EP2149786A1 - Améliorations relatives à l'analyse de détergent - Google Patents

Améliorations relatives à l'analyse de détergent Download PDF

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Publication number
EP2149786A1
EP2149786A1 EP08161667A EP08161667A EP2149786A1 EP 2149786 A1 EP2149786 A1 EP 2149786A1 EP 08161667 A EP08161667 A EP 08161667A EP 08161667 A EP08161667 A EP 08161667A EP 2149786 A1 EP2149786 A1 EP 2149786A1
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EP
European Patent Office
Prior art keywords
agrostis
swatch
debris
species
green plant
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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EP08161667A
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German (de)
English (en)
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designation of the inventor has not yet been filed The
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Unilever PLC
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Unilever PLC
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Publication date
Application filed by Unilever PLC filed Critical Unilever PLC
Priority to EP08161667A priority Critical patent/EP2149786A1/fr
Priority to EP09802487A priority patent/EP2307875A1/fr
Priority to PCT/EP2009/059307 priority patent/WO2010012624A1/fr
Priority to CN200980130613.4A priority patent/CN102112863B/zh
Publication of EP2149786A1 publication Critical patent/EP2149786A1/fr
Withdrawn legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase

Definitions

  • the present invention is concerned with improvements relating to detergent analysis and in particular to improvements relating to the preparation of so-called "swatches" for use in such analysis.
  • a "swatch" is a piece of generally flexible material such as a fabric that has a stain applied thereto.
  • the material can be, for example, a fabrics made of cotton, polyester or various mixtures of natural and synthetic fibres.
  • the swatch can be non-woven (e.g. filter paper or nitrocellulose) or even a piece of a hard material, for example, ceramic.
  • the stain may include blood, milk, ink, grass, tea, wine, spinach, gravy, chocolate, egg, cheese, clay, pigment, oil, or mixtures of these components.
  • Swatches are commonly used in the evaluation of laundry detergent compositions. In the traditional "model wash” analysis, as they are a small part of the wash-load, the bulk of the load being made up of "ballast", which comprises various sheets of cloth. One or more swatches (also known as “monitors”) and a quantity of "ballast”, are washed under known conditions so that the degree of stain removal can be determined.
  • United States Patent 7122334 discloses a more modern technique for analysis of detergent compositions.
  • a "smaller swatch" a piece of the swatch that has been cut or otherwise removed from the swatch of material either before or after fixing the stain to the swatch is placed into the well of a 24, 48 or 96 well micro-titer plate.
  • the "smaller swatch” can also be made by applying a stain to a small piece of material. Typically these "smaller swatches” are around 5mm in diameter.
  • “swatch” includes both larger and smaller swatches.
  • Swatches having stains of known "strength" on various types of material are commercially available (from EMPA, St. Gallen, Switzerland; WFK-Testgewebe GmbH, Krefeld Germany; or Center for Test Materials, Vlaardingen, The Netherlands) and/or can be made by the practitioner (as described for example in Morris and Prato, Textile Research Journal 52(4):280 286 (1982 )).
  • the present invention provides a swatch of fabric having an area of from 0.25 m 2 to 4x10 -6 m 2 , said swatch being stained in one or more patches over at least 0.1% of its surface with debris comprising chloroplast material wherein at least 80%wt of the chloroplast material present in a patch is from a single species of green plant other than tea or spinach.
  • the fabric is cellulosic, polyester or a mixture thereof.
  • the remaining 20%wt of the debris is from no more than five, preferably three, preferably one other species.
  • the stain is derived from a single species.
  • the debris is one or more species of the genera:
  • the debris is from a Dicotyledone.
  • the debris is from one or more of the species:
  • the debris is from one or more of the order Ranunculales or the family Asteraceae .
  • Agrostis are the bent grasses ( Agrostis stolonifera - " creeping bent " is commonly used on golf-course greens), and are widely used on lawns.
  • the Fescue genus are tufted grasses (used on bowling greens and for fodder)
  • Lolium are the ryegrasses
  • Poa includes European meadowgrass
  • Holcus are also grasses.
  • Trifolium includes the clovers
  • Bellis includes the daisy
  • Taraxacum includes the dandelion
  • Ranunculus includes the buttercup.
  • Eurhynchium is a moss genus as are the Brachytheciaceae .
  • stains which comprise one or more of plants selected from the genus Lolium, preferably Lolium perenne (a perennial ryegrass).
  • Festuca preferably Festuca pratensi (a meadow fescue).
  • Trifolium preferably Trifolium pratense (a red clover).
  • Other suitable stains may comprise Agrostis (bent grass), trifolium repens (white clover) and/or Taraxacum officinale (dandelion).
  • a swatch may comprise two or more stains which are different cultivars or varieties of the same species.
  • the swatch comprises a stain derived from trifolium repens (white clover) separate stains derived from the Aber Dai cultivar and the Aber Ace cultivar may be present.
  • At least one non-grass species is present and particularly preferred that this is selected from the non-vascular plants (Bryophytes), from non-angiosperm vascular plants or from the angiosperm families Asteraceae, Rubiaceae or Fabaceae .
  • Swatches can be prepared wherein the debris derived from true grasses (Poaceae) are less than 50%wt, preferably less than 25%wt of the material present. Swatches may be prepared in which none of the material present is derived from grasses.
  • More than one species-specific stain can be present on each swatch.
  • a smaller swatch may be uniformly stained or cut from a larger swatch.
  • a second aspect of the present invention subsists in a method for preparing a swatch which comprises the step of contacting a fabric substrate in sheet form having an area greater than 4x10 -6 m 2 (greater than 4mm 2 ) with chloroplast-containing green plant material wherein at least 80% of the debris is from a single species of green plant other than tea or spinach.
  • the preferred genera and species are as noted above and the process may be repeated to give a swatch bearing a plurality of stains.
  • a third aspect of the present invention provides a method for determining the effectiveness of laundry compositions which includes that step of treating swatches according to the present invention with the laundry composition.
  • the laundry composition comprises at least one enzyme.
  • chloroplasts contain DNA, it is relatively easy to determine the number and type of genera and species represented on a particular swatch.
  • the laundry composition being tested comprises at least one enzyme.
  • enzymes include proteases, alpha-amylases, cellulases, lipases, peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof.
  • Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included.
  • the protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279 ).
  • Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270 and WO 94/25583 .
  • Examples of useful proteases are the variants described in WO 92/19729 , WO 98/20115 , WO 98/20116 , and WO 98/34946 , especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274.
  • Preferred commercially available protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A/S), MaxataseTM, MaxacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces ), e.g. from H. lanuginosa ( T. lanuginosus ) as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580 , a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes ( EP 218 272 ), P. cepacia ( EP 331 376 ), P. stutzeri ( GB 1,372,034 ), P.
  • lipase variants such as those described in WO 92/05249 , WO 94/01541 , EP 407 225 , EP 260 105 , WO 95/35381 , WO 96/00292 , WO 95/30744 , WO 94/25578 , WO 95/14783 , WO 95/22615 , WO 97/04079 and WO 97/07202 .
  • LipolaseTM and Lipolase UltraTM, LipexTM are preferred commercially available lipase enzymes.
  • the method of the invention may be carried out in the presence of cutinase. classified in EC 3.1.1.74.
  • the cutinase used according to the invention may be of any origin.
  • Preferably cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
  • Cutinases are enzymes which are able to degrade cutin.
  • the cutinase is derived from a strain of Aspergillus, in particular Aspergillus oryzae, a strain of Alternaria , in particular Alternaria brassiciola , a strain of Fusarium, in particular Fusarium solani, Fusarium solani pisi, Fusarium roseum culmorum , or Fusarium roseum sambucium , a strain of Helminthosporum , in particular Helminthosporum sativum , a strain of Humicola , in particular Humicola insolens, a strain of Pseudomonas , in particular Pseudomonas mendocina, or Pseudomonas putida , a strain of Rhizoctonia , in particular Rhizoctonia solani , a strain of Streptomyces , in particular Streptomyces
  • the cutinase is derived from a strain of Humicola insolens , in particular the strain Humicola insolens DSM 1800.
  • Humicola insolens cutinase is described in WO 96/13580 which is herby incorporated by reference.
  • the cutinase may be a variant, such as one of the variants disclosed in WO 00/34450 and WO 01/92502 , which are hereby incorporated by reference.
  • Preferred cutinase variants include variants listed in Example 2 of WO 01/92502 , which is hereby specifically incorporated by reference.
  • Preferred commercial cutinases include NOVOZYMTM 51032 (available from Novozymes A/S, Denmark).
  • phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32.
  • phospholipase is an enzyme which has activity towards phospholipids.
  • Phospholipids such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol.
  • Phospholipases are enzymes which participate in the hydrolysis of phospholipids.
  • phospholipases A 1 and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
  • lysophospholipase or phospholipase B
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (A 1 or A 2 ), phospholipase B activity, phospholipase C activity or phospholipase D activity.
  • phospholipase A used herein in with an enzyme of the invention is intended to cover an enzyme with Phospholipase A 1 and/or Phospholipase A 2 activity.
  • the phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase activity.
  • the phospholipase activity may, e.g., be from a lipase with phospholipase side activity.
  • the phospholipase enzyme activity is provided by an enzyme having essentially only phospholipase activity and wherein the phospholipase enzyme activity is not a side activity.
  • the phospholipase may be of any origin, e.g., of animal origin (such as, e.g., mammalian), e.g. from pancreas (e.g., bovine or porcine pancreas), or snake venom or bee venom.
  • animal origin such as, e.g., mammalian
  • pancreas e.g., bovine or porcine pancreas
  • snake venom or bee venom e.g., from snake venom or bee venom.
  • the phospholipase may be of microbial origin, e.g., from filamentous fungi, yeast or bacteria, such as the genus or species Aspergillus, e.g., A. niger; Dictyostelium, e.g., D. discoideum; 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; Whetzelinia, e.g., W. sclerotiorum; Bacillus, e.g., 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, e.g., K. pneumoniae; Proteus, e.g., P. vulgaris; Providencia, e.g., P. stuartii; Salmonella, e.g. S. typhimurium; Serratia, e.g., S. liquefasciens, S. marcescens; Shigella, e.g., S. flexneri; Streptomyces, e.g., S.
  • the phospholipase may be fungal, e.g., from the class Pyrenomycetes , such as the genus Fusarium, such as a strain of F. culmorum, F. heterosporum, F. solani , or a strain of F. oxysporum .
  • the phospholipase may also be from a filamentous fungus 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 strain of Humicola , especially Humicola lanuginosa .
  • the phospholipase may be a variant, such as one of the variants disclosed in WO 00/32758 , which are hereby incorporated by reference.
  • Preferred phospholipase variants include variants listed in Example 5 of WO 00/32758 , which is hereby specifically incorporated by reference.
  • the phospholipase is one described in WO 04/111216 , especially the variants listed in the table in Example 1.
  • the phospholipase is derived from a strain of Fusarium, especially Fusarium oxysporum .
  • the phospholipase may be the one concerned in WO 98/026057 derived from Fusarium oxysporum DSM 2672, or variants thereof.
  • the phospholipase is a phospholipase A 1 (EC. 3.1.1.32). In another preferred embodiment of the invention the phospholipase is a phospholipase A 2 (EC.3.1.1.4.).
  • Examples of commercial phospholipases include LECITASETM and LECITASETM ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark).
  • Suitable amylases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g. a special strain of B. licheniformis, described in more detail in GB 1,296,839 , or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060 .
  • amylases are the variants described in WO 94/02597 , WO 94/18314 , WO 96/23873 , WO 97/43424 , WO 01/066712 , WO 02/010355 , WO 02/031124 and PCT/DK2005/000469 (which references all incorporated by reference.
  • amylases are DuramylTM, TermamylTM, Termamyl UltraTM, NatalaseTM, StainzymeTM, FungamylTM and BANTM (Novozymes A/S), RapidaseTM and PurastarTM (from Genencor International Inc.).
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium , e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila , and Fusarium oxysporum disclosed in US 4,435,307 , US 5,648,263 , US 5,691,178 , US 5,776,757 , WO 89/09259 , WO 96/029397 , and WO 98/012307 .
  • cellulases are the alkaline or neutral cellulases having color care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257 , EP 0 531 372 , WO 96/11262 , WO 96/29397 , WO 98/08940 .
  • Other examples are cellulase variants such as those described in WO 94/07998 , EP 0 531 315 , US 5,457,046 , US 5,686,593 , US 5,763,254 , WO 95/24471 , WO 98/12307 and PCT/DK98/00299 .
  • cellulases include CelluzymeTM, CarezymeTM, EndolaseTM, RenozymeTM (Novozymes A/S), ClazinaseTM and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
  • Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus , e.g. from C. Cinereus , and variants thereof as those described in WO 93/24618 , WO 95/10602 , and WO 98/15257 . Commercially available peroxidases include GuardzymeTM and NovozymTM 51004 (Novozymes A/S).
  • pectate lyases examples 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) FEBS Letts. 335:319-326 ) and Bacillus sp. YA-14 ( Kim et al. (1994) Biosci. Biotech. Biochem. 58:947-949 ). Purification of pectate lyases with maximum activity in the pH range of 8-10 produced by Bacillus pumilus ( Dave and Vaughn (1971) J. Bacteriol. 108:166-174 ), B.
  • the pectate lyase comprises the amino acid sequence of a pectate lyase disclosed in Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331-334 and Henrissat et al., (1995) Plant Physiol. 107: 963-976 .
  • pectatel lyases are disclosed in WO 99/27083 and WO 99/27084 .
  • Other specifically contemplates pectate lyases derived from Bacillus licheniformis is disclosed as in US patent no. 6,284,524 (which document is hereby incorporated by reference).
  • pectate lyase variants are disclosed in WO 02/006442 , especially the variants disclosed in the Examples in WO 02/006442 (which document is hereby incorporated by reference).
  • alkaline pectate lyases examples include BIOPREPTM and SCOURZYMETM L from Novozymes A/S, Denmark.
  • mannanases examples include mannanases of bacterial and fungal origin.
  • the mannanase is derived from a strain of the filamentous fungus genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus ( WO 94/25576 ).
  • WO 93/24622 discloses a mannanase isolated from Trichoderma reseei. Mannanases have also been isolated from several bacteria, including Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, No. 11, pp.
  • JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp.
  • JP-A-63056289 describes the production of an alkaline, thermostable beta-mannanase.
  • JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase.
  • JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001.
  • a purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/11164 .
  • WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active.
  • mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp., and Humicola insolens disclosed in WO 99/64619 .
  • Bacillus sp. mannanases concerned in the Examples in WO 99/64619 which document is hereby incorporated by reference.
  • mannanases examples include MannawayTM available from Novozymes A/S Denmark.
  • Any enzyme present in the composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708 .
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid
  • Stains were aged in the dark and at room temperature for 3 days prior to washing.
  • the detergent used was PersilTM Bio and non-Bio powder.
  • the 1*a*b and ⁇ E values of grass stains were obtained before and after wash using a Hunterlab TM calibrated against clean cotton and polyester fabrics.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Detergent Compositions (AREA)
EP08161667A 2008-08-01 2008-08-01 Améliorations relatives à l'analyse de détergent Withdrawn EP2149786A1 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
EP08161667A EP2149786A1 (fr) 2008-08-01 2008-08-01 Améliorations relatives à l'analyse de détergent
EP09802487A EP2307875A1 (fr) 2008-08-01 2009-07-20 Perfectionnement se rapportant à l'analyse d un détergent
PCT/EP2009/059307 WO2010012624A1 (fr) 2008-08-01 2009-07-20 Perfectionnement se rapportant à l'analyse d’un détergent
CN200980130613.4A CN102112863B (zh) 2008-08-01 2009-07-20 与洗涤剂分析有关的改进

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
EP08161667A EP2149786A1 (fr) 2008-08-01 2008-08-01 Améliorations relatives à l'analyse de détergent

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EP2149786A1 true EP2149786A1 (fr) 2010-02-03

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EP09802487A Withdrawn EP2307875A1 (fr) 2008-08-01 2009-07-20 Perfectionnement se rapportant à l'analyse d un détergent

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NL2011816A (en) 2012-11-30 2014-06-04 Asml Netherlands Bv Method of determining dose and focus, inspection apparatus, patterning device, substrate and device manufacturing method.
NL2014938A (en) 2014-06-30 2016-03-31 Asml Netherlands Bv Method of determining dose, inspection apparatus, patterning device, substrate and device manufacturing method.

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