are not proteases, or of itself, by a process called autolysis. The prior art examples have attempted to solve the problems of enzymatic stability induced by the aqueous solution by minimizing water (see U.S. Patent No. 3,697,451 to Mausner and co-inventors, issued October 10, 1972) or to eliminate the water of the liquid composition containing enzyme (see U.S. Patent 4,753,748 to Lailem and co-inventors, issued June 28, 1988). As described by Mausner and co-inventors, and apparent from Lailem and co-inventors, water is advantageous for dissolving the enzyme (s) and other water-soluble ingredients, such as builders, and carrying them effectively or coupling them into the water. liquid, non-aqueous detergent vehicle to effect a homogeneous isotropic liquid, which will not separate its phases in any other way. In order to commercialize an aqueous enzyme composition, the enzyme must be stabilized, so that it retains its functional activity for prolonged periods of time (shelf life or storage time). If a stabilized enzyme system is not used, an excess enzyme is usually required to compensate for the expected loss. However, enzymes are expensive and, in fact, are the most expensive ingredients in a commercial detergent, even when they are present in relatively minimal quantities. Thus, it is not surprising that methods for stabilizing liquid, aqueous, enzyme-containing detergent compositions are described extensively in the patent literature (see Guilbert, U.S. Patent No. 4,238,345). While the stabilizers used in aqueous, liquid enzyme detergent compositions inhibit the deactivation of the enzyme by chemical intervention, the literature also includes enzyme compositions containing high percentages of water, but either the water or the enzyme or both are immobilized.; or physically separated in another way, to prevent hydrolytic interaction. For examples of an encapsulated aqueous enzyme, formed by extrusion, see U.S. Patent No. 4,087,368 to Borrello, issued May 2, 1978. For examples of an aqueous-based, gel-like enzyme detergent, see U.S. Patent No. No. 5,064,553, Dixit and co-inventors, issued November 12, 1991. For examples of a double component composition, in two packages, where the enzyme is separated from alkalis, builders and sequestrants, see U.S. Pat. 4,243,543, by Guilbert and coauthors, issued January 6, 1981. De Groot and co-inventors, in GB 2 271 120, published in 1994, discloses a formed detergent composition, in which a mutated enzyme is stabilized with a combination of boron and a polyol. In 1985, it was presented at the Second International Conference of Fouling and Cleaning in Food Processing, a document entitled Cleaning Chemicals - State of the Knowledge in 1985, by the authors D. R. Kane and N. E. Middlemiss; editors: Lund, D., Plett, E and Sandu, C; pages 312-335, University of Wisconsin, Madison Duplicating Extension, Madison, 1985, E. U. A.). This document emphasized the CIP (cleanup on site) to clean up in the dairy industry. Within the text of that document, the authors conclude that the use of enzyme in the food-related cleaning industry is not broad for several reasons, including the instability of the enzyme at high pH and over time; at the cost of the enzyme and the enzyme stabilizer; to the concern about the residual enzyme and the adverse effects on the quality of the food, the incompatibility of the enzyme with chlorine, the slow reactivity of the enzyme, which requires long cleaning cycle times, and the lack of justification commercial. The present invention addresses and resolves these drawbacks and problems and provides a useful control method for use in the cleaning composition. The technique contains a prior description of detergent compositions containing enzyme, which have application in food processing equipment. US Patent 4,169,817 to Weber, issued October 2, 1979, describes a liquid cleaning composition containing detergency builders, surfactants, enzyme and stabilizing agent. The compositions claimed by Weber can be used as a laundry detergent, as a laundry soaker or as a general purpose cleaner for dairy processing and cheese making equipment. Weber's detergent solution generally has a pH on the scale of 7.0 to 11.0. The above mentioned teaching incorporates surfactants with high foam production and does not provide detergents that can be used in CIP cleaning systems. U.S. Patent 4,212,761 to Ciaccio, issued July 15, 1980, discloses a composition net or for use in solution, containing a ratio of sodium carbonate and sodium bicarbonate, a surfactant, an alkaline protease and, optionally, tripolyphosphate of sodium. The Ciaccio detergent solution is used to clean dairy equipment, including on-site cleaning methods. The pH of the solution used in Ciaccio varies from 8.5 to 11. Ciaccio does not describe working examples with detergent concentrate modalities. Ciaccio only states that the convenient form of the detergent would be a premixed particle, not a solid block. Of the varieties of ingredients discussed, it becomes obvious to one skilled in the art that such compositions would be too wet, sticky and mud-like, in practice, to be easily marketed. U.S. Patent Nos. 4,238,345 and 4,243,543 to Guilbert, issued January 6, 1981, teach a two-part liquid cleaning system for on-site cleaning applications, where one part is a concentrate consisting essentially of an enzyme proteolytic, enzyme stabilizers, surfactant and water; and the second part is a concentrate consisting of alkalis, builders, sequestrants and water. When both parts are combined at the dilution of use, according to Guilbert, the pH of this use solution will typically be 11 or 12. US Patent No. 5,064,561, issued by Rouillard on November 12, 1991, describes a cleaning system in two parts, for use in on-site cleaning facilities. Part one is a liquid concentrate consisting of a strongly alkaline material (NaOH), a defoamer, a solubilizer or emulsifier, a sequestrant and water. Part two is a liquid concentrate containing an enzyme that is a protease, generally present as a liquid or as a suspension within a non-aqueous carrier, which ordinarily is an alcohol, a surfactant, a polyol or a mixture thereof. The Rouillard use solution generally has a pH of approximately 9.5 to 10.5. Rouillard teaches the use of strongly alkaline materials; and, paradoxically, the optional use of regulators to stabilize the pH of the composition. The Rouillard invention describes compositions in which the unstable aqueous mixtures of inorganic salts and organic defoamer are necessarily coupled by the inclusion of a solubilizer or emulsifier, to maintain an isotropic liquid concentrate. Rouillard further teaches that the defoamer may not always be necessary, if a liquid form (the term should be taken as "aqueous, stabilized") of the enzyme, is used in the second concentrate. That description would seem to be the result of the use of Esperase 8.0 SL, identified as a useful source of enzyme in the practice of the invention, and used in the working examples. Other details indicate that Esperase 8.0 SL is a proteolytic enzyme suspended in Tergitol 15-S-9, a surfactant with high foam production (hence the need for a defoamer and a solubilizer or emulsifier). Rouillard additionally describes that the proteolytic enzyme (Esperase 8.0 L) by itself does not clean as effectively as a chlorinated, strongly alkaline detergent, unless it is mixed with its co-operating alkaline concentrate. As discussed in WO 97/02753, issued to Olsen, on-site cleaning (CIP) involves circulating non-foaming detergents or with low foam production, through the process equipment, in an assembled state. A typical CIP sequence can consist of the following five stages (see Hygiene for
Management, by R. A. Sprenger, 5a. edition, page 135): 1. Pre-rinse with cold water to remove coarse dirt;
2. Circulation of detergent to eliminate detritus and adherent, residual incrustations; 3. Intermediate rinse with cold water to remove all traces of detergents; 4. Circulation of disinfectant to destroy the remaining microorganisms; and 5. Final rinse with cold water to remove all traces of disinfectants. U.S. Patent No. 4,858,449, issued to
Lehn, teaches the use of dispensers, which dispense alkaline, solid chemicals, used in cleaning processes that control the amount of chemical substance supplied, periodically measuring the conductivity of the concentrated chemical solution. That invention periodically measures the conductivity of the accompanying solution in order to determine the amount of solution that has been dispensed. Several chemical substances can be used, as long as the conductivity of the solutions can be correlated with their concentration. U.S. Patent 4,211,517, issued to Schmid, describes the use of pH measurement to determine conductivity. U.S. Patent No. 4,845,965, issued to Copeland and co-inventors, discloses the use of a conductivity sensor that is used to control the supply of multiple alkaline cleaning solutions to one or more laundry machines, preferably using a single laundry system. supply. The conductivity sensor is used to monitor the concentration of the concentrated detergent solution. U.S. Patent 4,826,661, also issued to Copeland and co-inventors, teaches the preparation of a concentrated cleaning solution by contacting a solid block cleaning composition with the liquid that dissolves it. U.S. Patent 4,690,305, issued to
Copeland and co-inventors, describes a washing chemical dispenser, for dispensing an alkaline, concentrated chemical solution, by contacting a solid block with an aqueous liquid. WO 97/02753, issued to Olsen, refers to an enzymatic method for on-site cleaning of self-processing equipment, in particular, to trace processing equipment. The invention describes a method for cleaning on site processing equipment, comprising circulating a solution comprising a protease and a lipase for a sufficient time to allow the action of the enzymes. WO 96/41859, issued to Nielsen, refers to a liquid composition, in particular to a liquid detergent composition, comprising an enzyme and an improved enzyme stabilizer. The "enzyme stabilizers in that patent are generally phenylboronic acid derivatives." WO 93/21299, issued to Marshall and co-inventors, refers to a detergent composition for automatic dishwashing machine, which is substantially free of chlorine and silicate bleach. The automatic dishwashing machine composition contains enzyme, an enzyme stabilizer and detergent surfactant or builder system, WO 97/07190, issued to Rouillard, teaches the use of enzymatic detergents, low in alkaline substances, in powder form, packaged in portions, to clean dairy pipes in a dairy facility.
BRIEF DESCRIPTION OF THE INVENTION
This invention describes formulations comprising enzyme, borate, carbohydrate, etc., in solid form. Other methods of manufacture and methods of use for compositions are described which have application as detergents in the food processing industry. A method that controls the concentration of enzyme with conductivity has also been discovered. Said compositions are used to clean surfaces soiled by food. The materials are made in concentrated form. The diluted concentrate, when supplied to the target surfaces, will give its cleaning. The concentrated product is a solid. Concentrated products that are manufactured by any of numerous solid mixing methods known in the art include pouring, casting, compression molding, extrusion molding, or similar form packing operations. The preferred embodiment comprises the use of extrusion to create the solid block detergent. These products are designed for on-site cleaning cleansing regimes (CIPs) in the food processing industries, such as a dairy plant and a dairy farm; fluid byproducts of milk and processed milk. More specifically, the present invention describes detergent compositions which generally contain enzymes, surfactants and sequestrants. The claimed compositions eliminate the need for strongly alkaline builders, secondary defoamers, corrosion inhibitors and chlorine releasing agents. Consequently, the claimed compositions are safer in their use and the resulting effluent is friendly to the environment. When used, the claimed composition will continue to clean soiled food processing equipment surfaces, equal to or better than current, strongly alkaline, chlorinated, conventional detergents. Preferred methods have also been found for cleaning protein-containing food processing units. In preferred methods of the invention, 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. Optionally, before contacting the food processing surface with the detergent, the unit can be pre-rinsed with an aqueous rinse composition to remove coarse dirt from food. The protein residue present in the food processing unit is contacted with a detergent of the invention, for a sufficient time to remove the protein film. It can be denatured using a variety of techniques, any protease enzyme residue remaining on the surfaces of the unit or otherwise within the food processing unit. The food processing unit can be heated with a thermal source comprising steam, hot water, etc., above the denaturation temperature of the enzyme protease. Typically, the required temperatures vary between about 60-90 ° C, preferably about 60-80 ° C. Additionally, the residual protease enzyme remaining in the food processing unit can be denatured by exposing the enzyme to an extreme pH. Typically, it is sufficient to denature the enzyme a pH greater than about 10, preferably greater than about 11 (alkaline pH) or less than 5, preferably less than about 4 (acid pH). Additionally, the protease can be denatured by exposing any residual protease enzyme to the effects of an oxidizing agent. A variety of known oxidizing agents that also have the benefit of acting as an acceptable sanitizer for foods, include: aqueous hydrogen peroxide, ozone-containing aqueous compositions, peroxyacid aqueous compositions, wherein the peroxyacid comprises a monocarboxylic or dicarboxylic acid composition. to 24 carbon atoms. Additionally, iodophors or interhalogen complexes (ICI, CIBr, etc.) can be used to denature the enzyme, if used in accordance with accepted procedures. The denatured enzyme remaining in the system after the denaturation step may have little or no effect on any proteinaceous food. The quality of the resulting product does not vary. Preferred foods, treated in food processing units that have a denaturing step after the cleaning step, include milk and milk products; beer and other fermented malt beverages, puddings, soups, yogurt or any other liquid food material, thickened or semi-solid liquid containing protein. The objectives of this invention, therefore, are the following: 1. provide the food processing industry and operations related to environmental hygiene, a cleaning system for on-site cleaning, with detergent of low alkaline substances, without chlorine; 2. satisfy a commercial need for cost-effective detergents, friendly to the user and less intrusive to the environment. 3. and resolve objections to the use of detergent enzymes for cleaning in food processing environments, which are sensitive to enzyme residues, by teaching cooperative cleaning and sanitizing programs, which ensure complete deactivation of the enzyme before of contact with food.
BRIEF DESCRIPTION OF THE DRAWING
Figure 1 is a graphical representation of the stability of the residual enzyme activity data for various test formulations.
DETAILED DESCRIPTION OF THE INVENTION
The invention comprises a composition of use solution, for dilution of use, which has exceptional detergency properties when applied as a cleaning treatment to surfaces of equipment contaminated with food, and which have particular cleaning efficiency, on tough films of protein . Preferred embodiments of the invention give cleaning performance superior to highly alkaline, chlorine-containing conventional detergents, and is directed in particular to the dairy industry, where milk proteins are involved. The present invention generally comprises in a solid or solid block formulation, low foam production, free of alkali metal hydroxide, or a source of active chlorine: 1. an enzyme or a mixture of enzymes; 2. an alkali metal borate composition, which acts as an enzyme stabilizer system; 3. a carbohydrate compound; _ 4. a sequestrant; 5. water A preferred embodiment of the present invention is a detergent system comprising a solid, stabilized block detergent, which is made by solidifying a premix of liquid detergent with borate alone or together with other solidifying agents. The premix contains a source of liquid protease enzyme, an optional surfactant and a sequestrant. The other so-called 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. It is an important aspect the use of borate for multiple functions: stabilization of the enzyme, solidification, source of alkalinity and regulatory agent (with a pKa of 9.1). It has been found that solid enzyme-containing detergents, stabilized by the stabilizing compounds of the invention can be further improved by using a borate stabilizing material. The combination of an alkali metal borate with the vicinal hydrocarbon stabilizer compositions of the invention produces increased stability. The chemistry of boric acid, like many other chemicals, is complex and contains many simple and complex compounds. Mixtures of B (OH) 3 and B (OH) 4"1 appear in classical regulatory systems, which depend on pH, sodium borate, potassium borate, disodium tetraborate, disodium tetraborate pentahydrate, disodium tetraborate, etc., in the stabilized materials of this invention It has been found that borate compounds, alone and combined with a carbohydrate compound having vicinal hydroxyl groups, can act as stabilizing agents for the enzyme materials. use alkali metal salts of boric acid or more complex borates (boric acid oligomers including both linear and cyclic borate materials) Preferred materials are species such as Na2O.B4O .XH2O, disodium tetraborate pentahydrate, tetraborate decahydrate of disodium, anhydrous borax, sodium pentaborate decahydrate, sodium metaborate octahydrate, sodium metaborate tetrahydrate and others. borax and borax pentahydrate by extraction of dry lake brines and other natural sources. The enzyme stabilizer compositions of the invention may also include an organic compound of 4 carbon atoms, with at least two vicinal hydroxyl groups, corresponding to the following formula:
OH OH • C - C - where the empty bonds correspond to carbon, oxygen, hydrogen, sulfur, nitrogen or other atoms common in the stabilizing compounds available. The simplest examples are glycerin derivatives, such as the lower alkyl monoesters of glycerin and the ethers, including glyceryl monostearate, glyceryl monooleate, glyceryl monoethyl ether, glyceryl diethyl ether, etc.; 2,3-dihydrobutiraldehyde and other organic compounds with more than 4 carbon atoms, which have vicinal hydroxyl. A preferred class of stabilizers is monosaccharides, which include the compounds: aldot'etrose, aldopentose, aldohexose, aldoheptose, aldooctose, ketotetrosa, ketopentose, ketohexose, etc. Said compounds include: erythrose, ribose, glucose, mannose, galactose; isomers and derivatives thereof and other similar monosaccharides. Additionally useful are disaccharide compounds which include: sucrose, lactose, cellobiose, maltose. The present invention relates to a CIP system in which the stabilized enzyme is used to remove milk proteins from milk processing equipment. Additionally, 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 the possibility of cleaning with enzymes. Consequently, the cleaning solution is less alkaline and uses less water. Because chlorine is not used, there are fewer corrosivity problems.
THE ENZYMES
Enzymes are important and essential components of biological systems; Its function is to catalyze and facilitate organic and inorganic reactions. For example, enzymes are essential for metabolic reactions that occur in animal and plant life. The enzymes of the invention are simple proteins or conjugated proteins, produced by living organisms, and which function as biochemical catalysts that, in the technology of detergents, degrade or alter one or more types of the dirt residues found on the surfaces of the food processor equipment, thereby eliminating dirt or making dirt more removable by the detergent cleaning system. Both the degradation and the alteration of dirt residues improve the detergency, reducing the physicochemical forces that bind the dirt to the surface that is being cleaned, that is, the dirt becomes more soluble in water. As defined in the art, enzymes are known 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 their activity, called cofactor, which is a metallic or organic biomolecule, often called a coenzyme. The cofactors are not involved in the catalytic events of the enzymatic function. Rather its role seems to be to keep the enzyme in an active configuration. As used herein, "enzyme activity" refers to the ability of an enzyme to effect the desired catalytic function of degradation or alteration of dirt, and enzyme stability refers to the ability of an enzyme to remain or be maintained in an active state. . Enzymes are extremely effective catalysts. In practice, very small quantities will accelerate the rate of degradation of dirt and the reactions of alteration of dirt, without being consumed in the process. Enzymes also have substrate specificity (dirt), which determines the amplitude of their catalytic effect. Some enzymes interact only with a specific substrate molecule (absolute specificity); while other enzymes have broad specificity and catalyze reactions in a family of structurally similar molecules (group specificity). The enzymes exhibit catalytic activity by virtue of three general characteristics: the formation of a non-covalent complex with the substrate; Substrate specificity, and catalytic velocity. Many compounds can bind to an enzyme, but only certain types will lead to a subsequent reaction. The latter are called substrates and satisfy the specific enzyme specificity requirement. Materials that bind, but do not react chemically after that, can affect the enzymatic reaction either positively or negatively. For example, unreacted species, called inhibitors, interrupt enzymatic activity. Enzymes that degrade or alter one or more types of dirt, that is, that increase or help eliminate the dirt from the surfaces to be cleaned, are identified and can be grouped into six main classes, based on the types of chemical reactions that catalyze these processes of degradation and alteration. Those classes are: (1) oxidoreductase; (2) transferase; (3) hydrolase; (4) Nasa; (5) isomerase; and (6), ligase. Several enzymes can enter more than one class. A valuable reference on enzymes is Industrial Enzymes, Scott, D., in Kirk-Othmer Encyclopedia of Chemical Technology, 3a. edition
(editors Grayson, M. and EcKroth, D.), volume 9, pages 173-224; John
Wiley & Sons, New York, 1980. In summary, oxidoreductases, hydrolases, liasses and iigasas degrade dirt residues, thus eliminating dirt or making dirt more removable.; and transferases and isomerases alter soil debris with the same effect. Of these classes of enzymes, hydrolases (which include esterase, carbohydrase or protease) are particularly preferred for the present invention. Hydrolases catalyze the addition of water to the dirt with which they interact, and generally cause degradation or breakdown of that dirt residue. This decomposition of the dirt residue is of particular and practical importance in detergent applications, because the dirt adhering to the surfaces is loosened and eliminated or made more easily removable by detergent action. Thus, hydrolases are the most preferred class of enzymes for use in cleaning compositions. Preferred hydrolases are esterases, carbohydrases and proteases. The most preferred sub-class of hydrolases for the present invention is that of proteases.
Proteases catalyze the hydrolysis of the peptide-binding bond of amino acid polymers, including peptides, polypeptides, proteins and related substances (generally protein complexes) such as casein containing carbohydrate (glycol group) and phosphorus, as integral parts of the protein, and exist as distinct globular particles, held together by calcium phosphate; or as a milk globulin that can be said to be a sandwich of protein and lipids, which comprise the milk fat globule membrane. Thus, proteases divide the macromolecular, complex protein structures present in the dirt residues, to simpler short chain molecules that, by themselves, are easily desorbed from the surfaces, solubilized or more easily eliminated in another way, by means of detergent solutions containing said proteases. The proteases, a subclass of the hydrolases, are further divided into three distinct groups, which are grouped according to the optimum pH (ie, the optimal enzymatic activity for a given pH scale). These three subgroups are the alkaline proteases, the neutral ones and the acid ones. These proteases can be of vegetable, animal or microorganism origin; but preferably they are of the latter origin, which includes yeasts, molds and bacteria. Particularly preferred for the embodiments of this invention are bacterial alkaline proteolytic enzymes, active for serine, obtained from alkalophilic Bacillus strains, especially Bacillus subtilis and Bacillus licheniformis. Purified or unpurified forms of these enzymes can be used. Proteolytic enzymes produced by chemically or genetically modified mutants are included herein by definition, since they are intimate structural variants of the enzyme. These alkaline proteases are not generally inhibited by metal chelating agents (sequestrants) nor thiol poisons them, nor are they activated by metal ions or by reducing agents. All have relatively broad substrate specificities; are inhibited by diisopropylfluorophosphate (DFP), all are endopeptidases, generally have molecular weights on the scale of 20,000 to 40,000, and are active on the pH scale of about 6 to about 12 and on the approximate temperature scale of 20 ° C at 80 ° C. Examples of suitable commercially available alkaline proteases are: Alcalase®, Savinase® and Esperase®, all from Novo Industri AS, Denmark; Purafect® by Genencor International; Maxacal®, Maxapem® and Maxatase®, all from Gist-Brocades International NV, The Netherlands; Optimase® and Opticlean® by Solvay Enzymes, E. U. A., etc. Commercial alkaline proteases can be obtained in liquid form or in dry form; they are sold as raw aqueous solutions or in purified, processed and compound, varied forms; and comprise about 2% to 80% by weight of active enzyme, generally in combination with stabilizers, regulators, cofactors, impurities and inert carriers. The actual content of active enzyme depends on the manufacturing method and is not critical, as long as the detergent solution has the desired enzymatic activity. The particular enzyme selected for use in the process and the products of this invention, depends on the conditions of ultimate utility, including the physical form of the product, the pH of use, the temperature of use, the types of dirt that will be degraded or altered. The enzyme can be selected to provide optimal activity and stability for any desired series of utility conditions. For example, Purafect® is a preferred alkaline protease for use in detergent compositions of this invention, which have application in low temperature cleaning programs (approximately 30 ° C to 65 ° C), while Esperase® is the alkaline protease of selection for high temperature detergent solutions, approximately 50 ° C to 85 ° C. In the preferred embodiments of this invention, the amount of commercial alkaline protease mixed composition, present in the final use dilution, or the use solution, varies from about 0.001% (10 ppm) by weight of the detergent solution, to about 0.02% (200 ppm) by weight of the solution, of the commercial enzyme product, typically containing 5 to 10% of active enzyme. Although it is a practical convenience to establish the percentage by weight of commercial alkaline protease necessary, for the manufacturing modalities of the present, the variation in the commercial protease concentrates and the additive and negative environmental effects in situ, on the activity of the protease , require an analytical technique that better discerns the protease analysis to quantify the activity of the enzyme and establish the correlations of elimination performance of dirt residue, and for the stability of the enzyme within the preferred modality; and, if it is a concentrate, use dilution solutions. The activity of the alkaline proteases of the present invention is easily expressed in terms of activity units; more specifically, Kilounidades de proteasa Novo (KNPU, acronym for its English designation: Kilo-Novo Protease Units), which are units of azocasein analysis activity, well known in the art. A more detailed discussion of the azocasein analysis procedure can be found in the publication entitled The Use of Azoalbumin as a Substrate in the Colorimetric Determination of Peptic and Tripic Activity, Tomarelli, RM, Charney, J. and Harding, ML, J. Lab. Clin. Chem., 34, 428 (1949), incorporated herein by this reference. In the preferred embodiments of the present invention the activity of proteases in the use solution varies between about 1 x 10"5 KNPU / g of solution, up to about 4 x 10" 3 KNPU / g of solution. Naturally, mixtures of different proteolytic enzymes can be incorporated into this invention. While several specific enzymes have been described above, it should be understood that any protease that can confer the desired proteolytic activity to the composition can be used, and this embodiment of the present invention is not limited, in any way, by the specific selection of the Proteolytic enzyme. It should be understood that, in addition to proteases, whoever is skilled in the art will see from the above enumeration that other enzymes that are well known in the art can also be used, with the composition of the invention. Other hydrolases are included, such as esterases, carboxylases and the like; and other kinds of enzyme. In addition, in order to increase its stability, the enzyme or a mixture of enzymes can be incorporated, in various non-liquid embodiments of the present invention, such as in coated, encapsulated, agglomerated, lumpy or elongated bodies.
THE ENZYME STABILIZER SYSTEM
The enzyme stabilizer system of the present invention consists of sodium borate, sucrose, milk or a combination of them. It seems obvious to conclude that this enzyme stabilizer system would provide a certain degree of stabilizing effect for the activity of the enzyme at all levels. free and bound water levels, which exist in the liquid detergent composition with enzyme, typically around 1% to 99% by weight of water. It has been found that the incorporation of the preferred enzyme stabilizer system has a pronounced beneficial effect on the alkaline protease cleaning performance, ie, increased removal of protein film, in dilution solutions of use. Normally there is no description, teaching or suggestion in the technique when they are used for maintenance of the storage life of the enzymatic activity within the product concentrate, which suggests that the enzyme stabilizer systems contribute to, or have some cooperative action expected with, the enzymatic activity or a functional improvement manifested in the cleaning, within detergent environments of the dilution solution of use. The enzyme stabilizer compositions of the invention include an organic compound of more than four carbon atoms, with at least two vicinal hydroxyl groups, corresponding to the following formula:
OH OH
I I c - c - where the empty bonds correspond to atoms of carbon, oxygen, hydrogen, sulfur, nitrogen or other atoms common in the available stabilizing compounds. The simplest examples are the glycerin derivatives, such as the lower alkyl monoesters of glycerin and the ethers, including glyceryl monostearate, glyceryl monooleate, glyceryl monoethyl ether, glyceryl diethyl ether, etc .; 2,3-dihydrobutiraldehyde and other organic compounds with more than 4 carbon atoms, which have vicinal hydroxyl. A preferred class of reversal inhibitors is the monosaccharides, which include the compounds: aldotetrose, aldopentose, aldohexose, aldoheptose, aldooctose, ketotetrosa, ketopentose, ketohexose, etc. Said compounds include: erythrose, ribose, glucose, mannose, galactose; isomers and derivatives thereof and other similar monosaccharides. Additionally useful are disaccharide compounds which include: sucrose, lactose, cellobiose, maltose. The stabilizing, solidifying, etc. agent of the invention can include any metal borate. It has also been discovered that 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 the more complex borates (boric acid oligomers including both linear and cyclic borate materials) can be used. Preferred materials are species such as Na2B4O7.XH2; Na2O.B4O6.XH2O or Na2O.B2O3.XH2O etc .; wherein X is about 0 to 12, including: disodium tetraborate decahydrate, disodium tetraborate pentahydrate, anhydrous borax, sodium pentaborate decahydrate, sodium metaborate octahydrate, sodium metaborate tetrahydrate and others.
Borax (anhydrous), borax decahydrate and borax pentahydrate are produced by extraction and drying of dry lake brines and other natural sources. Additionally, there is no description, teaching or suggestion in the art that enzyme stabilizing systems demonstrate this synergistic, cooperating effect at high temperatures that otherwise are destructive of enzymes or make them thermolabile.
THE SURGICAL AGENT
The surfactant or mixture of surfactants of the present invention may be selected from nonionic, non-ionic semipolar, anionic, cationic, amphoteric or zwitterionic surfactants., soluble in water or dispersible in water, or any combination of them. The particular surfactant or the particular mixture of surfactants, selected for use in the process and the products of the invention, depend on the conditions of ultimate utility, including the method of manufacture, the physical form of the product, the pH of use, the temperature of use, the control of foam and the type of dirt. The surfactants incorporated in the present invention must be compatible with the enzyme and be free of enzymatically reactive species. For example, when proteases and amylases are employed, the surfactant must be free of peptide and glycosidic ligands, respectively. Care should be taken when including cationic surfactants, because there are reports of some decrease in the effectiveness of the enzyme. The preferred surfactant system of the invention is selected from nonionic or anionic surfactant species, or mixtures of each of these types or both. Nonionic and anionic surfactants offer diverse commercial selections including, and low price; and very importantly, excellent detergents effect, which means surface moistening, penetration into dirt and removal of dirt from the surface being cleaned, as well as suspension of dirt in the detergent solution. This preference does not teach the exclusion of utility for cationic surfactants or for the subclass of the nonionic semi-polar non-ionic surfactants, nor for those surfactants which are characterized by persistent double-ion, cationic and anion behavior, thus deferring from the classic amphoteric surfactants, and which are classified as hybrid ion surfactants. One of ordinary skill in the art will understand that the inclusion of cationic, non-ionic, semi-polar or zwitterionic surfactants, or mixtures thereof, will impart beneficial and / or differentiating utility to various embodiments of the present invention. As an example, foam stabilization for detergent compositions intended to be foamed on equipment or floor surfaces, walls and ceilings; or the development of gel for products dispensed as a thin sticky gel on dirty surfaces; or for antimicrobial preservation, or for prevention of corrosion, etc. The most preferred surfactant system, in the present invention, is selected from nonionic or anionic surfactants, or from mixtures of each or both, which impart low foam production to the solution for use in dilution of use of the detergent compositions, during the application. It is preferred that the surfactant or the individual surfactants participating in the surfactant mixture by themselves be low foaming within normal usage concentrations, and within the operating application parameters of the detergent composition and of the cleaning program. However, in practice, there is an advantage in mixing low foam surfactants with the higher foaming surfactants, because the latter often impart superior detergent properties to the detergent composition. Mixtures of non-ionic low and high foam production, non-ionic
• Low production of foam and anionic high foam production, in the present invention, if the foam profile of the combination is of low foam production under the conditions of normal use. Thus, judiciously non-ionic and anionic high foam production can be employed, without departing from the spirit of this invention. The particularly preferred concentrate modalities of this invention are designed for CIP (on-site cleaning) cleaning systems, within food processing facilities and, most particularly for dairy farms and producers of milk and fluid dairy by-products. The foam is the main concern in those systems of recirculation by pump, strongly agitated, during the cleaning program. Excessive foam reduces the flow rate, causes cavitation in the recirculation pumps, inhibits the contact of the detergent solution with dirty surfaces and prolongs drainage. Such occurrences during CIP operations adversely affect cleaning performance and sanitation efficiencies. Therefore, the low foam production is a descriptive characteristic of the detergent, broadly defined as a quantity of foam that does not manifest any of the problems listed above when the detergent is incorporated in the cleaning program of a CIP system. Because the ideal is no foam, the question is to determine what is the maximum level or the maximum amount of foam that can be tolerated within the CIP system without causing the mechanical alteration or observable detergent; and then only market formulas with foam profiles at least below that maximum, to ensure optimal detergent operation and optimum operation of the CIP system. Acceptable foam levels in CIP systems have been determined empirically in practice by iterative methods. Obviously there are currently commercial products that fill the profile of low foam production necessary for the operation of the CIP. Therefore, it is a relatively simple task to employ such commercial products as standards for comparison and to establish laboratory devices for the evaluation of foam, and test methods that simulate, or better, duplicate, the conditions of the CIP program, ie , the parameters of agitation, temperature and concentration. In practice, the present invention allows the incorporation of high concentrations of surfactant, in comparison with conventional, chlorinated, highly alkaline CIP and COP cleaners. Certain surfactants or certain mixtures of surfactants of the invention are generally not physically compatible or chemically stable with conventional alkali and chlorine. This great differentiation of the technique makes necessary not only a careful analysis of the foam profile of the surfactants that are included within the compositions of the invention, but also demands a critical scrutiny of their detergent properties in the elimination and suspension of the dirt. The present invention is based on the surfactant system for the removal of coarse dirt from surfaces of equipment and for the suspension of dirt in the detergent solution. The suspension of dirt is a property of surfactant so important in CIP detergent systems as the removal of dirt, to prevent the redeposition of dirt on cleaned surfaces during recirculation and, subsequently, during reuse in CIP systems that store and reuse the same detergent solution for several cleaning cycles. In general, the concentration of surfactant or mixture of surfactants, useful in the use dilution use solutions of the present invention, ranges from about 0.02% (20 ppm) by weight to 0.1% (1000 ppm) by weight , preferably about 0.005% (50 ppm) by weight to 0.075% (750 ppm) by weight; and most preferably, about 0.008% (80 ppm) by weight to 0.05% (500 ppm) by weight. The 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 percentage by weight in the total formula of the composition which contains enzyme. A typical listing of the classes and species of surfactants useful herein appears in US Patent 3,664,961, issued May 23, 1972 to Norris, incorporated herein by this reference. Nonionic Surfactants, published by Schick, MJ, volume 1 of the Surfactant Science Series series, Marcel Dekker, Inc., New York, 1983, is an excellent reference for the wide variety of nonionic compounds generally employed in the practice of the present invention. . The 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 condensation of an aliphatic, alkylaromatic or polyoxyalkylenic hydrophobic compound, with a hydrophilic portion of alkaline oxide , which in common practice is ethylene oxide or a polyhydration product thereof, polyethylene glycol. Virtually 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 mixtures thereof with alkoxylenes, such as propylene oxide, to form a nonionic surfactant. The length of the polyoxyalkylene hydrophilic portion, which is condensed with any particular hydrophobic compound, can be easily adjusted to produce a water-soluble or water-dispersible compound having the desired degree of balance between the hydrophilic and hydrophobic properties. The nonionic surfactants useful in the present invention include: 1. Polyoxypropylene-polyoxyethylene block polymer compounds, based on propylene glycol, ethylene glycol, glycerol, trimethylolpropane and ethylenediamine as a reactive hydrogen reactant compound. Examples of polymeric compounds made from sequential propoxylation and ethoxylation of the initiator are commercially available under the trademarks Pluronic® and Tetronic®, manufactured by BASF Corp. Pluronic® compounds are difunctional compounds (two reactive hydrogens) formed by condensing oxide of ethylene 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 approximately 1,000 to 4,000. Ethylene oxide is then added to sandwich this hydrophobe between two hydrophilic groups, controlled in their length to constitute approximately 10% by weight to 80% by weight of the final molecule. Tetronic® compounds are tetrafunctional block copolymers, derived from the sequential addition of propylene oxide and ethylene oxide to ethylenediamine. The molecular weight of the propylene oxide hydrotype varies from about 500 to 7,000; and the hydrophilic ethylene oxide is added to make up about 10% by weight to 80% by weight of the molecule. 2. The condensation products of one mole of alkylphenol, wherein the alkyl chain, with straight chain or branched chain configuration, of the single or double alkyl constituent, contains about 8 to 18 carbon atoms, with about 3 to about 50 moles of ethylene oxide. For example, the alkyl group may be represented by diisobutylene, diamyl, polymerized propylene, isooctyl, nonyl and dinonyl. Examples of commercial compounds of this chemistry are available on the market, under the Igepal® brands, manufactured by Rhone-Poulenc and Triton®, manufactured by Union Carbide. 3.- Condensation products of one mole of a saturated or unsaturated alcohol, straight or branched chain, having approximately 6 to 24 carbon atoms, with about 3 to 50 moles of ethylene oxide. The alcohol moiety may consist of blends of alcohols on the carbon scale delineated above, or may consist of an alcohol having a specific number of carbon atoms, within this scale. Examples of commercial surfactant of this type are available under the trademark Neodol®, manufactured by Shell Chemical Co., and Alfonic®, manufactured by Vista Chemical Co. 4.- Condensation products of one mole of saturated or unsaturated carboxylic acid, straight or branched chain, having about 8 to 18 carbon atoms with about 6 to 50 moles of ethylene oxide. The acid portion may consist of mixtures of acids in the above-defined scale of carbon atoms, or it may consist of an acid having a specific number of carbon atoms, within the scale. Examples of commercial compounds of this chemistry are commercially available under the trademarks Nopalcol®, manufactured by Henkel Corporation and Lipopeg®, manufactured by Lipo Chemicals, Inc. In addition to the ethoxylated carboxylic acids, commonly referred to as polyethylene glycol esters, other esters of Alkanoic acid, formed by reaction with glycerides, glycerin and polyhydric alcohols (saccharide or sorbitan / sorbitol) have application in this invention for specialized modalities, particularly in indirect additive applications for foods. All these ester portions have one or more sites of reactive hydrogen in their molecule, which may undergo additional acylation, or addition of ethylene oxide (alkoxide) to control the hydrophilicity of those substances. Care should be taken when adding these fatty esters or acylated carbohydrates to the compositions of the present invention which contain amylase and / or lipase enzymes, due to their potential incompatibility. Preference is given to low-foaming alkoxylated nonionics, although other alkoxylated nonionics with higher foam production can be used without departing from the spirit of this invention, if used in conjunction with low foaming agents, in order to control the foam profile of the mixture within the detergent composition, in its entirety. Examples of low foam production nonionic surfactants include: 5. Compounds of (1) which are modified, essentially inverted, by adding ethylene oxide to ethylene glycol, to give a hydrophilic of designated molecular weight and then adding propylene oxide to obtain hydrophobic blocks on the outside (ends) of the molecule. The hydrophobic portion of the molecule weighs about 1,000 to 3,100, the central hydrophilic comprising 10% by weight to about 80% by weight of the final molecule. These reverse Pluronics® are manufactured by BASF Corporation under the trademark Pluronic® R surfactants. Likewise Tetronic® 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 approximately 2,100 to 6,700, the hydrophilic comprising 10% by weight to 80%) by weight of the final molecule. 6.- Compounds of groups (1), (2), (3) and (4) that are modified by "coronation" or "end blocking" of the terminal hydroxy group or groups (of multifunctional portions) to reduce foaming by reaction with a small hydrophobic molecule, such as propylene oxide, butylene oxide, benzyl chloride; and fatty acids, alcohols or alkyl halides, of short chain, containing from 1 to about 5 carbon atoms; and its mixtures. Also included are reagents such as thionyl chloride, which converts the terminal hydroxy groups to a chloride group. Said modifications to the terminal hydroxy group can lead to non-ionic all-block, block-heteric, hetérico-bloque or totally hetereric. 7. Further examples of effective low-foam nonionics include: The alkylphenoxypolyethoxyalkanols of US Pat. No. 2,903,486, issued September 8, 1959 to Brown and co-inventors, incorporated herein by reference, represented by the formula:
wherein 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 from 7 to 16 and m is an integer from 1 to 10. The polyalkylene glycol condensates of U.S. Patent No. 3,048,548, issued August 7, 1962 to Martin and coauthors, incorporated herein by this reference, having chains Hydrophilic oxyethylene and hydrophobic oxypropylene chains, wherein the weight of the terminal hydrophobic chains, the weight of the intermediate hydrophobic unit and the weight of the hydrophilic linker units each represent approximately one third of the condensate. The nonionic surfactants defoamers, described in US Pat. No. 3,382,178, issued May 7, 1968 to Lissant and co-inventors, incorporated herein by this reference, having the general formula Z [(OR) nOH] z, wherein Z is material alkoxylabie, R is a radical derived from an alkylene oxide, which may be ethylene and propylene, and n is an integer, for example, from 10 to 2,000 or more; and z is an integer determined by the number of reactive oxyalkylatable groups.
The conjugated polyoxyalkylene compounds, described in U.S. Patent No. 2,677,700, issued May 4, 1954 to Jackson and coauthors, incorporated herein by this reference, corresponding to the formula Y (C3H6O) n (C2H4O) mH, where Y is the residue of organic compound having about 1 to 6 carbon atoms and one reactive hydrogen atom; n has an average value of at least about 6.4, when determined by the hydroxyl number; and m has a value such that the oxyethylene portion constitutes approximately 10% to 90% by weight of the molecule. The conjugated chickenxyalkylene compounds described in U.S. Patent No. 2,674,619, issued April 6, 1954 to Lundsted and co-inventors, incorporated herein by this reference, having the formula U [(C3H6On (C2H4o) rtlH] x, where Y is the residue of an organic compound having approximately 2 to 6 carbon atoms and containing x reactive hydrogen atoms, where x has a value of at least about 2; n has a value such that the molecular weight of the base Hydrophobic polyoxypropylene is at least about 900 μm and has a value such that the oxyethylene content of the molecule is about 10% to 90% by weight Compounds that fall within this scope of definition for Y include, for example: propylene glycol, glycerin, pentaerythritol, trimethylolpropane, ethylenediamine and the like The oxypropylene chains, optionally but advantageously, contain small amounts of ethylene oxide and the oxyethylene chains They also contain, optionally but advantageously, small amounts of propylene oxide. Advantageously, additional conjugated polyoxyalkylene surfactants are used in the compositions of this invention, corresponding to the formula P [(C3H6O) n (C2H4o) mH] x, where P is the residue of an organic compound having approximately 8 to 18 carbon atoms and containing x reactive hydrogen atoms; where 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 such a value, that the oxypropylene content of the molecule is about 10% to 90% by weight. In any case, the oxypropylene chains may optionally but advantageously contain small amounts of ethylene oxide, and the oxyethylene chains may also optionally but advantageously contain small amounts of propylene oxide. Examples of commercial surfactants, especially preferred, are listed in Table II:
TABLE II
EXAMPLES OF COMMERCIAL, FAVORITE NON-IONICS
General structure Examples AP- (EO) x- (PO) yH Triton® CF-21 C8P (EO) 9 5 (PO) 5H Alcohol- (EO)? - (PO) yH Sulfonic® JL-80X C9.11 (EO) ) 9 (PO) 1.2H Alcohol- (PO) x- (EO) yH Poly-Tergent® SL- = 42, C8.10 (PO) 3 (EO) 5H Alcohol- (PO) x- (EO) y- (PO2H Poly-Tergent® SLF-18, C8.10 (PO) 16.17 (EO) 12 (PO) 1.2H Alcohol- (PO) x- (EO) y-benzyl Triton® DF-12, C8.?o ( PO) 2 (EO) 13-benzyl, Alcohol- (EO) x- (BuO)? H Plurafac® LF-221, C10-? 2 (EO) 9 5 (BuO) ,. 2 Alcohol- (EO) x- alkyl Dehypon® Lt-104, C16.18 (EO) 12CH2OC4H9 Alcohol- (EO) x-benzyl Triton® DF-18, C14.16 (EO) 16-benzyl
a AP NMR analysis = alkylphenoxy EO = ethylene oxide PO = propylene oxide BuO = butylene oxide. Triton® is a registered trademark of Union Carbide Chemical & Plastics Co. Surfonic® is a registered trademark of Texaco Chemical Co. Poly-Tergent® is a registered trademark of Olin Corporation Plurafac® is a registered trademark of BASF Corporation Dehypon® is a registered trademark of Henkel Corporation
SEMIPOLAR NON-IONIC SURGICAL AGENTS Non-ionic surfactants of the semipolar type are another class of nonionic surfactants useful in the compositions of the present invention. In general, semi-polar nonionic surfactants are high in foam production and foam stabilizers that have limited application in CIP systems. However, within the composition modalities of this invention, designed for the cleaning methodology with high foam production, such as the cleaning of installations that frequently use detergent solutions dispensed on foam surfaces, the semi-polar non-ionics would have utility immediate Semi-polar nonionic surfactants include: amine oxides, phosphine oxides, sulfoxides and their alkoxylated derivatives. 8.- The amine oxides are tertiary amine oxides corresponding to the general formula:
R1 - (OR4) - N - »O I R3
wherein the arrow is a conventional representation of a semipolar ligature; and R1, R2 and R3 can be aliphatic, aromatic, heterocyclic, alicyclic or combinations thereof. In general, for the interesting amine oxides for detergents, R1 is an alkyl radical of from about 8 to about 24 carbon atoms; R2 and R3 are selected from the group consisting of alkyl or hydroxyalkyl of 1 to 3 carbon atoms, and mixtures thereof; R 4 is an alkylene or hydroxyalkylene group containing 2 or 3 carbon atoms; and n ranges from 0 to about 20. Useful water-soluble amine oxide surfactants are selected from cocoalkyl or tallowalkyl di (lower alkyl) amine oxides; whose specific examples are: dodecyldimethylamine oxide, tridecyldimethylamine oxide, tetradecyldimethylamine oxide, pentadecyldimethylamine oxide, hexadecyldimethylamine oxide, heptdecyldimethylamine oxide, octadecyldimethylamine oxide, dodecyldipropylamine oxide, tetradecyldipropylamine oxide, hexadecyldipropylamine oxide, tetradecyldibutylamine oxide, oxide of octadecyldibutylamine, bis (2-hydroxyethyl) dodecylamine oxide, bis (2-hydroxyethyl) -3-dodecoxy-1-hydroxypropylamine oxide, dimethyl- (2-hydroxydecyl) amine oxide, 3,6,9-trioctadecyldimethylamine oxide and 3-dodecoxy-2-hydroxypropyl- (2-hydroxyethyl) amine oxide. The nonionic, semipolar, useful surfactants also include the water-soluble phosphine oxides, which have the following structure:
R2 R1 + P - O R3 where the arrow is a conventional representation of a semipolar ligature; and R1 is an alkyl, alkenyl or hydroxyalkyl portion ranging from 10 to about 24 carbon atoms in the chain length; and each of R2 and R3 is an alkyl portion, selected separately from alkyl or hydroxyalkyl groups containing from 1 to 3 carbon atoms. Examples of useful phosphine oxides include: dimethyldecylphosphine oxides, dimethyltetradecylphosphine oxide, methylethyltetradecylphosphone oxide, dimethylhexadecylphosphine oxide, diethyl-2-hydroxyoctyl-cyclysphine oxide, bis (2-hydroxyethyl) dodecylphosphine oxide and bis (hydroxymethyl) oxide. ) tetradecylphosphine .. The semipolar nonionic surfactants, useful herein, also include the water-soluble sulfoxide compounds, which have the structure:
R1 S ^ O l2 R2 in which the arrow is a conventional representation of a semipolar ligature; and R1 is an alkyl or hydroxyalkyl portion of from about 8 to about 28 carbon atoms; from 0 to about 5 ether ligatures and about 0 to 2 hydroxyl substituents; and R2 is an alkyl portion consisting of alkyl and hydroxyalkyl groups having from 1 to 3 carbon atoms.
Useful examples of these sulfoxides include: dodecylmethyl sulfoxide; 3-hydroxytridecylmethyl sulfoxide, 3-methoxytridecylmethyl sulfoxide and 3-hydroxy-4-dodecoxybutylmethyl sulfoxide.
ANIONIC SURGICAL AGENTS
Also useful in the present invention are surfactants which are categorized as anionic 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 it (eg, carboxylic acids). The carboxylate, the sulfonate, the sulfate and the phosphate are the polar (hydrophilic) solubilizing groups found in the anionic surfactants. Of the cations (counter ions) associated with these polar groups, sodium, lithium and potassium impart solubility in water; the ammonium and substituted ammonium ions provide solubility in water and in oil; and calcium, barium and magnesium ions promote solubility in oil. Those skilled in the art will understand that anionics are excellent detergent surfactants and, therefore, will favor additions to heavy duty detergent compositions. However, in general, anionics have high foam production profiles that limit their use alone or at high concentration levels in cleaning systems, such as CIP circuits that require strict control of the foam. However, anionics are very useful additives for the preferred compositions of the present invention; at low percentages or in cooperation with a non-ionic low foaming agent or a defoaming agent, for application in CIP and similar cleaning regimes, with controlled foam; and at higher concentrations in detergent compositions designed to produce detergent foaming solutions. Certainly the anionic surfactants are preferred ingredients in various embodiments of the present invention, which incorporate foam for delivery and utility, for example, sticky foams used for cleaning installations in general. Additionally, surfactant compounds are useful for imparting special chemical or physical properties in addition to detergency, within the composition. The anionics can be used as gelling agents or as part of a gelation or thickening system. The anionics are excellent solubilizers and can be used for hydrotropic effects and turbidity point control. The anionics can also serve as solidifiers for solid forms of product of the invention, and others. Most commercial large-volume anionic surfactants can be subdivided into five main chemical classes and additional subgroups (taken from Surfactant Encyclopedia, Cosmetics &Toiletries, volume 104 (2), 71-86 (1989), and incorporated herein by this reference): A.- Acylaminoacids (and their salts): 1.- Acylglutamates 2.- Acylpeptides 3.- Sarcosinates 4.- Taurates. B.- Carboxylic acids (and their salts). 1.- Alkanoic acids (and alkanoates). 2.- Carboxylic ester acids 3.- Carboxylic ether acids. C- Esters of phosphoric acid (and its salts) 1.- acyl isethionates 2.- Alkylaryl sulphonates 3.- Alkyl sulphonates 4.- Sulfosuccinates. E. Esters of sulfuric acid (and its salts) 1. Alkyl ether sulfates 2. Alkyl sulfates It should be noted that some of these anionic surfactants may be incompatible with the enzymes incorporated in the present invention. As an example, acyl amino acids and their salts may be incompatible with proteolytic enzymes, due to their peptide structure. Examples of suitable synthetic, water-soluble anionic detergent compounds are ammonium and substituted ammonium salts (such as mono-, di- and triethanolamine) and alkali metal salts (such as sodium, lithium and potassium salts), of aromatic alkyl mononuclear sulfonates, such as alkylbenzene sulphonates containing about 5 to 18 carbon atoms in the alkyl group, in straight or branched chain, for example, the alkylbenzene sulphonate or alkyl toluene, xylene, cumene salts and phenolsulfonates; alkylnaphthalenesulfonate, diamilnaphthalenesulfonate and dinonylnaphthalenesulfonate, as well as their alkoxylated derivatives. Other anionic detergents are olefin sulfonates, which include the long chain alkenesulfonates, the long chain hydroxyalkanesulfonates or mixtures of alkenesulfonates and hydroxyalkanesulfonates. Also included are alkyl sulphates, alkyl poly (ethyleneoxy) sulfates and poly (ethyleneoxy) aromatic sulfates, such as sulfates or condensation products of ethylene oxide and nonylphenol (generally having 1 to 6 oxyethylene groups per molecule). The particular salts will be selected appropriately depending on the particular formulation and the needs. The most preferred anionic surfactants for the most preferred embodiment of the invention are the linear and branched mono- and / or diaryl (C6.14) d-phenyloxide alkali metal mono- and / or disulphonates commercially available from Dow Chemical , for example, COWFAX® 2A-1 and DOWFAX® C6L.
THE CATIONIC SURFACTANTS AGENTS
Surfactants are classified as cationic if the charge in the hydrotropic portion of the molecule is positive. Surfactants in which the hydrotrope carries no charge, unless the pH is lowered almost to neutral or less, are also included in this group (eg, alkylamines). Theoretically, cationic surfactants can be synthesized from any combination of elements containing an RnX + Y "onium" structure and could include compounds other than nitrogen (ammonium), such as phosphorus (phosphonium) and sulfur (sulfonium). In practice, the field of cationic surfactants is dominated by nitrogen-containing compounds, probably because the synthetic routes for nitrogenous cationics are simpler and more direct, and give high yields of product, for example, are less expensive. Cationic surfactants refer to compounds that contain at least one hydrophobic long chain carbon group and at least one positively charged nitrogen. The long carbon chain group can be attached directly to the nitrogen atom by simple substitution, or preferably indirectly by one or more bridging functional groups, in the so-called interrupted alkylamines and amidoamines, which make the molecule more hydrophilic and, for consequently, more dispersible in water, more easily solubilized in water by surfactant coagent mixtures, or soluble in water. For increased water solubility, additional primary, secondary or tertiary amino groups can be introduced, or the amino nitrogen can be quaternized with low molecular weight alkyl groups. Additionally, the nitrogen may be a member of a branched or straight chain portion of varying degrees of unsaturation; or of a saturated or unsaturated heterocyclic ring. In addition, the cationic surfactants may contain complex bonds having more than one cationic nitrogen atom. The surfactant compounds classified as amine, amphoteric and zwitterionic oxides are in turn cationic in solutions of almost neutral to acid pH, and overlap the surfactant classifications. The polyoxyethylated cationic surfactants behave as nonionic surfactants in alkaline solution and as cationic surfactants in acid solution. The simplest cationic amines, the amine salts and the quaternary ammonium compounds can be schematically drawn in this way:
R 'R' R '/ R - NR - NH + X - R - N + - R "X + \ R" R "k - R represents a long alkyl chain, R', R" and R '"can be long alkyl chains or lower alkyl or aryl groups, or hydrogen, and X represents an anion Only the amine salts and the quaternary ammonium compounds are of practical use in this invention, due to the solubility in water. commercial, large volume cationic surfactants can be subdivided into four main classes and additional subgroups (taken from Surfactant Encyclopedia, Cosmetics &Toiletries, volume 104 (2) 86-96 (1989), and incorporated herein by reference): A .- Alkylamines (and their salts) B.- Alkylimidazolines C- Ethoxylated amines D.- Quaternary 1.- Alkylbenzyldimethylammonium salts 2.- Alkylbenzene salts 3.- Heterocyclic ammonium salts 4.- Tetraalkylammonium salts. In this invention, cationics are specialty surfactants, incorporates two for its specific effect; for example, detergency in compositions of neutral pH or below neutral; antimicrobial efficacy, thickening or gelling, in cooperation with other agents, etc.
The cationic surfactants useful in the compositions of the present invention have the formula R1mR2xY Z, wherein each R1 is an organic group containing straight or branched alkyl or alkenyl groups, optionally substituted with up to three phenyl or hydroxy groups; and optionally interrupted by up to four structures, selected from the following group:
R1 OR H
C - O - C - N C - N
isomers and mixtures thereof; and containing about 8 to 22 carbon atoms. The R1 groups may additionally contain up to 12 ethoxy groups; m is a number from 1 to 3. No more than one group R1 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 R2 is an alkyl group or hydroxyalkyl containing 1 to 4 carbon atoms or a benzyl group; no more than one R2 in a molecule is benzyl, and x is a number from 0 to 11, preferably from 0 to 6. The remainder of any positions of carbon atoms in the group Y are filled by hydrogens. And it is selected from the group consisting of, but not limited to:
p = around 1 to 12
(C2H4?) - N + - (C2H4O) = * around 1 to 12
~ N
and its mixtures. L is 1 or 2, the groups Y being separated by a selected portion of analogs of R1 and R2 (preferably alkylene or alkenylene) having from 1 to 22 carbon atoms and two simple free carbon bonds, when L is 2. Z is a water-soluble anion, such as anion halide, sulfate, methylisulfate, hydroxide or nitrate; with the chloride, bromide, iodide, sulfate or methylisulfate anions being preferred in a number that gives electrical neutrality of the cationic component.
THE SURFACTANT SURGICAL AGENTS
The amphoteric surfactants contain both a basic and an acidic hydrophilic group, and an organic hydrophobic group. These ionic entities can be any anionic or cationic group described in the preceding sections. A basic nitrogen and an acid carboxylate group are the predominant functional groups, although in a few structures sulfonate, sulfate, phosphonate or phosphate provide negative charge. • Ampholytic surfactants can be broadly described as secondary and tertiary aliphatic amine derivatives, wherein the aliphatic radical can be straight or branched chain, and where one of the aliphatic substituents contains about 8 to 18 carbon atoms, and one contains a water-solubilizing, anionic group, for example, carboxy, sulfo, sulfate, phosphate or phosphono. The amphoteric surfactants are subdivided into two main classes: (taken from Surfactant Encyclopedia, Cosmetics &Toiletries, volume 104 (2) 69-71 (1989)): A.- Acyl / dialkylethylenediamine derivatives (2-alkyl derivatives) hydroxyethylimidazoline) (and its salts). B. N-Alkylamino acids (and their salts). The 2-alkylhydroxyethylimidazoline is synthesized by condensation and ring closure of a long chain carboxylic acid (or its derivative) with dialkylethylenediamine. The commercial amphoteric surfactants are derived by subsequent hydrolysis and ring opening of the imidazoline ring by alkylation, for example, with chloroacetic acid or ethyl acetate. During the alkylation one or two carboxyalkyl groups react to form a tertiary amine and an ether linkage, producing the different alkylating agents, different tertiary amines. The long chain imidazole derivatives, which have application in the present invention, generally have the general formula:
wherein R is an acyclic hydrophobic group containing approximately 8 to 18 carbon atoms, and M is a cation to neutralize the charge of the anion, generally sodium. Commercially prominent imidazoline-derived amphoteric derivatives include, for example: Cocoanfo propionate, cocoanfocarboxypropionate, cocoanthine glycinate, cocoanfocarboxyglycinate, cocoanopropyl sulfonate and cocoanfocarboxypropionic acid. The carboxymethylated compounds (glycinates) mentioned above are frequently called betaines. Betaines are a special class of amphoters discussed in the section entitled Hybrid Ion Surfactants. Long chain N-alkylamino acids are easily prepared by the reaction of fatty amines RNH2 (R = C8.18), with halogenated carboxylic acids. Alkylation of the primary amino groups of an amino acid leads to secondary and tertiary amines. The alkyl substituents may have additional amino groups that provide more than one center of reactive nitrogen. Most commercial N-alkylamino acids are alkyl derivatives of beta-alanine or beta-N- (2-carboxyethyl) alanine. Examples of N-alkylamino acid ampholytes having application in this invention include the alkyl-beta-amino dipropionates, RN (C2H4COOM) 2 and RNHC2H4COOM. R is an acyclic hydrophobic group containing approximately 8 to 18 carbon atoms and M is a cation to neutralize the charge of the anion.
THE SURGICAL ION HYBRID AGENTS
The presence of a positively charged quaternary ammonium or, in some cases, of a sulfonium or phosphonium ion, and of a negatively charged carboxyl group within an aliphatic derivative compound, which generally has the betaine structure:
R "R" R "
R '- N + - CH2 - CO; R'- S - CH2 - CO; R 'P + - CH; CO;
R '"R"'
produces an amphoteric of special nature, called hybrid ion. These amphoters contain cationic and anionic groups that ionize to an almost equal degree in the isoelectric region of the molecule and develop "internal salt" attraction between the positive-negative charge centers. As a result, the betaine surfactants do not exhibit strong cationic or anionic characters at the pH extremes nor do they show reduced solubility in water in their isoelectric range. Unlike "external" quaternary ammonium salts, betaines are compatible with anionics. The synthetic zwitterionic surfactants useful in the present invention can be broadly described as aliphatic quaternary ammonium, phosphonium and sulfonium derivatives, wherein the aliphatic radicals can be straight or branched chain, and wherein one of the aliphatic substituents contain from 8 to 18 carbon atoms and one contains a water-solubilizing, anionic group, for example, carboxy, sulfonate, sulfate, phosphate or phosphonate. A general formula for these compounds is:
(R2) >
R1 - Y + - CH2 - R3 - Z '
wherein R1 contains an alkyl, alkenyl or hydroxyalkyl radical of 8 to 18 carbon atoms, having from 0 to 10 portions ethylene oxide and from 0 to 1 glyceryl portion; And it is selected from the group consisting of nitrogen, phosphorus and sulfur atoms; R2 is an alkyl or monohydroxyalkyl group containing from 1 to 3 carbon atoms; x is 1 when Y is a sulfur atom and 2 when Y is a nitrogen or phosphorus atom. R3 is an alkylene or hydroxyalkylene or hydroxyalkylene of 1 to 4 carbon atoms and Z is a radical selected from the group consisting of the carboxylate, sulfonate, sulfate, phosphonate and phosphate groups. Examples include: 4- [N, N-di (2-hydroxyethyl) -N-octadecylammonium butan-1-carboxylate; 3-Hydroxypentan-1-sulfate of 5- [S-3-hydroxypropyl-S-hexadecyl-sulfonium]; 2-hiroxypropan-1-phosphate of 3- [P, P-diethyl-P-3.6.9-trioxatetracosano-phosphonium]; 3-propan-1-phosphonate 3- [N, N-dipropyl-N-3-dodecoxy-2-hydroxypropyl-ammonium]; 3- (N, N-dimethyl-N-hexadecylammonium) propane-1-sulfonate; 2-hydroxy-propan-1-sulfonate of 3- (N, N-dimethyl-N-hexadecylammonium); 4- [N, N-di (2- (2-hydroxyethyl) -N- (2-hydroxy-dodecyl) ammonium] butan-1-carboxylate] n-1-phosphate 3- [S-ethyl-] S- (3-dodecoxy-2-hydroxypropyl) sulfonium]; propan-1-phosphonate of 3- [P, P-dimethyl-P-dodecylphosphonium; and 2-hydroxy-pentan-1-sulfate of S- [N, N] -di (3-hydroxypropyl) -N-hexadecyl-ammonium] The alkyl groups contained in said detergent surfactants can be straight or branched and saturated or unsaturated The nonionic and anionic surfactants listed above can be used individually or in combination , in practice and the utility of the present invention.
Semi-polar nonionic, cationic, amphoteric and zwitterionic surfactants are generally used in combination with non-ionic or anionic agents. The preceding examples are simply specific illustrations of numerous surfactants having application within the scope of this invention. The above organic surfactant compounds can be formulated in any of the various commercially convenient composition forms of this invention having the utility described. Said compositions are cleaning treatments for surfaces contaminated with food, in concentrated form, which, when dispensed or dissolved in water, properly diluted by means of a proportioning device, and supplied to target surfaces as a solution a gel or a foam , they will provide cleaning. Said cleaning treatments consist of a product or involve a system of two products, where proportions of each one are used. Said product is in the form of liquid or emulsion concentrates; in the form of solids, such as tablets or capsules; powder or particulate, gel or paste; and in suspension or in the form of mud.
THE SOLIDIFYING AGENTS
Solidifying agents are used in the claimed invention in order to convert the liquid detergent premix to a solid. Borate can function as a solidifying agent within the present invention. Other solidifying agents can be chosen from the group consisting of carbonates, bicarbonates, sulfates and urea.
THE KIDNAKERS
In order to soften or treat the water, to prevent the formation of precipitates or other salts, the composition of the present invention generally comprises components known as chelating agents, builders or sequestering agents. In general, sequestrants are those molecules that are capable of complexing or coordinating the metal ions commonly found in service water, and thereby preventing metal ions from interfering with the operation of the detergent components within the composition. Any number of sequestrants can be used within the composition. Representative sequestrants include salts of aminocarboxylic acids, salts of phosphonic acid, water-soluble acrylic polymers, among others. The molecular weight of these polymeric materials is about 200 to 8,000, preferably 4,000 to 6,000. The term "condensed phosphate" indicates a material having at least one group according to the formula:
OH OH OH
- O - P - O - O - P - O -
where the free ligatures are directed to other phosphate groups, cations, etc., which may be part of a linear, condensed or cyclic phosphate composition. Compounds with phosphate moieties useful as scavengers are fused alkali metal phosphates, cyclic phosphates, organophosphonic acids and salts of organophosphonic acid. Useful fused phosphates include alkali metal pyrophosphate, an alkali metal polyphosphate, such as sodium tripolyphosphate (STPP), obtainable in a variety of particle sizes. Useful organophosphonic acids include the mono-, di-, tri- and tetraphosphonic acids, which may 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 be inverted can be controlled using a condensed phosphate that reduces the impact of the caustic and water on the sequestering material. Such effects can be reduced by using a sequester of effective particle size and using barrier technologies. The inorganic fused phosphate can also be combined with a carboxylate, phosphonate, phosphonic acid or a phosphonic acid salt. Organic materials can help to sequester hardness ions in cleaning processes. The aminocarboxylic acid chelating agents include N-hydroxyethyiiminodiacetic acid, nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), N-hydroxyethyl-ethylenediaminetriacetic acid (HEDTA) and diethylenetriaminepentaacetic acid (DTPA). When used, these aminocarboxylic acids are generally present in concentrations ranging from about 1% by weight to 50% by weight, preferably from about 2% by weight to 45% by weight, and most preferably, around from 3% by weight to 40% by weight. Other suitable scavengers include soluble acrylic polymers having -CO 2"1 -dependent groups used to condition wash solutions under the conditions of end use, such polymers include: polyacrylic acid, polymethacrylic acid, copolymers of acrylic acid-methacrylic acid, copolymers of acrylic acid - itaconic acid, 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, their respective alkali metal salts (for example, sodium or potassium) or ammonium, can also be used. The number average molecular weight of the polymers is approximately 4,000 to 12,000. Preferred polymers include: polyacrylic acid, the partial sodium salts of polyacrylic acid and sodium polyacrylate, which have an average molecular weight within the range of 4,000 to 8,000. These acrylic polymers are generally useful at concentrations ranging from about 0.5% by weight to 20% by weight, preferably from about 1 to 10, most preferably from about 1 to 5. Useful phosphonic acids are also: acid 1 -hydroxyethane-1, 1-diphosphonic acid, aminotri (methylene phosphonic acid), aminotri- (methylenephosphonate), sodium salt of 2-hydroxyethyl-iminobis (methylene phosphonic acid), diethylenetriaminepenta- (methylene phosphonic acid), sodium salt of diethylenetriamine penta ( methylenephosphonate), potassium salt of hexamethylenediamine- (tetramethylene phosphonate); bis (hexamethylene) triamine acid (pentamethylene phosphonic acid (HO2) POCH2N [(CH2) 6N [CH2PO (OH) 2j2] 2 and phosphorous acid H3PO3 The preferred phosphonate is aminotrimethylenephosphonic acid or its salts, optionally combined with diethylenetriaminepentatic acid (methylene phosphonic) When used as a sequestrant in the invention, the phosphonic acids or salts are present at a concentration ranging from about 0.25 to 25% by weight, preferably from about 1 to 20% by weight and, very preferable, from about 1 to 18% by weight, based on the solid detergent.
DETAILED DISCUSSION OF THE FIGURE
The figure shows data referring to the stability of the enzymatic activity in the solid block materials. Each preparation must be compared with the enzyme control represented by the dashed line. Certain compositions, examples 5, 6, 7, 8 and 9, all have superior stability of enzymatic activity, as compared to the enzyme material alone. This stability is present for twelve days, under comparatively severe conditions.
METHOD OF USE
This refers to a cleaning method, by which the cleaning solution or solutions are pumped through the processing equipment, while remaining in place. It is not necessary to disassemble the processing equipment. In the preferred embodiment of the present invention the product is dissolved by spraying water in a solid dispenser and is supplied to a drain or directly to the solution tank of use, from which the use solution is pumped to where cleaning is necessary. The concentration of use is typically about 0.1% in aqueous solution. The pH is about 9.0 to 10 and the temperature is between 54.4 ° C and 65.6 ° C. In any method of use, control over the concentration of the enzymatic cleaner in the aqueous solution must be maintained. It has been found that the conductivity of the ionic species in the aqueous solution (sodium ions, potassium, borate, etc.) can be used to control the total concentration of the detergent components, including surfactants, enzymes and other non-conductive materials. It has been discovered that by using direct current or alternating current conductivity in measurements of the use solution, a spray can be used from a dispenser to deliver an aqueous concentrate, to maintain the use solution at an appropriate concentration of agent enzymatic surfactant and other components. The conductivity of the use solution is measured using electrical conductivity measuring means. As the conductivity of the use solution drops, the concentration of the enzyme, the surfactant and other active ingredients in the use solution is also proportionally reduced. The solution for the use of the enzymatic surfactant and other active ingredients can be replenished 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 a suitable amount of the detergent into the solution of the detergent. use. When the solid block containing the enzymatic surfactant and other active components is dissolved, by the water spray, the inorganic ionizable materials are also dispensed. By monitoring the conductivity created by the ionizable materials in the aqueous solution, the concentration of the enzymatic component and other surfactants and other ingredients can also be controlled quite intimately. Typically the conductivity of the use solution is maintained between 500 and 800 μsiemens / cm to give an adequate concentration of the enzyme, the surfactant and other active ingredients. Although conductivity measurements have long been used as a means to investigate the properties of electrolytes in solution, such as dissociation, activity, complex formation and hydrolysis, these measurements also provide the basis for the instrumentation used. in industry, to detect water ion contamination and to determine the concentration of simple electrolyte solutions (see Van Nostrand's Scientific Encyclopedia, 6th edition, volume I, pages 1056-1058). In this reference, the term electrolytic conductivity has been applied almost exclusively to aqueous solutions of electrolytes in which the mechanism of electric current transfer depends on the ions. However, solid and molten salts also exhibit electrolytic conductivity. The electrolytic conductivity (specific conductance) is defined as the electrical conductance of a unit cube of electrolytic solution. It is expressed in the same units as the electrical conductivity, that is, reciprocal ohms per unit length. Most commonly, you will find the conductivity units of:
Mhos / cm.siemens / cm.microsiemens / cm (μS-cm "1) and siemens / meter (1mho / cm = 1 siemens / cm = 100 siemens / meter)
It typically increases the conductivity to a maximum value and then decreases with increasing concentration. Sometimes an additional point of inflection can occur. The conductivity of saline solutions typically increases with temperature. Pure water changes a little more with changes in temperature, while acids and strong bases change a little less. From the preceding discussion it can be seen that the value of the conductivity measurement is useless without knowledge of the temperature at which the measurement was made. Frequently electrical conductivity is measured by placing electrodes in contact with the electrolyte solution that is contained in such a way that the electrical conductance measured between the electrodes can be related to the conductivity of the solution. A conductivity cell commonly comprises a shell made of electrically insulating material, such as glass or plastic, which contains a portion of the solution and which accommodates the two electrodes. The cell constant of said device is then used to relate the electrical conductance measured between the electrodes with the actual electrolytic conductivity. Two electrodes of one square centimeter, located on opposite internal faces of a hollow cube one centimeter from one edge, would have a cell constant of 1 / cm, and a measured conductance of 0.005 mhos / cm (0.5 siemens / meter) to 25 ° C. If the electrical conductance between the electrodes with direct current is measured, the resulting electrolysis and gas evolution can interfere with the passage of the current and change the composition of the solution. Alternating current measurements greatly reduce these interference factors and have wide use in these measurements. Appropriately designed inductive alternating current 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 are the most widely used, accepted instrumentation for electrolytic conductivity measurements. Changes in the temperature of the solution change the bridge characteristics in a similar way, thus allowing the bridge to remain balanced, except for the real changes in the concentration of the solution. Conductivity meters generally apply a constant alternating voltage across the electrodes and respond to the resulting current flow, which is proportional to the conductivity of the solution. Automatic temperature compensation means are also included in these circuits. Measurements of electrolytic conductivity by means of electric induction can be made without using contact electrodes. Said measurements are made by inducing an alternating current in an electrolyte, through the use of a wire coil. The magnitude of the induced current is proportional to the conductivity of the electrolyte. The current is flowed 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, therefore, the conductivity, is measured by a second similar coil.
A typical laboratory-type CD conductivity cell employing two platinized platinum electrodes, contained in an open-bottom cylindrical chamber, is formed of 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 diluted solutions used in the laboratory. This kind of cell is immersed in an open upper end container containing the sample to be measured. Wide use is made in the laboratory of conductivity cells of this type to determine the water quality and to select samples that are to be titrated or further analyzed by other means. A wide variety of conductivity cells are available for use, including DC and AC cells, cells without electrodes and others.
EXAMPLES
In order to test the stability of the claimed invention, various formulations were tested. These formulations are described in the following table.
ENZYME SOLID CLEANING FORMULATIONS
The specific test results appear in the list in the following table, and are also shown graphically in figure 1:
SOLID PRODUCT STABILITY - FORMULATION STUDY
Additionally, the conductivity of several solutions was tested. The results are given in the following table:
CONTROL OF DOSAGE BASED ON CONDUCTIVITY
The use of an electrolyte, such as sodium, allows the conductivity to be used to control the dosage of the enzyme and also of the surfactant.
CONDUCTIVITY
Conductivity probes (inductive or electrodes) can be used to monitor the concentration of the enzyme in wash solutions, when dispensed from a sprayer or dispenser. The use of an electrolyte material in the detergent can increase the conductivity of the deionized water (approximately 1 TS-cm "1), to an adequate conductivity or for typical service water from municipal networks, which can vary from 100 to 300 TS-cm "1. Since detergent materials are typically dispensed in water from the urban network, a substantial increase in conductivity is needed to control the enzyme concentration, when dispensed in water from the urban network. Consequently, a substantial difference in conductivity must be obtained from the material dispensed when compared to the conductivity of the water in the urban network. Accordingly, a minimum conductivity of the wash solution is greater than about 300 μsiemens / cm, preferably greater than 400 μsiemens / cm, most preferably, greater than 500 μsiemens / cm. Frequently the process can operate efficiently at conductivities in the scale of more than 650 μsiemens / cm, more than 750 μsiemens / cm or more than 1000 μiemens / cm. It has been found that even in the presence of substantial dirt, the conductivity of the enzyme cleaner is useful for controlling the concentration. The material can be dispensed even in the presence of a substantial concentration of milk, a dirt that can coat the electrode surfaces and reduce efficiency. The description, the examples and the preceding data provide an enabling description of the manufacture and use of the composition of the invention. Since many embodiments of the invention can be made, without departing from the spirit and scope of the invention, the invention resides in the claims that follow. All percentages in the claims are based on the detergent composition as a whole.
Claims (18)
1. - A method for dispensing a stabilized enzyme composition, in solid block, with a spray dispenser, at a use site, where the method has control over the enzyme concentration; characterized in that the method comprises: (a) placing a stabilized enzyme composition, in solid block, close to a water spraying means; the composition comprising a stabilized enzyme system and an electrolyte; the spraying means being capable of creating an aqueous concentrate when spraying the block composition with water, and of directing the aqueous concentrate to a volume of aqueous cleaner to a site of use; and (b) maintaining an effective concentration of the enzyme, causing the spray on the dispenser to create the concentrate and control the enzyme concentration, maintaining the conductivity of the aqueous cleaner volume above a preselected minimum conductivity.
2. The method according to claim 1, further characterized in that the minimum conductivity is greater than about 300 TS-cm "1.
3. The method according to claim 1, further characterized in that the minimum conductivity is greater than approximately 400 TS-cm'l
4. The method according to claim 1, further characterized in that the minimum conductivity is greater than about 500 TS-cm "1.
5. The method according to claim 1, further characterized in that the minimum conductivity is greater than about 750 TS-cm "1.
The method according to claim 1, further characterized in that the site of use comprises a On-site cleaning system
7. The method according to claim 6, further characterized in that the on-site cleaning system is installed in a dairy
8. A cleaning composition containing solid block enzyme, characterized in that it comprises: (a) about 0.1 to 50% by weight of an enzymatic cleaning composition, and (b) an amount of a stabilizing composition effective to stabilize the enzymatic cleaning composition, the stabilizer comprising about 1 to 40% by weight of a alkali metal borate and a carbohydrate comprising a monosaccharide, a disaccharide or mixtures thereof, wherein the detergent is formed and solidified in a or by extrusion, and is free of alkali metal hydroxides and active chlorine sources.
9. The composition according to claim 8, further characterized in that the enzyme comprises a protease.
10. - The composition according to claim 8, further characterized in that it comprises a monosaccharide consisting of glucose, galactose, fructose or mixtures thereof.
11. The composition according to claim 8, further characterized in that the carbohydrate comprises a disaccharide consisting of sucrose, lactose, maltose or mixtures thereof.
12. The composition according to claim 8, further characterized in that the cleaning composition containing solid block enzyme additionally comprises an effective amount of solidifying agent.
13.- The composition in accordance with the claim 12, further characterized in that the solidifying agent comprises an alkali metal carbonate, an alkali metal bicarbonate or an alkali metal borate, or mixtures thereof.
14.- The composition in accordance with the claim 13, further characterized in that the alkali borate is a disodium tetraborate in anhydrous form, of pentahydrate or decahydrate, or mixtures thereof.
15.- The composition in accordance with the claim 8, further characterized in that the cleaning composition containing the solid block enzyme additionally comprises a surfactant, a sequestrant, an antioxidant, an ancrobial agent or an anti-corrosion agent, or mixtures thereof.
16. The composition according to claim 8, further characterized in that the cleaning composition containing enzyme in solid block is a bar, briquette or block form, packed in a bag, bucket or capsule, or is wrapped in shrink wrap.
17. The composition according to claim 8, further characterized in that the cleaning composition containing solid block enzyme is extruded and formed in a bucket.
18. The cleaning composition containing solid block enzyme, according to claim 8, further characterized in that the cleaning composition additionally comprises sufficient electrolyte for an aqueous concentrate, generated by spraying with water the cleaning composition containing enzyme in solid block , create an aqueous concentrate that has a conductivity greater than about TS-cm "1.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US09/040,628 | 1998-03-18 |
Publications (1)
Publication Number | Publication Date |
---|---|
MXPA00009136A true MXPA00009136A (en) | 2001-09-07 |
Family
ID=
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