MXPA98008792A - Surfactants of den-acilo etilendiamintriacyl acid as surfactants compatible with enzymes, stabilizers and activated - Google Patents

Abstract

The present invention relates to compositions that include one or more enzymes, and as the compatible chelating surfactant, salts of the N-acyl ethylenediamine triacetic acid ("ED3A"). The N-acyl ED3A salts do not easily denature several enzymes and are therefore highly compatible with such enzymes, and improve their detergent effectiveness to an unexpected degree

Description

SURFACTANTS OF N-ACIL ETHELENDIAMINTRIACTIC ACID AS SURFACTANTS COMPATIBLE WITH ENZYMES, STABILIZERS AND ACTIVATORS FIELD AND BACKGROUND OF THE INVENTION Ethylenediaminetriacetic acid (ED3A) and its salts (such as its alkali metal salts, including ED3ANa3) have applications in the field of chelation chemistry, and can be used as a starting material in the preparation of strong chelating polymers, chelating agents soluble in oil, surfactants and others. Conventional pathways for the synthesis of ethylenediaminetriacetic acid are achieved via its N-benzyl derivative, which is subsequently hydrolyzed in alkaline solutions for ED3ANa3, then cyclization is avoided for its 2-oxo-l, 4-piperazindiacetic acid derivative ( 3KP). An example of the synthesis of ethylene diamine N, N, N'-triacetic acid is described in Chemical Abstracts 78, Vol. 71, page 451, no. 18369c, 1969. It is established that ethylenediamine reacts with C1H2CC02H in a molar ratio of 1: 3 in basic solution at 10 ° C for 24 hours to form a mixture from which ethylene diamine-N can be separated, N, N'-triacetic forming complex itself REF .: 28501 with Co (III). The resulting cobalt complexes can be isolated through ion exchange. U.S. Patent No. 5,250,728, the description of which is incorporated herein by reference, describes a simple process for the synthesis of ED3A or its salts in high yield. Specifically, a salt of N, N'-ethylenediamidiacetic acid (ED2AH2) is condensed with stoichiometric amounts, preferably light molar excesses of formaldehyde, at the temperature between 0 ° C and 110 ° C, preferably 0 ° C to 65 ° C and the pH greater than 7.0 to form a ring intermediate with 5 stable elements. The addition of a source of cyanide, such as gaseous or liquid hydrocyanic acid, aqueous solutions of hydrocyanic acid or alkali metal cyanide, in stoichiometric amounts or in a slight molar excess, through this cyclic material at temperatures between 0 ° C and 110 ° C, preferably between 0 ° C and 65 ° C, forms the ethylene diamine N, N'-diacetic acid-N'-cyanomethyl or salts thereof (mononitrile-diacid). The nitrile in aqueous solutions can be cyclized spontaneously in the presence of less than 3.0 moles of base: mol of ED2AH2, the base includes hydroxides of alkali metals or alkaline earth metals, to form 2-oxo-l, 4-piperazindiacetic acid (3KP) ) or salts thereof, this is the desired cyclic intermediate. In the presence of excess base, ED3A salts are formed with excellent yield and purity. This patent also describes an alternative embodiment in which the starting material is ED2AHaXb / wherein X is a base cation, for example, an alkaline or alkaline earth metal, a is 1 to 2, and b is 0 to 1 in aqueous solutions. The reaction mixture can also be acidified to ensure complete formation of carboxymethyl-2-oxopiperazine (the lactam) prior to the reaction. Formaldehyde is added, essentially resulting in the hydroxymethyl derivative. With the addition of a cyanide source, l-cyanomethyl-4-carboxymethyl-3-ketopiperazine (mononitrile monoacid) or a salt thereof is formed. Instead of CH20 and a source of cyanide, H0CH2CN, which is the product of formaldehyde and cyanide reaction, can also be used in this method. With the addition of any suitable base or acid, this material can be hydrolyzed to 3KP. The addition of a base will open this ring structure to form the ED3A salt. U.S. Patent No. 5,284,972, the disclosure of which is incorporated herein by reference, discloses ED3A derivatives of N-acyl and a process for producing the same. The production of N-acyl derivatives of ethylenediamine triacetic acid can be carried out or completed in accordance with the following general reaction scheme: NaOH ED3ANa3 + Acyl chloride > N-acyl ED3ANa3 + NaCl The starting ED3A derivative may be the acid itself, or suitable salts thereof, such as salts of alkaline metals and alkaline earth metals, preferably sodium or potassium salts. The saturated N-acyl ED3A derivatives which are the product of the preceding reaction can be represented by the following chemical formula: O CI? 2COOH fl 'C ^ t-C-N-CHjCHa- I \ CH, CH2COOH 1 COOH where n is from 1 to 40. Where unsaturation occurs, the structure can be shown as follows: O CHICCOOH II / C ^^, - C - N - CH2CH3 - N '\ CHa CH-COOH I COOH where n is from 2 to 40. When the unsaturation increases, the formulas are: O CH? COOH CHi CHjCOOH I COOH where n is 3 to 40, where n is 4 to 40; Y F? CH, COOH ri Y CpH? R? 7 - C - N * CH, CH * - N CH2 CH? E? OH COOH where n is 5 to 40, etc. Derivatives of poly-N-acyl ethylenediamine triacetic acid, such as dicarboxylic acid derivatives having the following general formula, can also be produced: HOOCCH, CH2COOH ^ N -CH2CH2 -NC- (CH,), - C-N-CII2CKi -N "- I I \ HOOCCH. CH2 CH2CO2H OOH OOII or: HOOCCHj N - CHnCH2 -NC - (CH? - COOH HOOCCH? / CH? OOH wherein x is 1 to 40. Specific examples include mono and di ED3A derivatives such as oxalyldi ED3A. oxalilmono ED3A, maleilmono ED3A, maleildi ED3A, succinoilmono ED3A, succinoildi ED3A, etc. In view of this relatively new technology, ethylenediaminetriacetic acid (ED3A) and its salts can now be easily produced in bulk and high yield. Enzymes such as proteases, lipases and amylases are commonly used to improve the performance of detergents for fabric washing liquids flooring, hard surface cleaners, to uncover fluid drainage, etc. By using an enzyme in a detergent, it is possible to hydrolyze proteins or starch residues in fabrics or fabrics to a degree that they could easily become soluble in water. Thus, a more effective removal of difficult starch or protein spots, including blood, mucus, and sweat, food products, etc. can be achieved. In addition, since insoluble proteins and starches cause dirt that adheres strongly to tissues, increasing the solubility of protein and starch also helps to remove dirt. Commercial enzymes are produced mainly by living cells such as yeasts, and are proteinaceous in nature. Enzymes with improved activity for commercial use are frequently produced by genetic engineering. The type of enzyme used depends on the detergent formulation and application conditions, especially since any given enzyme typically exhibits maximum effectiveness at pH's and specific temperatures. Previously its peak effectiveness temperature, it usually became denatured and never returned its activity. Enzymes are often denatured or deactivated by harsh or severe, such as sodium lauryl sulfate or linear alkyl benzene sulfate are also common for detergent formulations surfactants. It is believed that this denaturation or deactivation is due to the disturbance of the three-dimensional structure of the protein. Metal ions such as copper "1" 2, iron, nickel + 2, cobalt, etc., can also deactivate enzymes, possibly by interacting with and blocking the site of enzyme activity.

Therefore, it is an object of the present invention to provide surface-active agents compatible with enzymes. It is a further object of the present invention to provide detergent compositions containing an enzyme and a surfactant compatible with the enzyme. It is a still further object of the present invention to improve the detergent power of a detergent composition with a surfactant of N-acyl ED3A that is compatible with the enzyme in the detergent composition.

BRIEF DESCRIPTION OF THE INVENTION The problems of the prior art have been overcome by the present invention, which provides compositions that include one or more enzymes and one or more surfactants, provided that at least one of the surfactants is an N-acyl ethylenediamine triacetic acid or salt of the same. Surprisingly, the present invention has found that N-acyl ED3A is highly compatible with various enzymes, and improves its detergent effectiveness to an unexpected degree. Thus, the use of such surfactants with other enzyme systems, such as industrial processes, is also contemplated.

DETAILED DESCRIPTION OF THE INVENTION Suitable acyl groups in the N-acyl ED3A surfactant include linear or branched aliphatic or aromatic groups containing from 1 to 40 carbon atoms, such as pentanoyl, hexanoyl, heptanoyl, octanoyl, nananoyl, decanoyl, lauroyl, myristoyl, palmitoyl, oleoyl, stearoyl and nonanoyl. Examples of suitable branched acyl groups include neopentanoyl, neoheptanoyl, neodecanoyl, iso-octanoyl, iso-nananoyl and iso-tridecanoyl. Convenient aromatic acyl groups include benzoyl and naptoyl. The fatty acid chains can be substituted, such as by one or more halogen and / or hydroxyl groups. Examples of hydroxy-substituted fatty acids include ipurolic (3, 11-dihydroxytetradecanoic), usthyl (2,15, 16-trihydroxyhexadecanoic), ambretolic (16-hydroxy-7-hexadecanoic), rytolemic (12-hydroxy-cis-9) -octadecenoic acid), ricinelalylic (12-hydroxy-trans-9-octadecenoic), 9, 10-dihydroxyoctadecanoic, 12-hydroxyoctadecanoic, kalmlenic (18-hydroxy-8, 11, 13-octadecatrienoic), ximeninolic (8-hydroxy-trans 11-octadecen-9-inoic), isanolic (8-hydroxy-17-octadecen-9, 11, diinoic) and lequeroic (14-hydroxy-cis-11-eicosenoic), as well as acyl derivatives of the above ( previously named derivatives where the "oico" suffix is replaced by "oilo chloride"). Suitable halogen-substituted fatty acids include trifluoromethylbenzoyl chloride, pentadecafluoro-octanoyl chloride, pentafluoropropionoyl chloride, pentafluorobenzoyl chloride, perfluorostearoyl chloride, perfluorononamoyl chloride, perfluoroheptanoyl chloride and trifluoromethylacetyl chloride. Preferably, the N-acyl group contains from 8 to 18 carbon atoms. The surfactant properties of N-acyl ED3A molecules allow the dispersion of fatty residues or grease stains and thus improve the lipase activity against grease stains. When the interfacial tension between the aqueous phase and the fatty phase is reduced, the interfacial area increases, allowing the enzyme in the more superficial aqueous phase to attack, thereby increasing the reaction rate. The improved stain moistening allows a more efficient attack by enzymes, such as proteases, on deposited residues or proteinaceous stains.

In addition, the stability of N-acyl ED3A is not inhibited by the presence of excess electrolyte, such as sodium chloride, and multivalent hardness ions, such as Ca ++ and Mg ++. Surprisingly, the present inventors have found that such electrolytes and hardness ions actually significantly improve the stability of the N-acyl ED3A foam of alkali metal. The ability of ED3A of N-acyl to find transition metal and heavy ions also mitigate the potential for the enzyme activity to be reduced as a result of these ions. It is preferred to use the N-acyl ED3A in the form of its salts, in view of its solubility. Where the N-acyl ED3A is produced first, it can easily be converted into salts by partial or complete neutralization of the acid with the appropriate base. The acid can also be produced from ED3A salts of N-acyl by neutralization of the base with a quantitative amount of acid. Chelating surfactants, preferred, for use in the detergent compositions of the present invention, are sodium and potassium lauroyl-ED3A. Other suitable counterions or counter ions include triethanolamine, diethanolamine, monoethanolamine, ammonium, isopropyl amine, N-propylamine and amino alcohols such as 2-amino-1-butanol, 2-amino-2-methyl-1,3-propane diol, 2-amino-2-methyl-1-propanol, 2-amino-2-ethyl-l, 3-propane diol and Tris (hydroxylmethyl) aminomethane. The ED3A salts of N-acyl can be used in the detergent compositions of the present invention, alone or in combination with other surfactants. Preferably, the total amount of surfactant in the composition is between about 5 to about 30%, more preferably about 10 to about 25%, more preferably about 12%. The pH of the detergent composition depends in part on the particular enzyme that is used, but is generally within a range of about 7 to about 12. Suitable enzymes include proteolytic enzymes such as Alcalase®, Esperase®, Savinase® , and Durazym1®, amylases such as Termamyl®, BAN, lipases such as Lipolase®, and cellulases. Savinase®, for example, is a serine protease that has an optimum pH of 9-11 and an optimum temperature of 55 ° C. Avinase®, for example, has an optimum pH of about 6-8 and an optimum temperature of about 60 ° C. Lipases have the ability to decompose hydrophobic substances (such as hydrophobic triglycerides) into more hydrophilic compounds which are more easily removed by the action of the detergent.

In addition to the surfactant, detergent formulations typically comprise about 13-25% of forming agent, such as nitrilotriacetic acid, phosphates and zeolites. You can also add up to approximately 25% bleaching persales. Conventional surfactants that can be used in combination with the N-acyl ED3A include anionics such as sarcosinates (including oleoyl, lauroyl and myristoyl), soluble linear alkylbenzene sulfonate, alkyl sulfate and alkyl ethoxy sulfates, lauryl ether sulfate of sodium; nonionics such as ethoxylates of alcohol and alkyl polyglycosides; cationics such as C 2 -C 4 trimethyl ammonium chloride, di-tallow di-methyl ammonium chloride; and di-tallow methylamine, etc., and many of the foregoing compounds are frequently used in combination, such as a binary mixture of linear alkylbenzene sulfonate and alcohol ethoxylates. Other ingredients conventionally added to detergent compositions may be included, such as soaps, dyes, perfumes, thickeners, conditioners, humectants, buffers, opacifiers, preservatives, optical brighteners, fabric softeners, etc. Examples of suitable formulations are as follows: Detergent for Heavy Task, European, Traditional Type Sodium Lauroil ED3A 5-20% Non-ionic 1-7% Sodium Trifosphate 0-30% Zeolite 0-35% Sodium perborate / whiteness activator 10-25. Sodium carbonate 2-15% Sodium silicate 0-10% 0-1% complexing agent Polycarboxylates 0-3% Optical brighteners, Perfume 0.4-0.5% Enzymes: Alcalase 2.0 T or 0.4-0.8% Durazym 6.0 T or 0.3 -0.8% Wait 4.0 T or 0.4-0.8% Savinase 6.0 T 0.3-0.6% Lipolase 100 T 0.2-0.6% Termamyl 60 T 0.4-0.8% Celluzyme 0.7 T 1.0-3.0% Sodium sulphate, water, etc. 100% Balance pH 9.5-10.5 Compact Type Heavy Duty Detergent Miristoil ED3A sodium 5-35% Non-ionic 1-15% Sodium triphosphate 0-40% Zeolite 0-40% Sodium perborate / whiteness activator 15-30% Sodium silicate 2-10% Sodium carbonate 5-20% Complex forming agent (phosphonate, citrate) 0-1% Polycarboxylates 0-3% Optical brighteners, perfume 0.4-0.6% Enzymes: Durazym 6.0 T or 0.6-1.5% Wait for 4.0 T or 0.6-1.5% Savinase 6.0 T or 0.6-1.5% Lipolase 100 T 0.3-0.8% Termamyl 60 T 0.2-1.0% Celluzyme 0.7 T 1.2-3.0% Sodium sulfate, water, etc. Balance at 100% pH 9.5-11 Heavy Duty Liquid Detergent Oleoyl ED3A of triethanol amine 5-35% Nonionic 3-20% Sodium triphosphate 0- -30% Zeolite 0- -30% Complexing agent (phosphonate, citrate) 1-5% Polycarboxylates 0- -5 % Optical brighteners, perfume 0. .1-0. , 5% Enzymes: Alcalase 2.5 L or 0. .4-1. , 0% Durazym 16.0 L or 0. .2-0. , 6% Wait for 8.0 T or 0. .4-1. .0% Savinase 16.0 L or 0. .2-0. , 6% Termamyl 300 L 0. .2-0. , 6% Water 30-50% pH 7., 0-9. .5 Automatic Dishwasher Detergent Sodium Miristoil ED3A 2-5% Sodium Trifosphate 0-40% Sodium perborate / whiteness activator 4-20% Sodium silicate 5-30% Polycarboxylates 0-3% Complexing agent (phosphonate, citrate) 0-35% Enzymes: Durazym 6.0 T 1-3% Wait 6.0 Tr 1 -3% Savinase 6.0 T 1-3% Termamyl 60 T 1-3% Sodium sulphate, water, etc. Balance at 100% pH 9.5-11.0 EXAMPLE 1 The myristoyl and lauroyl ED3A acids are neutralized with aqueous sodium hydroxide to produce a 20% by weight Al solution. The resulting sodium lauroyl ED3A and sodium myristoyl ED3A are used at a concentration of 0.2% by weight. Ten grams of surfactant (20% by weight of AI) were added to 990 grams of distilled deionized water to produce the 0.2% by weight solution. One milliliter of protease enzyme (Savinase 174 16.0 L EX type commercially available from Novo Nordisk) was diluted to 100 ml with distilled deionized water. 1.43 ml of the enzyme solution were then added to four of five Tergotometer cells and allowed to acclimate for 20 minutes. The contents of the cells were as follows: Blood smear samples stained with blood / ink / milk were placed in each cell and allowed to soap for 90 minutes. The tergotometer was activated and the samples were washed with water for thirty minutes. After thirty minutes, the wash water was decanted. One liter of water was distilled, deionized then added to each cell and the cells were placed back into the tergotometer, which was activated for 10 minutes. The water was then decanted and the test cloth was removed and placed on a piece of white cardboard. The cloth was allowed to dry overnight in the air. The reflectance was measured using a photovoltaic detector with a detergent head and green filter. Four reflectance measurements were recorded for each test cloth, two measurements per side. The results of initial and final reflectance are shown in Table 2. The difference in reflectance between the final and initial values are shown in Table 3. The change in reflectance due to the activity of the enzyme is shown in Table 4.

The results demonstrate the compatibility of ED3A of N-acyl with protease enzyme. In addition, the presence of N-acyl ED3A significantly improves the cleaning power of the enzyme system. The presence of the enzyme also improves the cleaning power of the surfactant solution (relative to the cleaning power of the surfactant solution alone), which contributes about 12 extra brightness points.

EXAMPLE 2 The miristoil and oleoyl ED3A acids are neutralized with aqueous sodium hydroxide to produce a 20% by weight AI solution. In addition, a linear alkyl benzene sulphonate, mainly a 40% by weight sodium dodecylbenzene sulphonate solution (Strepantan DS-40) are diluted with distilled deionized water to produce a 20% by weight solution of AI. The aforementioned solutions, together with a solution of lauroyl ED3A, were evaluated at a concentration of 12.5% by weight in a base detergent having the following formulation: zeolite A 30.2% by weight sodium carbonate 20.8% by weight sodium sulfate 30.2% by weight sodium silicate 5.2% by weight eme 1.0% by weight The total detergent concentration tested was 3.5 grams of detergent / liter of water. Thus, the amount of dry detergent loaded in each cell was 3.06 grams, while the amount of liquid surfactant charged in each cell was 2.18 grams (using 20% by weight of surfactant AI). The exact weights used are shown in Table 5 below: TABLE 5 The surfactant portion of the detergent was added to each cell (containing one liter of distilled deionized water). The pH was adjusted to 8.3 with dilute NaOH. The remaining portion of the detergent was then added to the solution. The temperature of the solution in each of the cells was 48 ° C and the pH was 10.5. One milliliter of protease enzyme (Savinase4 * 16.0 L type EX commercially available from Novo Nordisk) was diluted to 100 ml. with distilled deionized water. Then 1.43 ml of the enzyme solution was added to three of six cells of the Tergotometer and allowed to acclimate for 10 minutes. Bloodstained cotton / ink / milk test samples were placed in each cell and the tergotometer was activated and the samples were washed for thirty minutes. After thirty minutes, the wash water was decanted. One liter of deionized, distilled water was then added to each cell and the cells were placed back into the tergotometer, which was then activated for 10 minutes. Then the water was decanted and the test tissue was removed and placed on a piece of white cardboard. The cloth was allowed to air dry all night. The reflectance was measured using a photovoltaic detector with a detergent head and green filter. Four reflectance measurements were recorded for each test cloth, two measurements per side. The results of initial and final reflectance are shown in Table 6. The change in reflectance due to the quality of detergent is present in Table 7. The change in reflectance due to the activity of the enzyme is shown in Table The linear alkylbenzene sulfonate deactivates the enzyme completely, and there was no increase in brightness between systems 1 and 4. However, systems 5 and 6 produce significantly higher values than systems 2 and 3. In the case of miristoil ED3A , the presence of the enzyme increases the brightness by 3.3 points. The n-acyl ED3A was compatible with the enzyme.

It is noted that in relation to this date, the best method known to the applicant to carry out the aforementioned invention, is that which refers to the manufacture of the objects to which it refers. Having described the invention as above, property is claimed as contained in the following

Claims (10)

1. A detergent composition, characterized in that it contains an enzyme and a salt of ethylenediaminetriacetic acid of N-acyl, wherein the acyl group is an aliphatic or aromatic group, linear or branched, containing from 1 to 40 carbon atoms.

2. The detergent composition according to claim 1, characterized in that the enzyme is selected from the group consisting of proteases, amylases, lipases and cellulases.

3. The detergent composition according to claim 1, characterized in that the enzyme is a protease.

4. The detergent composition according to claim 1, characterized in that the acyl group contains from 8 to 18 carbon atoms.

5. The detergent composition according to claim 1, characterized in that the N-acyl ethylenediaminetriacetic acid salt is an alkali metal salt.

6. The detergent composition according to claim 1, characterized in that the salt of ethylenediaminetriacetic acid of N-acyl is a salt of alkanol amine.

7. The detergent composition according to claim 1, characterized in that the N-acyl ethylenediaminetriacetic acid salt is an amino alcohol salt.

8. The detergent composition according to claim 1, characterized in that the acyl group is selected from the group consisting of lauroyl, oleoyl and nairistoyl. 3i

9. The detergent composition according to claim 8, characterized in that the acyl group is lauroyl.

10. The detergent composition according to claim 1, characterized in that it also comprises a forming agent.