Enzymatic Composition of Detergent and Substrate Treatment Process

Abstract

The invention provides an enzymatic detergent composition comprising the combination of a surfactant system; one or more enzymes and one or more lignin compounds. The invention also provides a process for treating a substrate, comprising the steps of treating the substrate with an enzymatic detergent composition comprising the combination of a surfactant system; one or more enzymes and one or more lignin compounds.

Description

"ENZYMATIC COMPOSITION OF DETERGENT AND SUBSTRATE TREATMENT PROCESS" Field of Invention The present invention relates to enzymatic detergent compositions. History of the Invention Enzymes are used in detergent formulations to aid in cleaning and stain removal. Brief Description of the Invention: The objective of the present invention is to improve the performance of enzymes in detergent formulations. Brief Description of the Figures Figure 1 graphically illustrates the data in Table 1. Figure 2 graphically illustrates the data from Table 2. Figure 3 graphically illustrates the data from Table 3. Detailed Description of the Invention In a first aspect, the present invention provides an enzymatic detergent composition comprising a combination of: i. a surfactant system; ii. one or more enzymes; and iii. one or more lignin compounds. In a second aspect, the present invention provides a substrate cleaning process comprising the step of treating the substrate with the enzymatic detergent composition according to the first aspect of the present invention. Cleaning performance is improved with the present invention. As used in this document, the term substrate includes fabric and clothing and laundry items. Consequently, the process is primarily intended for cleaning fabrics, i.e., removing stains / dirt from 30 fabrics. Preferably, the cleaning process takes place in a washing receptacle containing a washing solution comprising water and... I. Enzymatic composition of detergent. The washing solution can be applied to the substrate, or the substrate can be completely or partially immersed in the washing solution. The cleaning process may alternatively comprise the direct application of the enzymatic detergent composition (undissolved, i.e., without the addition of water) to part or all of the fabric, to directly treat a stain or stains on the fabric. This process is preferably a pre-treatment process, and may therefore be followed by treatment with / in a washing solution (for example, as a main washing process). The main washing is preferably in accordance with the second aspect of the present invention. Preferably, the process duration is less than 60 minutes, more preferably less than 30 minutes. If it is a pre-treatment process, the pre-treatment step preferably lasts less than 5 minutes 15 and, more preferably, less than 2 minutes (although cleaning by the applied enzyme will continue during at least part of any subsequent washing process). The synergistic combination according to the present invention is radically improved at low temperatures, where cleaning oil and grease stains and dirt is more problematic. Ideally, the temperature of the washing solution in the process should be less than 40°C, more preferably less than 30°C, and even more preferably less than 25°C at all times. Using a washing solution at a low temperature is both ecologically and financially advantageous. The enzymatic detergent composition is preferably a low-temperature composition. Consequently, the enzymatic detergent composition is preferably packaged with instructions on how to treat at low temperatures, where low temperatures are preferably less than 40°C, more preferably less than 30°C, and even more preferably less than 25°C. The present invention provides enzymatic performance on oily dirt and / or stains in low-temperature cleaning processes (with (F low-temperature washing solution) without serious consideration for the enzyme's temperature sensitivity. Thus, the enzyme can be selected more freely in accordance with other considerations. The present invention is particularly advantageous for the situation where enzymatic cleaning of oily dirt and / or stains is required in low-temperature cleaning processes (with low-temperature washing solution), but the compositions are, by necessity, stored at high temperatures. Psychrophilic enzymes are efficient at low temperatures but are sensitive at high temperatures due to their flexibility. Mesophilic (and thermophilic) enzymes are stable at high temperatures but have reduced performance. The present invention provides low-temperature enzymatic cleaning of a substrate using mesophilic enzymes without the need to expend effort in developing psychrophilic enzymes that can withstand high temperatures. Consequently, the enzyme system preferably comprises a system of mesophilic or thermophilic enzymes. The enzyme system may even be a system of mesophilic and / or thermophilic enzymes to the exclusion of psychrophilic enzymes. Enzymes can be of bacterial origin (derived from bacteria) 20 or fungal origin (derived from fungi), but enzymes of bacterial origin are preferred. The composition preferably comprises from 1 to 70% by weight of a surfactant, more preferably 10 to 30% by weight. Preferably, the surfactant system comprises at least 1% by weight (based on the cleaning composition) of a biosurfactant. Preferably, the biosurfactant is of bacterial origin. Preferably, the biosurfactant and the enzyme are of bacterial origin. Engineered or chemically modified mutant proteins are included. One or more enzymes can be supplied as a system. Preferably, one or more enzymes comprise a lipase. Preferred lipases include lipases from Humicola (synonym Thermomyces), for example, from H. lanuginosa (T. lanuginosus) or H. insolens, a lipase from Pseudomonas, for example, from P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis, a Bacillus lipase, e.g. from B. subtilis (Dartois et al (1993), Biochemica et Biophysica Acta, 1131, 253-360), B. stearothermophilus (JP 64 / 744992) or B. pumilus (WO 91 / 16422). Commercially available lipase enzymes include Lipolase® and Lipolase Ultra®, Lipex® (Novozymes A / S), and the bacterial enzyme, Lipomax® from Genecor. This is a lipase derived from the bacterial form of the M21L variant of Pseudomonas alcaligenes lipase as described in WO 94 / 25578 by GistBrocades (M. M. MJ Cox, H. BM Lenting, LJSM Mulleners, and JM van der Laan). Preferred phospholipases (EC 3.1.1.4 and / or EC 3.1.1.32) include enzymes that hydrolyze phospholipids. Phospholipases A1 and A2, which hydrolyze a fatty acyl group (at the sn-1 and sn-2 positions, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B), which can hydrolyze the remaining fatty acyl group into lysophospholipid, are included, as well as phospholipase C and phospholipase D (phosphodiesterases), which release diacylglycerol or phosphatidic acid, respectively. The term phospholipase A used in this document in connection with an enzyme according to the present invention is intended to cover an enzyme with phospholipase A1 and / or phospholipase A2 activity. The phospholipase activity may be provided by enzymes that also possess other activities, such as, for example, a lipase with phospholipase activity. Phospholipase can be of any origin, for example, of animal origin (such as mammalian), for example, from the pancreas (e.g., bovine or porcine pancreas), or snake or bee venom. Preferably, phospholipase can be of microbial origin, for example, from filamentous fungi, yeasts, or bacteria, such as the genera or species Aspergillus, e.g. A niger, Dictyostelium, e.g. D. discoideurrr, Mucor, e.g. M. javanicus, M. mucedo, M. subtilissimus; Neurospora, e.g. N. crassa-, Rhizomucor, e.g. R. pusillus; Rhizopus, e.g. R. arrhizus, R. japonicus, R. stolonifer, Sclerotinia, e.g. S. libertiana; Trichophyton, e.g. T. rubrum; Whetzellnia, for example, IV. sclerotiorum; Bacillus, for example, B. megaterium, B. subtilis; Citrobacter, e.g. C. freundii; Enterobacter, e.g. E. aerogenes, E. cloacae Edwardsiella, E. tarda·, Erwinia, e.g. E. herbicola; Escherichia, e.g. E. coli; Klebsiella, for example, K. pneumoniae; Proteus, for example, P. vulgaris; Providencia, for example, P. stuartii; Salmonella, for example, S. typhimurium; Serratia, for example, S. liquefaciens, S. marcescens; Shigella, for example, S. flexneri; Streptomyces, for example, S. violeceoruber; Yersinia, for example, Y. enterocolitica.Thus, phospholipase can be fungal, for example, from the class Pyrenomycetes, such as the genera Fusarium, like a strain of F. culmorum, F. heterosporum, F. solani, or a strain of F. oxysporum. Phospholipase can also be from a filamentous fungal strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger, or Aspergillus oryzae. Preferred phospholipases are derived from a Humicola strain, especially Humicola lanuginosa or a variant; and from Fusarium strains, especially Fusarium oxysporum. A phospholipase can be derived from Fusarium oxysporum DSM 2672. Preferred phospholipases comprise either a phospholipase A-1 (EC. 3.1.1.32) or a phospholipase A2 (EC. 3.1.1.4). Examples of commercial phospholipases include LECITASE® and LECITASE® ULTRA, YIELSMAX or LIPOPAN F (available through Novozymes A / S, Denmark). Commercially available protease enzymes include Alcalase®, Savinase®, Primase®, Duralase®, Dyrazym®, Esperase®, Everlase®, Polarzyme® and Kannase® (Novozymes A / S), Maxatase®, Maxacal®, Maxapem®, Properase®, Purafect®, Purafect OxP®, FN2® and FN3® (Genencor International Inc.). Other enzymes may be selected from the group comprising: cellulases, esterases, peroxidases / oxidases, oxidoreductases, pectases, lyases, mannanases and mixtures thereof. Bacterial enzymes for use in the present invention are cellulases, esterases, peroxidases / oxidases, pectases, lyases, and mannanases, or mixtures thereof. Bacterial genes encoding these enzymes can be transferred to preferred expression production hosts, which are not limited to bacteria and include, for example, other microbial hosts. Bacterial enzyme expression as used in this document includes enzymes originating from bacteria, but expressed. The composition may comprise cutinase as classified in EC 3.1.1.74. An example of bacterial cutinase is from a Pseudomonas strain, in particular Pseudomonas mendocina or Pseudomonas putida. The enzyme may be a phospholipase classified as EC 3.1.1.4 and / or EC 3.1.1.32. As used in this document, the term phospholipase refers to an enzyme that has activity on phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in the outer (sn-1) and central (sn-2) positions and esterified with phosphoric acid in the third position; in turn, the phosphoric acid may be esterified with an amino alcohol. Phospholipases are enzymes that participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be noted, including phospholipases A1 and A2, which hydrolyze a fatty acyl group (in the sn-1 and sn-2 positions, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B), which can hydrolyze the remaining fatty acyl group into lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterase) release diacylglycerol or phosphatidic acid, respectively. The term phospholipase includes enzymes with phospholipase activity, for example, phospholipase A (A1 or A2), phospholipase B activity, phospholipase C activity, or phospholipase D activity. The expression phospholipase A used in this document with respect to an enzyme according to the present invention is intended to cover an enzyme with phospholipase A1 and / or phospholipase A2 activity. Phospholipase activity can be provided by enzymes that... They also possess other activities, such as, for example, a lipase with phospholipase activity. The phospholipase activity may, for example, be that of a lipase with secondary phospholipase activity. In other embodiments of the present invention, the phospholipase enzyme activity is provided by an enzyme 5 essentially with only phospholipase activity, and in which the phospholipase enzyme activity is not a secondary activity. Preferably, the phospholipase is of bacterial origin, for example, Bacillus, B. megaterium, B. subtilis; Citrobacter, for example, C. freundii; Enterobacter, for example, E. aerogenes, E. cloacae; Edwardsiella, E. tarda; Erwinia, for example, E. herbicola; Escherichia, for example, E. coli; Klebsiella, for example, K. pneumoniae; Proteus, for example, P. vulgaris; Providencia, for example, P. stuartii; Salmonella, for example, S. typhimurium; Serratia, for example, S. liquefaciens, S. marcescens; Shigella, for example, S. flexneri. Suitable cellulases are primarily of bacterial origin. 15 Chemically modified or protein-elaborated mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, and Clostridia. Suitable peroxidases / oxidases are primarily of bacterial origin. Chemically modified or protein-elaborated mutants are included. An example of an oxidative bacterium is, but is not limited to, Aeromonas sp., from which oxidases can be derived. Examples of pectate lyases include pectate lyases that have been cloned from different bacterial genera, such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as from Bacillus subtilis (Nasser et al (1993), 25 FEBS Letts, 335: 319-326) and Bacillus sp. YA-14 (Kim et al (1994), Biosci. Biotech. Biochem. 58: 947-949). Examples of mannanases (EC 3.2.1.78) include those isolated from various bacteria, including Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol. 56, No. 11, pp. 3505-3510 (1990) describe a beta30 mannanase derived from Bacillus stearothermophilus. Mendoza et al., World J. Microbiol. Biotech. Vol. 10, No. 5, pp. 551-555 (1994) describe a betamannanase derived from Bacillus subtilis. JP-A-03047076 describes a betamannanase derived from Bacillus sp. JP-A-63056289 describes the production of an alkaline and thermostable betamannanase. JP-A-63036775 refers to the microorganism Bacillus FERM P-8856 which produces betamannanase and betamannosidase. JP-A-08051975 describes alkaline betamannanases from Bacillus sp. AM-001 alkalophilic. A purified mannanase from Bacillus amyloliquefaciens is described in WO 97 / 11164. WO 91 / 18974 describes a hemicellulase as an active glucanase, xylanase, or mannanase. The Bacillus sp. mannanases in question are found in Examples WO 99 / 64619. The composition may also include other enzymes of bacterial origin and / or enzymes that are not of bacterial origin. Lignin compounds Preferably, the lignin compound comprises a lignin polymer and, more preferably, is a modified lignin polymer. As used in this document, modified lignin polymer refers to lignin that has undergone a chemical reaction to covalently attach chemical fragments to the lignin. The attached chemical fragments are typically randomly substituted. Preferred modified lignin polymers are lignins substituted with anionic, cationic, alkoxy groups or mixtures thereof. Preferably, the substitution occurs on the aliphatic portion of the lignin and is random. Preferably, the modified lignin polymer is substituted with an anionic group, preferably a sulfonate. A preferred cationic group is a quaternary amine. Preferred alkoxy groups are polyalkylene oxide chains with repeating alkoxy moieties in the range of 5 to 30, preferably more ethoxy. Preferably, the modified lignin sulfonate is substituted with anionic or alkoxy groups. Modified lignin polymers are discussed in WO / 2010 / 033743. Most preferably, the modified lignin polymer is lignin sulfonate (lignosulfonate). Lignin sulfonate can be obtained by the Howard process. Examples of lignin sulfonate can be obtained from a variety of sources, including hardwood, softwood, recycling, or effluent streams. Lignin sulfonate can be used in pure or crude form, for example, as such, in a complete solution, or in a purified lignin sulfonate form from which or in which sugars and other saccharide constituents have been removed or destroyed, or from which or in which inorganic constituents have been completely or partially eliminated. Lignin sulfonate can be used in salt forms, including calcium lignin sulfonate, sodium lignin sulfonate, ammonium lignin sulfonate, potassium lignin sulfonate, magnesium lignin sulfonate, and mixtures or combinations thereof. Lignin sulfonate preferably has a weight-average molecular weight of 2000 to 100000. Its basic structural unit is phenylpropane. The degree of sulfonation is preferably 0.3 to 1.0 sulfate groups per phenylpropane unit. Commercially available lignin sulfonates include Ultrazine from Borregaard LignoTech. Other suppliers include Georgia-Pacific Corporation, Lenzing AG, and Tembec Inc. Lignin sulfonates are discussed in Lauten, RA, Myrvold, BO, and Gundersen, SA (2010), New Developments in the Commercial Utilization of Lignosulfonates, in Surfactants from Renewable Resources (eds. M. Kjellin and I. Johansson), John Wiley & Sons, Ltd., Chichester, United Kingdom. Surfactant a. Biosurfactants derived from bacteria Preferably, the biosurfactant comprises a rhamnolipid that may be derived from Pseudomonas sp. Other biosurfactants derived from bacteria are available in Mapping of Patents in Bioemulsifiers and Biosurfactants - analysis, published in Journal of Scientific and Industrial Research, Vol. 65, 2006, p. 91. Within the definition of biosurfactants produced by bacteria, we include those in which a bacterial gene is cloned and subsequently expressed from another organism as a manufacturing technique. For example, rhamnolipids have been produced from E. coli in this way. b. Biosurfactants from non-bacterial sources Biosurfactants within the scope of the present invention may also be derived from yeasts and fungi. Biosurfactants from non-bacterial microbial sources include those derived from yeasts and fungi, for example, sophorolipids from Candida sp. and Torulopsis sp., Candida apicola, Candida bombicola, Candida lipolytica, and Candida bogoriensis. See: Environmental Applications for Biosurfactants - Environmental Pollution, Volume 133, 2005, pp. 183-198, Catherine N. Mulligan. See also: Towards Commercial Production of Microbial Surfactants - Trends in Biotechnology, Volume 24, 2006, pp. 509-515: Soumen Mukherjee, Palashpriya Das, Ramkrishna Sen. Mannosylerythritol lipids are typically from Pseudozyma (formerly known as Candida) antarctica. Cellobiose lipids are typically from Ustilago maydis. Trehalose lipids are typically from Rhodococcus sp. Further information is provided in Production, Characterisation and Applications of Biosurfactants Review - Biotechnology - Volume 7, 2008, p. 370: Pattanathu, Rahman and Gakpe. Surfactants that are not usually classified as biological may also be included in the present invention. Nonionic surfactants include, in particular, the reaction products of compounds possessing a hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids, amides, or alkylphenols with alkylene oxides, especially isolated ethylene oxide or with propylene oxide. Specific nonionic detergent compounds are concentrates of C6a-C22 alkylphenol oxide, generally 5 to 25 EO, i.e., 5 to 25 ethylene oxide units per molecule, and the condensation products of primary or secondary linear or branched C8a-C18 aliphatic alcohols with ethylene oxide, generally 5 to 40 EO. Non-ionic detergent compounds that have been used are generally water-soluble alkaline metal salts of organic sulfates and sulfonates with alkyl radicals containing from about 8 to about 22 carbon atoms, wherein the term alkyl used includes the alkyl portion of larger acyl radicals. Examples of suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulfates, especially those obtained by sulfation of higher C8 to C8 alcohols, produced, for example, from coconut oil or tallow; sodium and potassium C9 to C20 alkyl benzene sulfonates, particularly sodium and potassium C10 to C15 alkyl benzene sulfonates; and sodium alkyl glyceryl ether sulfates, especially the ethers of higher alcohols derived from coconut oil or tallow and synthetic alcohols derived from petroleum. Preferred anionic detergent compounds are sodium C15 alkylbenzene sulfonates and sodium C12a C18 alkyl sulfates.Surfactants such as those described in EP-A-328 177 (Unilever), which show resistance to desalination, alkyl polyglycoside surfactants described in EP-A-070 074, and alkyl monoglycosides are also applicable. Preferred surfactant systems are mixtures of anionic and nonionic detergent active materials, in particular the groups and examples of anionic and nonionic surfactants indicated in EP-A-346 995 (Unilever). It is especially preferred that the surfactant system be a mixture of an alkaline metal salt of a primary alcohol sulfate C16a C18 together with an ethoxylate EO3 to 7 of a primary alcohol C12a C15. Non-ionic detergents are preferably present in quantities greater than 10%, for example, 25 to 90% by weight of the surfactant system. Anionic surfactants may be present, for example, in quantities in the range of about 5% to about 40% by weight of the surfactant system. The detergent composition may include other ingredients commonly found in laundry liquids. Especially 25 soil-releasing polymers, polyester substances, hydrotropes, opacifiers, dyes, perfumes, other enzymes, other surfactants, microcapsules of ingredients such as perfume or assistive additives, softeners, polymers for anti-redeposition of dirt, bleach, bleach activators and bleach catalysts, antioxidants, pH control agents and buffers, thickeners, 30 external structuring agents for rheological modification, visual signals, with or without incorporated functional ingredients and other ingredients known to those skilled in the art. The present invention will now be described with reference to the following non-limiting examples. Examples - All values ​​are expressed as a percentage by weight. Detergent Formulation A Ingredient % by weight Non-ionic surfactant Neodol 25-7 6.2 Anionic surfactant LAS 11.8 Anionic surfactant SLES 3EO 6.5 Lauric fatty acid P5908 5.2 Glycerol 5.0 Monopropylene glycol 9.0 Citric acid 3.9 Minor ingredients 2.0 Water balance to 100 in which: - Shell Neodol 25-7: 7-ethoxylate alcohol - C15; - LAS acid = C10-Ci4benzene sulfonic alkyl acid; - SLES = C12-C13 alcohol 3-ethoxylate sulfate, Sal Na = sodium lauryl ether sulfate (with an average of 3 ethylene oxide groups); Lipolytic enzyme (lipase) The bacterial enzyme is Lipomax® from Genecor. This is a lipase derived from the M21L variant of Pseudomonas alcaligenes lipase as described in WO 94 / 25578 by Gist-Brocades (M. M. MJ Cox, H. BM Lenting, LJSM Mulleners and JM van der Laan). Rhamnolipid The rhamnolipid is RBR425 (25% AM) from Jeneil Biosurfactant Company. Liquinoline The Lignosulfonate is Ultrazine NA from Borregaard LignoTech. Example 1 In this example, enzymatic detergent formulations according to the present invention were tested to determine their ability to treat, i.e., remove meat grease stains from cotton fabric. CS61 (from CFT BV Vlaardingen, Netherlands), which is a colored meat fat stain on cotton, was cut into round discs with a 96-cavity tissue punch and placed in the cavities of a 96-cavity microtiter plate. Stains were washed into formulations in different combinations of: i. biosurfactant as a rhamnolipid (RL) solution (water solvent) 0.9 g / L; ii. Lignin sulfonate (LS) solution (water solvent) - 3 concentrations: 10 g / L, 5 g / L, 2.5 g / L; iii. Bacterial lipase is 10 mg / L when added: 172 g of Lipomax granules are added to 50 ml of water to make a standard solution with a concentration of 100 mg / L, which is then diluted in the well to generate a final concentration of 10 g / L; and iv. Detergent formulation A is dissolved in water to generate a standard solution of 6 g / L. The microtiter cavity layout was as follows (total cavity volume of 200 µl): 1. Detergent A 100%: 100 µl of detergent A (standard of 6 g / L), 80 μl of water, 20 μl of enzymes (20 μl of water in control cavities without enzyme). 2. Detergent A 70% and rhamnolipid 0.9 g / L: 70 μL A 6 g / L standard, 30 μL 24 g / L rhamnolipid (25% active), 80 μL water, 20 μL enzyme (20 μL water without enzyme control). 3. Detergent A 70% and rhamnolipid 0.9 g / L and 10 g / L of sodium lignosulfonate: 70 μL of detergent A 6 g / L standard, 30 μL 24 g / L of rhamnolipid (25% active), 80 μL of sodium lignosulfonate 25 g / L standard, 20 μL of enzyme (20 μL of water without enzyme control). 4. Detergent A 70% and rhamnolipid 0.9 g / L and 5 g / L of sodium lignosulfonate: 70 μl of detergent A 6 g / L standard, 30 μl 24 g / L of rhamnolipid (25% active), 80 μl of sodium lignosulfonate 12.5 g / L standard, 20 μl of enzyme (20 μl of water without enzyme control). 5. Detergent A 70% and rhamnolipid 0.9 g / L and 2.5 g / L of sodium sulfonate: 70 μL of detergent A 6 g / L standard, 30 μL 24 g / L of rhamnolipid (25% active), 80 μL of sodium lignosulfonate 6.25 g / L standard, 20 μL of enzyme (20 μL of water without enzyme control). 6. Detergent A 100% and 10 g / L of sodium lignosulfonate: 100 μL of detergent A 6 g / L standard, 80 μL of sodium lignosulfonate 25 g / L standard, 20 μL of enzyme (20 μL of water without enzyme control). 7. Detergent A 100% and 5 g / L of sodium lignosulfonate: 100 μL of detergent A 6 g / L standard, 80 μL of sodium lignosulfonate 12.5 g / L standard, 20 μL of enzyme (20 μL of water without enzyme control). 8. Detergent A 100% and 2.5 g / L of sodium lignosulfonate: 100 μL of detergent A 6 g / L standard, 80 μL of sodium lignosulfonate 6.25 g / L standard, 20 μL of enzyme (20 μL of water without enzyme control). The washes were performed at room temperature, agitated at 1400 rpm for one hour in an incubator shaker. After the washing operation, the fabric discs were rinsed twice with 200 μL of demineralized water before drying at room temperature overnight in the dark. Stain removal from fabric was measured at 410 nm using a flat-bed remission spectrophotometer after washing. The results are expressed as delta remission, which was generated using CIEL*a*b (CIELAB) values ​​obtained using the Hunterlab Ultrascan VIS remission spectrophotometer. The results are shown in Table 1 below: 1 2 3 4 5 6 7 8 with Lipomax average 37.64 44.85 58.04 54.58 49.09 39.66 37.60 37.77 Standard deviation 0.56 1.35 1.75 1.78 1.63 0.92 0.84 0.42 without Lipomax average 37.15 36.10 35.86 35.42 35.97 35.67 36.27 36.30 Standard deviation 1.03 1.13 0.59 0.25 0.87 0.97 1.08 0.45 Table 1 is illustrated graphically in Fig. 1. The results show that lignin sulfonate improves stain removal by a lipolytic enzyme (exemplified by Lipomax) at low temperatures, especially when a surfactant (exemplified by rhamnolipid) is incorporated. Example 2 In this example, various enzyme / biosurfactant / lignin sulfonate compositions were examined to determine their ability to remove a range of grease and oil stains. The stains were vegetable fat stains with violet pigment and dye and lard – under medium-scale washing conditions in tergotometers. Stains used - Multi-stain pattern of 4 x 1 cm on cotton fabric: violet dye and lard, ragu and 5% sunflower oil, green curry and instant meat sauce (only results for violet dye and lard are included), stains from Warwick Equest Limited. - Vegetable fat and pigment stain, 7 x 7 cm, on polyester (CFT BV Vlaardingen, Netherlands). The stains were washed together with cotton ballast (total fabric load of 20 g, weight ratio of fabric to liquid of 1:50) in duplicate in 1-liter tergometers at 20°C (final temperature of 23°C for 30 minutes, agitation at 100 rpm). The stains were washed in formulations with different combinations of: i. biosurfactant that is rhamnolipid (RL) - 0.9 g / L when added; ii. 3 concentrations of lignin sulfonate (LS): 10, 5, 2.5 g / L when added; iii. 10 mg / L of bacterial lipase when added; iv. Detergent formulation A dissolved in water to generate 5 varying concentrations of standard solutions. The quantities of standard solutions added to the thermometers were as follows: 1. Detergent A 100%: 20 ml of detergent A (150 g / L standard solution), 10 ml of Lipomax (1 g / L) or 10 ml of water for solutions without enzyme control. 2. Detergent A 100% and 10 g / L of sodium lignosulfonate: 20 ml of detergent A (150 g / L), 10 grams of sodium sulfonate and 10 ml of Lipomax (composes x100 standard at 1 g / L) or 10 ml of water for solutions without enzyme control. 3. Detergent A and 70% rhamnolipid 0.9 g / L: 14 ml of standard detergent A (150 g / L), 50 ml of standard rhamnolipid (72 g / L) and 10 ml of standard Lipomax (1 g / L) or 10 ml of water for solutions without enzyme control. 4. Detergent A 70%, rhamnolipid 0.9% and 10 g / L of sodium lignosulfonate: 14 ml of standard detergent A (150 g / L), 50 ml of standard rhamnolipid (72 g / L), 10 grams of sodium lignosulfonate and 10 ml of standard Lipomax (see above) or 10 ml of water for solutions without enzyme control. The washes were carried out at room temperature with agitation at 1400 rpm for one hour. After the washing operation, the fabric discs were rinsed twice with 200 pL of demineralized water before being dried at room temperature overnight in the dark. The color remission of the stains was measured at 410 nm using a Hunterlab Ultrascan VIS remission spectrophotometer before and after washing. The results are expressed as delta remission, which was generated using the CIEL*a*b (CIELAB) values. Table 2 (illustrated in figure 2) — __ Violet dye and lard MTS 100% MTS 100% 10 g / L NaL MTS 70% / Ramn 0.9 g / L MTS 70% / Ramn 0.9 g / L, 10 g / L NaL with Lipomax Average 18.74 9.58 27.48 36.54 Standard deviation 1.11 2.76 3.01 3.88 Control Average 12.73 9.56 13.32 12.78 Standard deviation 2.03 2.65 2.35 2.44 Table 3 (illustrated in figure 3) MTS 100% MTS 100% 10 g / L NaL MTS 70% / Ramn 0.9 g / L MTS 70% / Ramn 0.9 g / L, 10 g / L NaL with Lipomax Average 72.64 70.59 70.87 74.44 Standard deviation 0.67 1.29 0.79 1.13 MTS 100% MTS 100% 10 g / L NaL MTS 70% / Ramn 0.9 g / L MTS 70% / Ramn 0.9 g / L, 10 g / L NaL Without Lipomax Average 63.19 63.45 64.03 65.67 Standard deviation 0.49 0.69 0.77 0.91 The results demonstrate that lignin sulfonate improves lipase performance in a detergent composition, especially when a rhamnolipid is incorporated.

Claims

1 / 2 Claims 1. Enzymatic detergent composition, characterized by comprising the combination of: i. 1 to 70% by weight of a surfactant system; ii. one or more enzymes; and iii. one or more lignin components, wherein the lignin component(s) comprise lignin sulfonate with a weight-average molar weight of 2000 to 100000, wherein its basic structural unit is phenylpropane, the degree of sulfonation being between 0.3 and 1.0 sulfate groups per phenylpropane unit; wherein the surfactant system comprises at least 1% by weight of a biosurfactant; wherein the biosurfactants are surfactants derived from bacteria, yeasts or fungi.

2. Enzymatic detergent composition, according to claim 1, characterized in that the composition is packaged with instructions for treatment at low temperatures, such that the low temperatures are below 40°C, preferably below 30°C and, more preferably, below 25°C.

3. Detergent enzyme composition, according to claim 1 or 2, characterized by comprising a mesophilic or thermophilic enzyme system.

4. Enzymatic detergent composition, according to any of the preceding claims, characterized by the biosurfactant and each enzyme being derived from bacteria.

5. Substrate treatment process, characterized by comprising the steps of treating the substrate with the enzymatic composition of detergents, as defined in any one of claims 1 to 4. Petition 870210051111, dated 07 / 06 / 2021, page 28 / 31 2 / 2 6. Process, according to claim 5, characterized in that the enzymatic detergent composition is directly applied to part or all of the fabric to treat a stain or stains on the fabric.

7. Process according to claim 5 or 6, characterized in that the substrate comprises a fabric.

8. Process, according to any one of claims 5 to 7, characterized in that the process duration is less than 60 minutes, preferably less than 30 minutes.

9. Process, according to any one of claims 5 to 8, characterized in that the temperature of the process washing solution is less than 40°C, preferably less than 30°C and most preferably less than 25°C at all times. Petition 870210051111, dated 07 / 06 / 2021, pp. 29 / 31

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