MXPA97002041A - Intensifiers such as acetosiring - Google Patents
Intensifiers such as acetosiringInfo
- Publication number
- MXPA97002041A MXPA97002041A MXPA/A/1997/002041A MX9702041A MXPA97002041A MX PA97002041 A MXPA97002041 A MX PA97002041A MX 9702041 A MX9702041 A MX 9702041A MX PA97002041 A MXPA97002041 A MX PA97002041A
- Authority
- MX
- Mexico
- Prior art keywords
- enzyme
- peroxidase
- laccase
- hydrogen peroxide
- alkyl
- Prior art date
Links
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Abstract
The present invention relates to a method for oxidizing a compound with a phenol oxidizing enzyme (for example a peroxidase or a laccase) and an enhancing agent (for example acetosyringone). The invention also relates to a detergent additive and a detergent composition
Description
INTENSIFIERS SUCH AS ACETOSIRINGONE
FIELD OF THE INVENTION
The invention relates to a method for oxidizing a compound with a phenol oxidant enzyme and an enhancing agent. The invention also relates to a detergent additive and a detergent composition.
BACKGROUND OF THE INVENTION
By phenol oxidant enzyme is meant an enzyme which through the use of hydrogen peroxide or molecular oxygen, is capable of oxidizing organic compounds containing phenolic groups. Examples of such enzymes are peroxidases and oxidases. In principle it has been found that colored substances leached from dyed fabrics could be bleached by means of a phenol oxidant enzyme. The use of peroxidases or oxidases to inhibit dye transfer in this manner is described in WO 91/05839. Certain oxidizable substances, for example, metal ions and phenolic compounds such as 7-hydroxycoumarin, vanillin, and p-hydroxybenzenesulfonate, have
REF: 24186 bido described as accelerators or enhancing agents < The enzymatic bleaching reactions can be intensified (see, for example, WO 92/18683, WO 92/18687, and Kato M and Qiimizu S, Plain Cell Physiol. 1985 26 (7), pp. 1291-1301 'see Table 1 in particular)). Other types of enhancing agents are described in WO 94/12621, for example, phenothiazines and phenoxazines. The object of this invention is to provide a novel group of enhancing agents, which are effective to enhance the phenol oxidant enzymes.
BRIEF DESCRIPTION OF THE INVENTION
It has surprisingly been found that a novel group of organic chemicals functions excellently as enhancers of the phenol oxidant enzymes. This novel group of organic chemicals not only makes the bleaching reactions faster compared to the use of the phenol oxidant enzyme alone, but many compounds that could not be bleached then, can now be bleached by using the method of the invention.
Accordingly, the invention provides a method for oxidizing a compound with a phenol oxidant enzyme, characterized by the presence of an enhancing agent of the following formula:
formula in which A is a group such as -D, -CH = CH-D, -CH = CH-CH = CH-D, -CH = ND-, -N = ND, or -N = CH-D, wherein D is selected from the group consisting of -CO-E, -SO2-E, -N-XY, and -N * -XYZ, in which E can be -H, -OH, -R, or - OR, and X and Y and Z may be identical or different and selected from 5 -H and -R; R is a C? -C? 6 alkyl, preferably C: -Ce alkyl, alkyl which can be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C can be the same or different and can be selected from the CmH2m + group? 1 < m < 5. 20
BRIEF DESCRIPTION OF THE DRAWINGS
The present invention is best illustrated by
¿. D reference to Figure 1, which shows Acid Blue bleaching 45 added gradually in phosphate / borate buffer pH 10 at 35 ° C; (I): Only the addition of dye; (II): The addition of dye in the presence of Laccasa; (III): The addition of dye in the presence of Laccase + Acetosyringone; the experiment was conducted as described in Example 8.
DETAILED DESCRIPTION OF THE INVENTION
The present invention relates to a method for oxidizing a compound with a phenol oxidant enzyme, characterized by the presence of an enhancing agent of the following formula:
formula in which A is a group such as -D, -CH = CH-D, -CH = CH-CH = CH-D, -CH = ND-, -N = ND, or -N = CH-D, in which D is selected from the group consisting of -CO-E, -S02-E, -N-XY, and -N + -XYZ, in which E can be -H, -OH, -R, or -OR , and X and Y and Z may be identical or different and selected from -H and -R; R is a Ci-Cie alkyl, preferably C -C alkyl, alkyl which may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C can be the same or different and can be selected from the group of CmH2m + ?; 1 < m < 5. In a preferred embodiment A in the aforementioned formula is -CO-E-, in which E can be -H, -OH, -R, or -OR; R is a C 1 -C 6 alkyl, preferably a C 1 -C 8 alkyl, alkyl which may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C can be the same or different and be selected from CmH2m + ?; 1 < m < 5. In the formula mentioned above A, the hydroxy group can be placed in place instead of being placed in the para position as shown. In the particular embodiments, the enhancing agent is acetosyringone, syringaldehyde, methylsicylate, syringic acid, ethylsicylate, propylsyranthate, butylsicylate, hexylsicylate, octylsyarnate or ethyl 3- (4-hydroxy-3,5-dimethoxyphenyl) acrylate. The enhancing agent of the invention may be present in concentrations of 0.01 to 1000 μM, more preferably 0.1 to 250 μM, most preferably 1 to 100 uM.
Preparation of Intensifying Agents
The enhancing agents described herein may be prepared using methods well known to those skilled in the art; Some of the age intensifiers are also available commercially. No others produce methylsicylate, ethylsicylate, propylsalicylic acid, butylsicylate, hexylsicylate and octylsiring, or using the method described in Chem. Ber. 67, 1934, p. 67. Ethyl 3- (4-hydroxy-3, 5-dimethoxyphenyl) acrylate was synthesized from tinghyl syringaldehyde and phosphonoacetate in ethanol / sodium ethanolate. The product was further purified and characterized by ^ -RMN and 13C-NMR (showing the expected spectrum) and the melting point was 68-70 ° C.
Hydrogen Peroxide / Oxygen
If the phenol oxidizing enzyme requires a source of hydrogen peroxide, the source can be hydrogen peroxide or a hydrogen peroxide precursor for the production of hydrogen peroxide itself, for example percarbonate or perborate, or an enzymatic system generator of hydrogen peroxide, eg, an oxidase and a substrate for oxidase, 001 for example, an amino acid oxidase and a suitable amino acid, or a peroxycarboxylic acid or a salt thereof. Hydrogen peroxide should be added at the start or during the process, eg, in an amount corresponding to the levels of 0.001-25 mM, particularly at the 0.01-1 mM levels. S 'the phenol oxidant enzyme requires molecular oxygen, the molecular oxygen of the atmosphere will generally be prt; ite in sufficient quantity. If more O is necessary, additional oxygen can be added.
Oxidizing Enzyme of Phenol
In the context of the present invention the enzyme of the phenol oxidant enzyme can be an enzyme possessing peroxidase activity or a laccase or a laccase related to the enzyme as described below.
Peroxidases and Compounds that possess Peroxidase Activity
The compounds possessing peroxidase activity can be any enzyme peroxidase comprised by the enzymatic classification (EC 1.11.1.7), or any fragment derived therefrom, exhibiting peroxidase activity, or synthetic or semi-synthetic derivatives thereof ( for example porphyrin ring systems or icroperoxidases, see, for example, the North American Patent: -> No. 4,077,768, Patent Application EP 537,381, International Patent Applications WO 91/05858 and WO 92/16604) . Preferably, the peroxidase employed in the method of the invention is produced by plants (for example horseradish peroxidase or soybean) or microorganisms such as fungi or bacteria. Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hyphomycetei », for example Fusarium, Humicola, Trichoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicus and solens, Trichoderma resii, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fu ago, Ulocladium chartarum, Embellisia alli or Dreschlera halodes. Other preferred fungi include strains belonging to the subdivision Basidiomycotina, class
Basidiomycetes, for example Coprinus, Phanerochaete, Coriolus or Trametes, in particular Coprinus cinereus f. icrosporus
(IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (for example NA-12) or Trametes (formerly Polyporus), for example T. versicolor (for example PR4 28-A). Additional preferred fungi include strains belonging to the subdivision Zygomycotina, class Mycoraceae, for example Rhizopus or Mucor, in particular Mucor hiemalis. . Some preferred bacteria include strains of the order of Actinomycetales, for example, Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or S reptoverticillum verticilliu ssp. verticillium. Preferred bacteria include Bacillus pumilus (ATCC 12905), Bacillus stearothermophilus,
Rhodobacter sphaeroides, Rhodomonas palustri, Streptococcus lactis, Pseudomonas purrocinia (ATCC 15958) or Pseudomonas fluorescens (NRRL B-ll). Additional preferred bacteria include strains that pretend to Myxococcus, for example M. virescens. The peroxidase may also be one that is produced by a method comprising culturing a host cell transformed with a recombinant DNA vector, which contains a DNA sequence coding for peroxidase as well as DNA sequences encoding functions that allow the expression of the DNA sequence coding for peroxidase, in a culture medium under conditions that allow peroxidase expression and recover the peroxidase from the culture.
Particularly, peroxidase produced in a recombinant manner is a peroxidase derived from Coprinus sp., In particular C. macrorhizus or C. cinereus according to WO 92/16634. In the context of this invention, the compounds possessing peroxidase activity comprise the peroxidase enzymes and active fragments of peroxidase derived from cytochrome, hemoglobin or peroxidase enzymes, and synthetic or semi-synthetic derivatives thereof, for example, iron porphyrins and phthalocyanines of iron and derivatives thereof.
Determination of Peroxidase Activity (PODU)
1 unit of peroxidase (PODU) is the amount of enzyme that catalyzes the conversion of 1 μmol of hydrogen peroxide per minute in the following analytical conditions: hydrogen peroxide 0.88 mM, 2, 2'-azinobis (3-ethylbenzthiazolin-6-) sulfonate) 1.67 mM, 0.1 M phosphate buffer, pH 7.0, incubated at 30 ° C, followed photo-electrically at 418 nm.
Laccasa and Enzymes Related to Laccasa
In the context of this invention, the laccases and enzymes related to laccase comprise any enzyme laccase comprised by the enzymatic classification (EC 1.10.3.2), any enzyme catechol oxidase comprised by the enzymatic classification (EC 1.10.3.1), any bilirubin enzyme oxidase comprised by the enzymatic classification (EC 1.3.3.5) or any monophenol r 'monooxygenase enzyme comprised by the enzymatic classification (EC 1.14.99.1). The enzymes mentioned above can be derived from plants, bacteria or fungi (including filamentous fungi and yeasts) and suitable examples include
• '' a laccasa derivable from a strain Aspergillus, Neurospora, for example N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, for example T. villosa and T. versicolor, Rhizoctonia, for example, R Solani, Coprinus, for example, C. cinereus, C. comatus, C. friesii, and C ^;, plicatilis, Psathyrella, for example, P. condelleana, Panaeolus, for example, P. papilionaceus, Myceliophtora, for example, M. thermophila, Schytalidium, Polyporus, for example P. pinsitus, Phlebia, for example, P. radita (WO 92/01046), or Coriolus, for example, C. hirsutus (JP 2-238885). The laccase or enzyme related to laccase can also be one that is produced by a method comprising culturing a host cell transformed with a recombinant DNA vector, which contains a DNA sequence encoding laccase as well as a sequence de .- DNA that codes for functions that allow the expression of the DNA sequence that codes for laccase, in a medium of culture under conditions that allow the expression of the enzyme laccase and recover the laccase of the culture. V
Determination of Laccasa Activity (LACU)
The activity of laccase was determined from the oxidation of syringaldazine under aerobic conditions. The violet color produced was measured photometrically at 530 nm. The analytical conditions are syringaldazine 19 uM, acetate buffer 23.2 mM, pH 5.5, 30 ° C, reaction time 1 minute. 1 unit of laccase (LACU) is the amount of enzyme that catalyzes the conversion of 1.0 μmol of syringaldazin per minute to these conditions.
Industrial Applications
In a preferred embodiment, the method of the invention finds application for raising a textile dye or textile dyes or colorants in solution. Dyes and dyes are broad classes of natural and synthetic compounds. The following description and examples of dyes / colorants are not intended in any way to limit the scope of the invention as claimed: The synthetic textile dyes bleachable by the method of the invention are typically azo compounds (with one or more azo, or diazendiyl groups) ), as exemplified by Acid Red 151, Direct Blue 1, Direct Brown 44, and Orange II, or anthraquinone compounds, as exemplified by Acid Blue 45:
Acid Red 151
Direct Blue 1
Direct Brown 44
Orange II
Acid Blue 45
Other structural motifs may occur along with those, as exemplified in the formula of Reactive Blue 19: Reactive Blue 19
CH2CH2OS? 3Na Some dyes also contain groups capable of coupling to the surfaces of the fabric (reactive dyes), and some dyes are complexed with metal ions. Those modifications will often not infer the applicability of the present invention. A different structure bleachable by the method of the invention is the Indigo portion, exemplified herein by indigo soluble carmine dye:
Indigo Carmina
Other dyes and dyes may be of natural origin or they may be synthesized as identical structures or made from natural syrups. Examples of categories of colored substances extractable from plant sources are the polyphenolic, anthocyanin and carotenoid compounds. A specific embodiment of the present invention is provided by the domestic and institutional washing process. In such washing and rinsing processes, the dyes and colorants present in the fabrics can be leached into the wash or rinse liquor resulting in discoloration in the wash. The bleaching of the colored compounds in solution by the method of the invention can counteract this undesirable effect. The technique is known in other systems to inhibit dye transfer (for example WO 91/05839). In another specific embodiment, the bleached dyes in the process water during text processing can be bleached by the method of the invention to prevent undesirable deposition. In the art it is known in other systems (for example WO 92/18697). In a third modality, the method of the invention finds application in the bleaching of paper for the production of paper. Accordingly, the invention provides a method for bleaching for lignin-containing material, in particular pulp bleaching for the production of paper, which method comprises the treatment of lignin or the material containing lignin with a phenol oxidant enzyme. and an intensifying agent according to what is described in the present invention. In a fourth embodiment, the method of the invention finds application for the modification of lignin, for example in the manufacture of wood compositions, for example wood fiber materials such as gray cardboard, hardboard boards made of wood particles, or in the manufacture of laminated wood products, such as laminated beams and plywood.
In a fifth embodiment, the method of the invention finds application in the treatment of waste water, for example sewage from the chemical or pharmaceutical industry, from "the manufacture of dyes, dyeing works, textile industry, or pulp production
(see for example US 4,623,465, or JP-A-2-31887). In a more specific aspect, the invention provides a method for the treatment of waste water from the manufacture of dyes, dyeing works, the textile industry, or the manufacture of pulp, the method comprises the treatment of waste water with a phenol oxidant enzyme in the presence of an enhancing agent of the invention. In the processes mentioned above and in other applications of the invention, the enhancing agent can be added at the beginning of the process or later, in one or several additions. According to the invention, the phenol oxidant enzyme can be present in concentrations of 0.001-100 mg of enzyme protein per liter.
Detergent compositions
According to the invention, the enhancing agent and the phenol oxidant enzyme can typically be a component of a detergent composition. Such, it can be included in the detergent composition in the form of a detergent additive. Preferred additive detergent formulations are granules in particular non-powdery, liquid granules, in particular stabilized liquids or suspensions. Non-powdery granules can be produced, for example, as described in US 4,106,991 and 4,661,452 (-rabas by Novo Industri A / S) and can optionally be coated by methods known in the art. Examples of coating materials of waxy consistency are the products of poly (ethylene oxide) (polyethylene glycol, PEG) with average molecular weights of 1000 to 2000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are from 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono-, di- and triglycerides of fatty acids. Examples of coating materials that form films suitable for application by fluidized bed techniques are given in patent GB 1483591. Liquid enzyme preparations can, for example, be stabilized by the addition of a polyol such as propylene glycol, a sugar or an alcohol, lactic acid or boric acid according to established methods. Other enzyme stabilizers are well known in the art. Protected enzymes can be prepared according to the methods described in EP 238,216. The detergent composition of the invention may be in any convenient form, for example, powder, granules, paste or liquid. A liquid detergent can be aqueous, typically containing up to 70% water and 0-30% organic solvent, or non-aqueous solvent. The detergent composition comprises one or more surfactant, each of which may be anionic, nonionic, catonic, or zwitterionic. The detergent will usually contain 0-50% anionic surfactant such as linear alkylbenzene sulfonate (LAS), alpha-olefin sulphonate (AOS), alkyl sulfate (fatty alcohol sulfate) (AS), alcohol ethoxysulfate (AEOS or AES), secondary alkan sulfonates ( SAS), methyl esters of fatty alpha-sulfo acid, alkyl- or alkenyl-succinic acid, or soap. This may also contain 0-40% nonionic surfactant such as ethoxylated alcohol (AEO or AE), carboxylated alcohol ethoxylates, nonylphenol ethoxylates, alkyl polyglycoside, alkyldimethylamine oxide, ethoxylated fatty acid monoethanol amide, fatty acid iaonoethanolamide, or polyhydroxy alkyl fatty acid amide (for example as described in WO 92/06154?
The detergent composition may additionally comprise one or more other enzymes, such as amylases, lipases, cutjnases, proteases, and cellulases. The detergent may contain 1-65% of a detergent adjuvant or complexing agent such as zeolite, d-phosphate, triphosphate, phosphonate, citrate, isothriatriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminpentaacetic acid (DTPA), alkyl- or alkenyl-succinic acid, soluble silicates or layered silicates (for example, SKS-6 from Hoeschst). The detergent can also be non-adjuvant gel, ie essentially free of detergent adjuvant. The detergent may comprise one or more polymers. Examples are carboxymethylcellulose (CMC), poly (vinyl pyrrolidone) (PVP), polyethylene glycol (PEG), polyvinyl alcohol (FVA), polycarboxylates such as polyacrylates, maleic / acrylic copolymers and lauryl methacrylate / acid copolymers acrylic. The detergent may additionally contain other bleaching systems which may comprise a source of H, _02 such as perborate or percarbonate, which may be combined with a peracid-forming bleach activator such as tetraacetylethylenediamine (TAED) or nonanoyloxybenzenesulfonate (NOBS). Alternatively, the bleach system may comprise peroxyacids of, for example, the type of amide, imide, or sulfone. The enzymes of the detergent composition of the invention may be stabilized using stabilizing agents conventional, for example a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid or a boric acid derivative such as, for example, an aromatic borate ester, and the composition can be formulated as described in, for example, WO 92/19709 and WO 92/19708. The detergent may also contain other conventional detergent ingredients such as, for example, fabric conditioners including clays, generating foam suppressors sudsing, anticorrosion agents, soil suspending agents, soil antiredeposition, dyes, bactericides, optical brighteners or perfume. The pH (measured in aqueous solution at the use concentration), usually should be neutral or alkaline, for example, in the range of 7-11. Particular forms of the detergent compositions within the scope of the invention include: 1) A detergent composition formulated as a granulate comprising a bulk density of at least 600 g / 1 of composition
2) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
3) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
LÍ3 4) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
) An aqueous liquid detergent composition comprising
€) A composition of liquid detergent, structured aqueous, comprising
7) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
8) A detergent composition formulated as a granulate comprising
9) A detergent composition formulated as a granulate comprising
) An aqueous liquid detergent composition comprising
11) An aqueous liquid detergent composition, comprising
12) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
13) Detergent formulations as described in 1) -12) where all or portions of linear alkylbenzenesulfonate are replaced by alkyl sulfate (C? 2-C? 8).
14) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
) A detergent composition formulated as a granulate having a bulk density of at least 600 g / 1 comprising
16) Detergent formulations as described in 1) -15) which contain a stabilized or encapsulated peracid, either as an additional component or as a substitute for the bleaching systems already specified.
17) The detergent compositions as described in the inserts 1), 3), 7), 9) and 12) wherein the perborate is replaced by percarbonate.
8) Detergent compositions as described in
1 i, 3), 7), 9), 12), 14) and 15), which additionally contain a manganese catalyst. The manganese catalyst may, for example, be one of the compounds described in "Manganese catalysts efficient for bleaching at low temperature", Nature 369, 1994, p. 637-639.
19) A detergent composition formulated as a non-aqueous detergent liquid comprising a liquid non-ionic surfactant such as, for example, linear alkoxylated primary alcohol, an adjuvant system (eg phosphate), enzyme and alkali. The detergent may also comprise anionic surfactant and / or a bleach system. The following examples better illustrate the present invention, and are not intended to be in any way limiting the scope of the invention as claimed.
EXAMPLE 1
Blanqueado del Azul Directo 1 with soy peroxidase and with acetosyringone
A crude soy peroxidase (SBP), obtained from Mead Corp., Dayton, Ohio, was purified by anionic and cationic chromatography followed by gel filtration to a single protein on SDS-PAGE with a value of R7 (A04nm / A280nm)
125 nm of crude SBP were adjusted to pH 7, diluted to 2.3 mS and filtered through a 0.8μ filter. The sample was applied to the DEAE 300 ml column equilibrated with 20 mM phosphate pH 7.0 and the peroxidase was eluted with a linear gradient of 1 M NaCl in the same buffer. Fractions with peroxidase activity were pooled. The combined fractions of the anion exchange chromatography (190 ml) were concentrated and washed by ultrafiltration (GR61PP membrane from Dow, Denmark). The pH was adjusted to an ionic strength of 5.3 to 2.3 mS in the sample before application to a 200 ml S-Sepharose column previously equilibrated with 50 mM acetate pH 5.3. The effluent containing the peroxidase activity was concentrated and washed by ultrafiltration to a final volume of about 10 ml. 5 ml of concentrated sample of cation exchange chromatography was applied to a 90 cm Sephacryl S-200 column equilibrated and eluted with 0.1 M acetate pH 6.1. Fractions with peroxidase activity that gave only one band on SDS-PAGE were pooled. The bleaching speed of Direct Blue 1 (DB1) by the purified SBP was determined using an intensifier according to the invention. The following conditions were used:
Final Concentration - 200 μl of Britton-Robinson 50 mM buffer * pH 6, 8 and 10, respectively 10 mM
200 μl of DB1 ~ 3.0 Units Abs. 0.6 (A6? 0nm) (610 nm) i i 200 μl SBP with A404nm = 0.0005 at pH 6 and 8 with A4G, M = 0.005 at pH 10 0.0001 or 200 μl intensifier 50 μM 10 μM
200 μl of H202 100 μM 20 μM
* (50 mM acetic acid, 50 mM phosphoric acid, 50 mM boric acid, pH adjusted to the value of interest with NaOH). * Corresponding to approximately 0.04 mg / l and 0.4 mg / l. The reagents were mixed in a cuvette in a regulated form at 30 ° C and bleaching was started by adding hydrogen peroxide. Blanking was detected spectrophotometrically at 610 nm, which is the wavelength of the absorption peak of DB1. Blanching was followed for 4 minutes, and the reduction in absorbance was determined
(lüOX / Aei n, i, initial- iQnn, 4 run.) / g Onm, initial *) • The A6? onm, imciai was determined by replacing hydrogen peroxide with "water.
Table 1
Blanqueado del Azul Directo 1 with SBP in 4 Minutes
From the results presented in Table 1 above, it appears that by adding an intensifier of the invention a much faster bleaching of the dye is obtained compared to the experiment without intensifier.
EXAMPLE 2
Bleaching of Direct Blue 1 with Coprinus cinereus peroxidases with and without enhancers.
A Coprinus cinereus peroxidase (CiP) obtained as described in WO 9412621 was used. The described dilutions were made in a solution of 0.15 grams / 1 of Triton X-405. The bleaching speed of the Direct Blue 1 (DB1) by itself purified was determined using the following conditions:
Final concentration
200 μl of Britton buffer - 10 mM Robinson 50 mM * 200 μl of DB1 - 3.0 Units Abs. 0.6 (A6? 0n) (610 nm) 200 μl of CiP 0.40 mg / l (pH 8.5) 0.08 mg / l (pH 8.5) or
CiP 0.80 mg / l (pH 10.5) 0.16 mg / l (pH 10.5)
200 μl intensifier 25 μM 5 μM 200 μl H.02 100 μM 20 μM * (50 mM acetic acid, 50 mM phosphoric acid, 50 mM boric acid, the pH was adjusted to the value of interest with NaOH).
The reactants were mixed in a thermoregulated bucket at 30 ° C and the bleaching was started by the addition of hydrogen peroxide. The bleaching was detected spectrofometrically at 610 nm, which is the wavelength of the absorption peak of DB1. Bleaching was followed for 1 minute, and the initial reduction in absorbance was determined, from? MAbs / minute.
Table 2
Initial whitening of Azul Directo 1 with CiP
Intensifier -? MAbs / miñuto pH: 8.5 10.5 Acetosingone 239 1 Syruphaldehyde 151 4 Methylsicylate 245 8 Without intensifier 2 0
From the results presented in Table 2 above, it seems that by adding an intensifier of the invention, a much faster bleaching of the dye was obtained compared to the experiment without intensifier. Even at pH 10.5 significant bleaching was obtained with an intensifier of the invention, while bleaching could not be observed in all cases without the addition of an intensifier.
EXAMPLE 3
Bleaching of Chicago Sky Blue 6B (CSB) with Coprinus cinereus peroxidase and intensifiers
The bleaching tests were carried out in exactly the same manner as described in Example 2 except that instead of using DBl, Chicago Sky Blue (CSB) (obtained from Aldrich) was used, and the following enhancers were tested: methylsicylate ethylsicylate propylsingate butylsyrethacrylsilyate-octyl-octylationate 3- (4-hydroxy-3, 5-dimethoxyphenyl) -ethyl acrylate. The following results were obtained:
Table 3 Initial Bleaching of CSB with CiP
Intensificaclor -? MAbs / minute pH: 8.5 10.5 Methylsiureate 211 42 Ethylsicylate 240 52 Propylsiirbate 228 60 Butylesiureate 228 48 Hexylbisicylate 276 36 Octylsyarnate 192 15 3- (4-Hydroxy-3, 5-dimethoxy-phenyl) ethyl acrylate 48 48 Without enhancer 8 6
EXAMPLE 4
Bleaching of Direct Blue 1 (DBl) using several laccases of Coprinaceae and metilsiringate at pH 5.5-8.5.
Bleaching of Direct Blue 1 at various pH values was conducted using a laccase obtained from Coprinus comatus, Coprinus friesii, Coprinus plicatilis, Panaeolus papilionaceus or Psathyrella condolleana and methylsicylate. The strains mentioned above were fermented as follows: Strains were inoculated on PDA agar plates
(PDA: potato dextrose agar 39 g / 1) and were grown at 26 ° C for 3 clias. The shake flasks were then inoculated with 6-8 small squares (~ 0.5 cm x 0.5 cm) of agar containing mycelium. and fermented for 3-10 days at 26 ° C and 200 rpm using the following medium:
No. of Deposit of the Half Growth
Coprinus comatus * CBS 631.95 to 10 days
Coprinus friesii CBS 629.95 3 days Panaeolus papilionaceus CBS 630.95 10 days
Psathyrella condolleana CBS 628.95 B 7 days
Coprinus plicatilis CBS 627.95 to 8 days
* All the strains mentioned in this Example had already been deposited according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedures, on August 16, 1995, at Centraalbureau voor Schi melcultures, Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, The Netherlands, under the Access numbers mentioned above.
Means: A: soy flour 30 g / 1 maltodextrin 15 g / 1 bacto peptone 5 g / 1 pluronic 0.2 g / 1 10 B: potato flour 50 g / 1 barley flour 25 g / 1 BAN 800MG * 0.025 g / 1 caseinate Na 5 g / 1 crushed soybeans 10 g / 1., 5 Na2HP04, 12 H20 4.5 g / 1 Pluronic 0.05 ml / 1 * BAN 800MG obtainable from Novo Nordisk A / S.
After fermentation the culture broths were centrifuged and the supernatants were used in the tests described below. The bleaching speed of DBl was determined using the following conditions:
¿. or Final Concentration
400 μl of Britton-Robinson 50 mM * buffer, (pH 5.5, 7.0, and 8.5 respectively) 20 mM 200 μl of DBl - 3.0 Units Abs. 0.6 (A610nm) (610 nm)
200 μl of 50 μM methylsicylate 10 μM
200 μl of laccase at pH 5 and 7: 4 LACU / 1 at pH 8.5: 20 LACU / 1 0
* (50 mM acetic acid, 50 mM phosphoric acid, 50: 1 boric acid, pH adjusted to the value of interest with NaOH). The reagents were mixed in a thermoregulated cuvette of 1 ml at 30 ° C and the bleaching was started
J5 by the addition of laccase. The bleaching was followed electrically spectrofot at 610 nm, which is the wavelength of the DB1 absorption peak, with readings every 5 seconds for a period of 5 minutes. The initial bleaching speed was determined from the
linear part of the absorbance curve. The following results were obtained with ethyl syringate: -? MAbs / minute Laccasa pH; 5.5 7.0 C. comatus 33 23 2 C. friesii 40 55 61 Pan. Papilionaceus 16 19 18 Ps. condolleana 45 54 43 C. plicalitis 42 39 14
The following results were obtained without intensifier: -? MAbs / minute Laccasa pH: 5.5 7.0 8.5 C. comatus 0 0 or C. friesii 0 0 or Ps. condolleana 0 o o C. plicalitis 0 o o
EXAMPLE 5
Bleaching of Direct Blue 1 (DBl) using Coprinus cinereus laccase with / without intensifying agents at pH 5.5-8.5.
Bleaching of Direct Blue dye at various pH values was controlled using Coprinus cinereus laccase and one of the following inter alia agents: None acetosyringone iringaldehyde methylsicylate The laccase was obtained as follows: Coprinus cinereus was inoculated (IFO 30116 - freely available to the pc of the Fermentation Institute, Osaka (IFO) under the indicated deposit number) of a slice of PDA agar (PDA: 39 g / 1 of potato dextrose agar) in a 100 ml shake flask containing medium A (Medium A is described in Example 3). The culture was cultivated for 6 days at 26"C and 100 rpm A 10-liter fermenter containing medium A was inoculated with 100 ml of culture broth The fermentation was carried out for 6 days at 26 ° C and 100 rpm. The culture broth was filtered and concentrated by ultrafiltration The additional purification was carried out using hydrophobic interaction chromatography followed by anion exchange chromatography This process resulted in a preparation with a laccase activity of 3.6 LACU / ml. was> 80% based on the protein.The bleaching speed of the DB1 was determined using the following conditions:
Final concentration 400 μl of Britton-Robinson buffer 50 mM * ípH 5.5, 7.0 and 8.5 respectively), 20 mM 200 μl of DBl - 3.0 Units Abs. (610 nm) 0.6 (As10nm)
200 μl intensifying agent 50 μM 10 μM 200 μl laccase C. cinereus 1 mg / l
* (50 mM acetic acid, 50 mM phosphoric acid, 50 mM boric acid, pH adjusted to the value of interest with NaOH). The reagents were mixed in a thermoregulated cuvette of 1 ml at 30 ° C and the bleaching was started by the addition of laccase. The bleaching was followed spectrophotometrically between
610 nm, which is the wavelength of the DB1 absorption peak, with readings every 5 seconds for a period of 5 minutes. The initial bleaching speed was determined from the first linear part of the absorbance curve. The following results were obtained:
Intensifying agent - mAbs / minute pH: 5.5 7.0 8.5 none 13 5 3 acetosyringone 28 94 50 syringaldehyde 29 79 28 metilsiring to 20 94 57 EXAMPLE 6
Bleached Direct Blue (DBl) using Coprinus cinereus laccase and acetosyringone r The bleaching of Direct Blue 1 dye at various pH values was conducted using Coprinus cinereus laccase and acetosyringone intensifying agent. Laccase was obtained as described in i) Example 5. The bleaching speed of DB1 was determined using the following conditions: Final concentration 400 μl of Britton-Robinson 50 mM * buffer (pH 4.5, 6.7, and 8 respectively), 20 mM 200 μl DPI - 3.0 Units Abs (610 nm) 0.6 (A? ion 200 μl acetosyringone 50 μM 10 μM 200 μl laccase C. cinereus 3.2 mg / l
(50 mM acetic acid, 50 mM phosphoric acid, 50 mM boric acid, pH adjusted to the value of interest with NaOH).
The reagents were mixed in a thermoregulated cuvette of 1 cm at 30 ° C and the bleaching was started by the addition of laccase.
The blanching was detected spectrophotometrically at 610 nm, which is the wavelength of the absorption peak of the DB1. 5 seconds later the blanching was followed for 4 minutes. Sv_ obtained the following results: Bleached from DBl -.ni to PH (-? MAbs / min) (% of the value at pH 7) 4 18% 5 13% 6 35% 7 100% 8 69%
It can be seen from the results given above that optimum bleaching was achieved at a pH around 7, but the system also shows an effective bleaching at pH 8.
EXAMPLE 7
Blanqueado del Azul Directo 1 with laccasa de Trametes villosa with and without intensifying agents
Laccasa obtained from Trametes villosa: 800 ml of Trametes villosa culture broth, CBS 678.70, was filtered with a filter aid to give a clear filtrate, which was concentrated and washed by ultrafiltration on a membrane with a cut of 6-8 kDa. . Samples of one ml of concentrated preparation were applied on a Q-Sepharose HP column (Pharmacia, Sweden) equilibrated with 0.1 M phosphate at pH 7, and the laccase was eluted with a linear NaCl gradient around c 0.25 M. Fractions with laccase activity of 10 trials were pooled and concentrated by ultrafiltration at an activity of 500 LACU / ml. The following conditions were used: Final concentration 400 μl of 50 mM Britton-Robinson buffer * (pH 5.5 and pH 7.0 respectively), 20 mM 200 μl of DBl ~ 3.0 Units of Abs. (610 nm) ° -6 (Asió ™,) 200 μl of go counter 50 μM 10 μM 200 μl Enzyme dilution
* (50 mM acetic acid, 50 mM phosphoric acid, 50 mM boric acid, pH adjusted to the value of interest with NaOH). The reagents were mixed in a thermoregulated cuvette of 1 cm at 30 ° C and the bleaching was started by the addition of enzyme. Bleaching was detected spectrophotometrically at 610 nm, which is the peak of DBL absorption. 5 seconds later, the blanching was followed for 4 minutes.
From the results presented below, it appears that with the addition of the intensifiers of the invention it was possible to obtain a faster dye bleaching compared to the experiment without intensifier. The doses of enzyme given are in the final incubation mixture.
Bleaching of Direct Blue 1 with Trametes villosa laccase, obtained as described above, at pH 5.5 (1.6 mg / l) and pH 7.0 (16 mg / l):
Bleaching of DBl in 4 minutes Intensifier (-? MAbs / 4 min) pH 5.5 pH 7.0 Without enhancer 0 0 Acetosyringone 447 242 Syruphaldehyde 438 112
EXAMPLE 8
Bleaching of Acid Blue 45 gradually added with Coprinus cinereus laccase with and without intensifying agent
Ideally, the dye transfer inhibition system for laundry applications should be tested in a real wash where the dyed fabrics release dye to the wash solution as a result of the combined action of the detergent, temperature and mechanical agitation. that takes place. To simulate such a process, however, a flask with magnetic stirring was used as a reaction vessel and the dye was added gradually from the standard solution (using a Metrohi 725 dosimat). The solution was verified electrically using a Zeiss multi-channel spectrometer (MCS) equipped with an inverter probe. optical fiber. The acetosyringone standard solutions were prepared in a suitable water / ethanol mixture. The blue acid 45 anthraquinone dye standard solutions were made with water. '.5 Laccase was recovered from the fermentation of 10 liters of Coprinus cinereus (IFO 30116) as described in Example 4. The following conditions were used in the experiment: 0 Temperature: 35 ° C Medium and pH: phosphate buffer / 50 mM / 50 mM borate at pH 10 Acetosyringone (when applicable): 10 μM 25 Laccase: 10 mg / l Dye addition program: linear addition at a rate of 0.34 abs / 40 min, which refers to the absorbance from Acid Blue 45 to its maximum absorbance wavelength (590 nm for Acid Blue 45). Figure 1 shows the results of the bleaching tests. The following symbols were used: (I): Only addition of dye; (II): Addition of dye in the presence of Laccasa; (III): Addition of dye in the presence of Laccasa + acetosyringone. It can be seen from Figure 1 that the effect of bleaching is encouraged by acetosyringone.
EXAMPLE 9
Inhibition of Tint Transfer Using Laccasa from Coprinus cir.erius
A small-scale experiment was carried out in which clean cotton test pieces were washed together with fabrics that faded in the wash solution, the experiment was conducted in the absence and presence of laccase and enhancing agent. After washing, the Kunter color differences between the aforementioned cotton pieces and clean pieces of cotton (washed in the absence of fading fabrics) were measured and measured as the degree of dye transfer resulting from washing.
Used materials :
Faded fabrics dyed with Acid Red 151 (AR 151) or Direct Blue 1 (DBl). Clean white cotton (bleached, without adding optical brightener). Liquid detergent and powder detergent as typically found in the North American market; both detergents did not contain bleach system. Laccasa from Coprinus cinereus, obtained as described in Example 4.
Washing procedure:
The washing process was carried out in a beaker with magnetic stirring 35rC for 15 min., After which the test fabrics were rinsed thoroughly in running water and air-dried overnight before the water was taken. Hunter reading by using a Datacolor Elrephometer 2000 reflectance spectrometer.
Laccase system: Laccasa at a level of 10 mg / l with acetosyringone intensifying agent at the 10 μM level. The following results were obtained:
Washing in solution of liquid detergent (2 g / 1, water hardness 6 ° dH) at pH 8.5: Hunter color difference (delta E) with respect to white cotton, washing
Cotton washed with washing cotton bleaching agents with AR 151 decolorizing agents of DB 1
Washing without laccase system 12 26 Washing with laccase system 1 7
Washing in powder detergent solution (1 g / 1, water hardness 6 ° dH) at pH 10.0: Hunter color difference (delta E) with respect to white cotton, washing
Cotton washed with washing cotton bleaching agents with AR 151 decolorizing agents of DB 1
Washing without laccase system 21 29 Washing with s; Laccase stema 4 8 The typical significant differences in delta E readings are 2-3 units, so that the data reflects a significant reaction of dye transfer cor. Laccase treatments in relation to treatment without laccase system.
EXAMPLE 10
Inhibition of Tint Transfer Using Laccasa from Myceliophthora thermophila
A small-scale experiment was carried out in which cleaned cotton test pieces were washed together with stained fabrics that faded in the wash solution, the experiment was conducted in the absence and presence of laccase and the enhancing agent. After washing, the Hunter color differences between the cotton pieces mentioned above and the clean cotton pieces (washed in the absence of fading fabrics) were measured and measured as the degree of dye transfer resulting from washing.
Used materials :
Discolored fabrics dyed with Acid Red 151 (AR 151) or Direct Blue (DBl).
Clean white cotton (bleached, without optical brightener). Liquid detergent (No.l) as typically found in the European market; liquid detergent (No. 2) as typically found in the North American market. Laccasa from Myceliophthora thermophila produced as described in PCT / US95 / 06815).
Washing procedure:
The washing process was carried out in beakers with magnetic stirring at 35 ° C for 15 minutes, after which the test cloths were rinsed thoroughly in running water and dried overnight in the air in the dark before that the Hunter readings were taken using a Datacolor Elrephometer 2000 reflectance spectrometer.
Laccase system: M. thermophila laccasa at a level of
0. 87 mg / L with the intensifying agent acetosyringone (AS) or the enhancer methylsiringate (MS) at a level of 10 μM. The following results were obtained:
Washing in liquid detergent solution No. 1 (7 g / 1, hardness of water 12 ° dH) at an initial pH of 7. 0:
Hunter's color difference (delta E) with respect to white cotton, washed
Cotton washed with washing cotton bleaching agents with AR 151 decolorizing agents of DB 1
Washing without laccasa system 7 27
Washing with laccase system based on AS 5 13
Washing with laccase system based on MS 4 12
Washing in liquid detergent solution No. 2 (2 g / 1, water hardness 6 ° dH) at pH 8 .5:
Hunter's color difference (delta E) with respect to white cotton, washed
Cotton washed with washing cotton bleaching agents with AR 151 decolorizing agents of DB 1
Washing without laccase system 14 29
Washing with laccase system based on AS 5 10
Washing with laccase system based on MS 3 8 The typical significant differences in the reading of delta are 2-3 units, so that the data reflect a significant revision of the transfer of dye with laccase treatments in relation to treatment without system of laccasa. 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 is clear from the present description of the invention. Having described the invention as above, property is claimed as contained in the following:
Claims (28)
1. A method for oxidizing a compound with a phenol oxidant enzyme, characterized by the presence of an enhancing agent of the following formula: formula in which A is a group such as -D, -CH = CH-D, -CH = CH-CH = CH-D, -CH = ND, -N = ND, or -N = CH-D, in which D is selected from the group consisting of -CO-E, -SO? -E, -N-XY, and -N * -XYZ, in which E can be -H, -OH, -R, u- OR, and X and Y and Z may be identical or different and be selected from -H and -R; R is a Ci-Cie alkyl, preferably a C?-C8 alkyl, alkyl which may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C can be the same or different and be selected from C i; 1 < m < 5.
2. A method according to claim 1, characterized in that the enhancing agent is selected from the group consisting of acetosyringone, syringaldehyde, ethylsicylate, and syringic acid.
3. A method according to claims 1-2, characterized in that the phenol oxidant enzyme is a peroxidase and a source of hydrogen peroxide.
4. The method according to claim 3, characterized in that the peroxidase is horseradish peroxidase, soy peroxidase and a peroxidase enzyme derived from Cprinus, for example C. cinereus or C. macrorhizus, or n Bacillus, for example B. pumilus, or Myxococcus, for example, M. virescens.
5. The method according to claim 3 or 4, characterized in that the peroxidase source of
T > hydrogen is hydrogen peroxide or a precursor of hydrogen peroxide, for example perborate or percarbonate, or a hydrogen peroxide generating enzyme system, for example an oxidase and its substrate, or a peroxycarboxylic acid or a salt thereof. 6. The method according to claim 1, characterized in that the phenol oxidant enzyme is a laccase or a laccase-related enzyme together with oxygen.
7. The method according to claim 6, characterized in that the laccase is derived from Trametes, for example, Trametes villosa, or Coprinus, for example, Coprinus cinereus, or biirubin oxidase derived from Myrothecium, for example, M. verrucaria.
8. The method according to any of claims 1-7, characterized in that the method is a method for whitening dyes in solution.
9. The method according to any of claims 1-8, characterized in that the method is a method for inhibiting the transfer of a textile dye from a dyed fabric to another fabric where the fabrics are washed together in a wash liquor.
10. The method according to claim 8-9, characterized in that the enhancing agent is added at the beginning of, or during the process.
11. The method according to any of claims 8-10, characterized in that the concentration of enhancing agent is in the range of 0. 01-1000 μM, more preferably 0.1-250 μM, more preferably 1-100 μM.
12. A detergent additive, characterized in that it comprises a phenol oxidant enzyme and an enhancer of the formula formula in which A is a group such as -D, -CH = CH-D, -CH = CH-CH = CH-D, -CH = ND, -N = ND, or -N = CH-D, in which D is selected from the group consisting of -CO-E, -S02-E, -N-XY, and -N * -XYZ, in which E can be -H, -OH, -R, or -OR, and X and Y and Z can be identical or different and be selected from -H and -R; R is a C 1 -C 6 alkyl, preferably a C 1 -C a alkyl, which alkyl can be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C can be the same or different and selected from CmH2m * ?; 1 < m < 5.
13. The detergent additive according to claim 12, characterized in that the intensifying agent is selected from the group consisting of acetosyringone, syringaldehyde, methylsicylate and syringic acid.
14. The detergent additive according to claims 12-13, characterized in that the phenol oxidant enzyme is a peroxidase and a source of hydrogen peroxide.
15. The detergent additive according to claim 14, characterized in that the peroxidase is horseradish peroxidase, soy peroxidase or a peroxidase enzyme derived from Coprinus, for example C. cinereus or C. macrorhizus, or from Bacillus, for example B. pumilus , or Myxococcus, for example, M. virescens.
16. The detergent additive according to claims 14-15, characterized in that the source of hydrogen peroxide is hydrogen peroxide or a precursor of hydrogen peroxide, for example perborate or percarbonate, or an enzyme system generating hydrogen peroxide, by example an oxidase and a suitable substrate, or a peroxycarboxylic acid or a salt thereof.
17. The detergent additive according to claim 12, characterized in that the phenol oxidant enzyme is a laccase or an enzyme related to laccase together with oxygen.
18. The detergent additive according to claim 17, characterized in that the laccase is derived from Trametes, for example, Trametes villosa, or Coprinus, for example, Coprinus cinereus, or bilirubin oxidase derived from Myrothecium, for example, M. verrucaria.
19. The detergent additive according to any of claims 12-18, provided in the form of a granulate, preferably a non-powdery granulate, a liquid, in particular a stabilized liquid, a suspension or a protected enzyme.
20. A detergent composition, characterized in that it comprises an oxidant enzyme of the phenol, a surfactant and an enhancer of the formula formula in which A is a group such as -D, -CH = CH-D, -CH-CH-CH-CH-D, -CH-ND, -N = ND, or -N = CH-D, in wherein D is selected from the group consisting of -CO-E, -S02-E, -N-XY, and -N + -XYZ, in which E can be -H, -OH, -R, or -OR, and X and Y and Z may be identical or different and be selected from -H and -R; R is an alkyl of C? -C? 6, preferably an alkyl of C.-C ,, alkyl which can be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C can be the same or different and • selected from CmH2ra + 1; 1 < m < 5.
21. The detergent composition according to claim 20, characterized in that the enhancing agent is selected from the group consisting of acetosyringone, syringaldehyde, methyl syringate and syringic acid.
22. The detergent composition according to claim 21, characterized in that the enzyme j or oxidant of the phenol is a peroxidase and a source of hydrogen peroxide.
23. The detergent composition according to claim 22, characterized in that the peroxidase 20 is horseradish peroxidase, soy peroxidase or a peroxidase enzyme derived from Coprinus, for example C. cinereus or C. macrorhizus, or from Bacillus, for example B. pumilus, or Myxococcus, for example, M. virescens.
24. The detergent composition according to claims 22-23, characterized in that the source of hydrogen peroxide is hydrogen peroxide or a precursor of hydrogen peroxide, for example perborate or percarbonate, or an enzyme system generating hydrogen peroxide, by example an oxidase and its substrate, or a peroxycarboxylic acid or a salt thereof.
25. The detergent composition according to claim 20, characterized in that the phenol oxidant enzyme is a laccase or a laccase related enzyme together with oxygen.
26. The detergent composition according to claim 25, characterized in that the laccase is derived from Trametes, for example, Trametes villosa, or Coprinus, for example, Coprinus cinereus, or bilirubin oxidase derived from Myrothecium, for example, M. verrucaria.
27. The detergent composition according to any of claims 20-26, characterized in that it comprises one or more other enzymes, in particular a protease, a lipase, an amylase, a cellulase and / or a cutinase.
28. The method according to any of claims 1-7, characterized in that the method is a method for bleaching material containing lignin, in particular bleaching pulp for the production of paper.
Applications Claiming Priority (7)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DK110994 | 1994-09-27 | ||
DK1109/94 | 1994-09-27 | ||
DK0952/95 | 1995-08-25 | ||
DK95295 | 1995-08-25 | ||
DK104495 | 1995-09-19 | ||
DK1044/95 | 1995-09-19 | ||
PCT/DK1995/000384 WO1996010079A1 (en) | 1994-09-27 | 1995-09-27 | Enhancers such as acetosyringone |
Publications (2)
Publication Number | Publication Date |
---|---|
MXPA97002041A true MXPA97002041A (en) | 1997-06-01 |
MX9702041A MX9702041A (en) | 1997-06-28 |
Family
ID=27221018
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
MX9702041A MX9702041A (en) | 1994-09-27 | 1995-09-27 | Enhancers such as acetosyringone. |
Country Status (12)
Country | Link |
---|---|
US (1) | US5912405A (en) |
EP (1) | EP0781328B1 (en) |
JP (1) | JP3691516B2 (en) |
KR (1) | KR970706388A (en) |
CN (1) | CN1104498C (en) |
AT (1) | ATE229070T1 (en) |
AU (1) | AU3517695A (en) |
BR (1) | BR9509046A (en) |
DE (1) | DE69529080T2 (en) |
FI (1) | FI971262A0 (en) |
MX (1) | MX9702041A (en) |
WO (1) | WO1996010079A1 (en) |
Families Citing this family (59)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
BR9509046A (en) * | 1994-09-27 | 1998-07-14 | Novo Nordisk As | Process for oxidizing a compound with a phenol oxidizing enzyme and additive and detergent composition |
AU2635097A (en) * | 1996-04-29 | 1997-11-19 | Novo Nordisk A/S | Non-aqueous, liquid, enzyme-containing compositions |
DE69714594T2 (en) * | 1996-05-09 | 2003-04-24 | Novozymes As | ANTIMICROBIAL PEROXIDASE COMPOSITIONS |
MA24177A1 (en) * | 1996-05-13 | 1997-12-31 | Procter & Gamble | DETERGENT COMPOSITION COMPRISING A LACCASE ENZYME AND A DYE TRANSFER INHIBITOR POLYMER |
MA24176A1 (en) * | 1996-05-13 | 1997-12-31 | Procter & Gamble | DETERGENT COMPRISING AN ENZYME PROTEASE AND A LACCASE ENZYME |
DE69706434T2 (en) * | 1996-11-25 | 2002-04-11 | Unilever Nv | ENZYMATIC OXIDATION PROCEDURE |
US6100080A (en) * | 1996-12-18 | 2000-08-08 | Novo Nordisk A/S | Method for enzymatic treatment of biofilm |
TR199902957T2 (en) * | 1997-06-10 | 2004-12-21 | Unilever N.V. | A method of increasing the activity of an enzyme, bleach composition, detergent composition and method of preventing dye transfer. |
TR199903037T2 (en) * | 1997-06-13 | 2000-06-21 | Unilever N.V. | Bleaching enzymes. |
US6492316B1 (en) | 1997-07-09 | 2002-12-10 | The Procter & Gamble Company | Cleaning compositions comprising a cytochrome |
AU3668297A (en) * | 1997-07-09 | 1999-02-08 | Procter & Gamble Company, The | Cleaning compositions comprising an oxidoreductase |
ATE230012T1 (en) * | 1997-07-09 | 2003-01-15 | Procter & Gamble | CLEANING COMPOSITIONS CONTAINING CYTOCHROMES |
EP1002039A1 (en) * | 1997-07-09 | 2000-05-24 | The Procter & Gamble Company | Detergent compositions comprising a specific oxygenase |
US6251845B1 (en) | 1997-07-09 | 2001-06-26 | The Procter & Gamble Company | Detergent compositions comprising an oxygenase enzyme and cofactor to remove body soils |
US6204234B1 (en) * | 1997-07-09 | 2001-03-20 | The Proctor & Gamble Company | Cleaning compositions comprising a specific oxygenase |
US6074631A (en) * | 1997-08-14 | 2000-06-13 | Novo Nordisk A/S | Reduction of malodour |
US6080391A (en) * | 1997-08-14 | 2000-06-27 | Novo Nordisk A/S | Reduction of malodour |
BR9814855A (en) * | 1997-11-10 | 2000-10-03 | Novo Nordisk As | Process for antimicrobial treatment of microorganisms and / or viruses, and, antimicrobial composition. |
US6228128B1 (en) * | 1997-11-10 | 2001-05-08 | Charlotte Johansen | Antimicrobial activity of laccases |
JP2003527450A (en) | 1998-05-01 | 2003-09-16 | ノボ ノルディスク アクティーゼルスカブ | Enhancers such as N-hydroxyacetanilide |
AU6046199A (en) * | 1998-09-17 | 2000-04-03 | Novozymes North America, Inc. | Methods for deinking and decolorizing printed paper |
EP1137391B1 (en) * | 1998-12-01 | 2004-11-03 | Novozymes A/S | Method for treating hair |
US6572843B1 (en) | 1998-12-01 | 2003-06-03 | Novozymes, A/S | Method for treating hair |
US6322596B1 (en) | 1999-01-26 | 2001-11-27 | Kimberly-Clark Worldwide, Inc. | Method of decolorizing a dyed material in a predetermined pattern |
US6610172B1 (en) | 1999-05-06 | 2003-08-26 | Novozymes A/S | Process for treating pulp with laccase and a mediator to increase paper wet strength |
WO2000068500A1 (en) * | 1999-05-06 | 2000-11-16 | Novozymes A/S | A process for production of paper materials with improved wet strength |
US7063970B1 (en) * | 1999-05-06 | 2006-06-20 | Norozymes A/S | Enzymatic preservation of water based paints |
WO2001000769A1 (en) * | 1999-06-23 | 2001-01-04 | Unilever N.V. | Method and composition for enhancing the activity of an enzyme |
WO2001000768A1 (en) * | 1999-06-23 | 2001-01-04 | Unilever N.V. | Bleaching detergent compositions |
AU6557900A (en) * | 1999-08-10 | 2001-03-05 | Novozymes A/S | Reduction of malodour in soiled animal litter |
AU5822301A (en) * | 2000-05-08 | 2001-11-20 | Novozymes A/S | Oxidoreductase mediated antimicrobial activity |
US20030096394A1 (en) * | 2001-09-10 | 2003-05-22 | Cheng Huai N. | Laccase activity enhancers |
DE10257389A1 (en) | 2002-12-06 | 2004-06-24 | Henkel Kgaa | Liquid acidic detergent for low temperature antibacterial washing of textiles contains a nonionic surfactant, an esterquat and phthaloylaminoperoxycaproic acid |
WO2004067582A1 (en) * | 2003-01-28 | 2004-08-12 | Akzo Nobel Coatings International B.V. | Curable composition comprising a compound having radically polymerizable olefinically unsaturated groups, an oxidation-reduction enzyme, and a thiol-functional compound |
CA2535526C (en) | 2003-08-11 | 2015-09-29 | Diversa Corporation | Laccases, nucleic acids encoding them and methods for making and using them |
DE102004020015A1 (en) * | 2004-04-21 | 2005-11-10 | Henkel Kgaa | Textile Care |
WO2007054034A1 (en) * | 2005-11-11 | 2007-05-18 | Novozymes A/S | Uses of laccase |
DE102006012018B3 (en) | 2006-03-14 | 2007-11-15 | Henkel Kgaa | Color protecting detergent |
DE602007008702D1 (en) * | 2006-03-31 | 2010-10-07 | British Telecomm | METHOD AND DEVICE FOR OBTAINING ARTICLE INFORMATION USING RFID LABELS |
JP5186497B2 (en) * | 2006-07-27 | 2013-04-17 | チバ ホールディング インコーポレーテッド | Biocatalytic hydrophilization of polyolefins |
CA2795834A1 (en) | 2010-05-05 | 2011-11-10 | Basf Se | Fibrous composition for paper and card production |
WO2012001145A1 (en) | 2010-07-01 | 2012-01-05 | Novozymes A/S | Bleaching of pulp |
CN103209934B (en) * | 2010-09-21 | 2016-01-20 | 诺维信公司 | Selenium cyanate/salt or monohydrate selenium dioxide ester/salt is removed from the aqueous solution |
CA2834513A1 (en) | 2011-04-28 | 2012-11-01 | Novozymes, Inc. | Polypeptides having endoglucanase activity and polynucleotides encoding same |
PL2753749T3 (en) | 2011-09-09 | 2019-10-31 | Novozymes As | Improving properties of paper materials |
CN102650108B (en) * | 2012-04-19 | 2014-06-04 | 华中科技大学 | Method for producing fiberboards by lignocelluloses as raw materials |
EP2740840A1 (en) | 2012-12-07 | 2014-06-11 | Novozymes A/S | Improving drainage of paper pulp |
WO2014090940A1 (en) | 2012-12-14 | 2014-06-19 | Novozymes A/S | Removal of skin-derived body soils |
DE102014210791A1 (en) * | 2014-06-05 | 2015-12-17 | Henkel Ag & Co. Kgaa | Detergent containing at least one laccase as color transfer inhibitor |
EP3210630A1 (en) | 2016-02-29 | 2017-08-30 | G.L. Pharma GmbH | Abuse-deterrent pharmaceutical compositions |
EP3210596A1 (en) | 2016-02-29 | 2017-08-30 | G.L. Pharma GmbH | Abuse-deterrent pharmaceutical composition |
EP3231420A1 (en) | 2016-02-29 | 2017-10-18 | G.L. Pharma GmbH | Abuse-deterrent pharmaceutical compositions |
CN110892065A (en) | 2017-08-18 | 2020-03-17 | 宝洁公司 | Cleaning method |
WO2019035038A1 (en) | 2017-08-18 | 2019-02-21 | The Procter & Gamble Company | Cleaning agent |
WO2019035037A1 (en) | 2017-08-18 | 2019-02-21 | The Procter & Gamble Company | Cleaning kit |
US20210207321A1 (en) | 2018-05-31 | 2021-07-08 | Novozymes A/S | Method for treating dissolving pulp |
WO2021018751A1 (en) | 2019-07-26 | 2021-02-04 | Novozymes A/S | Enzymatic treatment of paper pulp |
CN110637970B (en) * | 2019-09-30 | 2021-07-20 | 中国农业科学院北京畜牧兽医研究所 | Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase |
EP4053328A1 (en) | 2021-03-02 | 2022-09-07 | CHT Germany GmbH | Combined bleaching treatment for textiles |
Family Cites Families (15)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
PE14291A1 (en) * | 1989-10-13 | 1991-04-27 | Novo Nordisk As | PROCEDURE TO INHIBIT THE TRANSFER OF DYES |
WO1992018683A1 (en) * | 1991-04-12 | 1992-10-29 | Novo Nordisk A/S | Process for bleaching of dyed textiles |
DK0580707T3 (en) * | 1991-04-12 | 1998-01-19 | Novo Nordisk As | Removal of excess dye from newly manufactured textiles |
EP0679183B1 (en) * | 1992-12-01 | 2003-04-16 | Novozymes A/S | Enhancement of enzyme reactions |
DK144392D0 (en) * | 1992-12-01 | 1992-12-01 | Novo Nordisk As | ENZYMER ACTIVATION |
WO1996006930A1 (en) * | 1994-08-26 | 1996-03-07 | Novo Nordisk A/S | Coprinaceae laccases |
BR9509046A (en) * | 1994-09-27 | 1998-07-14 | Novo Nordisk As | Process for oxidizing a compound with a phenol oxidizing enzyme and additive and detergent composition |
MX9701059A (en) * | 1994-10-20 | 1997-05-31 | Novo Nordisk As | Bleaching process comprising use of a phenol oxidizing enzyme, a hydrogen peroxide source and an enhancing agent. |
AU6870096A (en) * | 1995-09-19 | 1997-04-09 | Novo Nordisk A/S | Stain bleaching |
ES2187748T3 (en) * | 1996-01-12 | 2003-06-16 | Novozymes As | TISSUE TREATED WITH CELLULASE AND OXIDORREDUCTASE. |
WO1997040229A1 (en) * | 1996-04-19 | 1997-10-30 | Novo Nordisk A/S | Fabric treated with a cellulase and a hybrid enzyme comprising a phenol oxidizing enzyme |
WO1997040127A1 (en) * | 1996-04-19 | 1997-10-30 | Novo Nordisk A/S | Bleaching of fabric with a hybrid enzyme containing a phenol oxidizing enzyme fused to a cellulose binding domain |
AU2635097A (en) * | 1996-04-29 | 1997-11-19 | Novo Nordisk A/S | Non-aqueous, liquid, enzyme-containing compositions |
DE69714594T2 (en) * | 1996-05-09 | 2003-04-24 | Novozymes As | ANTIMICROBIAL PEROXIDASE COMPOSITIONS |
US5752900A (en) * | 1997-03-13 | 1998-05-19 | Holland, Jr.; Robert R. | Exercise belt apparatus |
-
1995
- 1995-09-27 BR BR9509046A patent/BR9509046A/en not_active IP Right Cessation
- 1995-09-27 US US08/793,022 patent/US5912405A/en not_active Expired - Fee Related
- 1995-09-27 MX MX9702041A patent/MX9702041A/en not_active IP Right Cessation
- 1995-09-27 CN CN95195321A patent/CN1104498C/en not_active Expired - Fee Related
- 1995-09-27 WO PCT/DK1995/000384 patent/WO1996010079A1/en active IP Right Grant
- 1995-09-27 AT AT95931922T patent/ATE229070T1/en not_active IP Right Cessation
- 1995-09-27 AU AU35176/95A patent/AU3517695A/en not_active Abandoned
- 1995-09-27 JP JP51128996A patent/JP3691516B2/en not_active Expired - Lifetime
- 1995-09-27 DE DE69529080T patent/DE69529080T2/en not_active Expired - Lifetime
- 1995-09-27 KR KR1019970701771A patent/KR970706388A/en active IP Right Grant
- 1995-09-27 EP EP95931922A patent/EP0781328B1/en not_active Expired - Lifetime
-
1997
- 1997-03-26 FI FI971262A patent/FI971262A0/en unknown
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