US20080229514A1 - Cleaning compositions comprising transglucosidase - Google Patents

Cleaning compositions comprising transglucosidase Download PDF

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Publication number
US20080229514A1
US20080229514A1 US11/728,060 US72806007A US2008229514A1 US 20080229514 A1 US20080229514 A1 US 20080229514A1 US 72806007 A US72806007 A US 72806007A US 2008229514 A1 US2008229514 A1 US 2008229514A1
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United States
Prior art keywords
enzyme
transglucosidase
composition
cleaning
natural gum
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Abandoned
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US11/728,060
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English (en)
Inventor
Ayrookaran J. Poulose
Hugh C. McDonald
Jayarama K. Shetty
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Danisco US Inc
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Individual
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Priority to US11/728,060 priority Critical patent/US20080229514A1/en
Assigned to DANISCO US INC., GENENCOR DIVISION reassignment DANISCO US INC., GENENCOR DIVISION ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: MCDONALD, HUGH C., POULOSE, AYROOKARAN J., SHETTY, JAYARAMA K.
Priority to CA002681657A priority patent/CA2681657A1/en
Priority to PCT/US2008/003788 priority patent/WO2008118382A2/en
Priority to RU2009138938/10A priority patent/RU2501855C2/ru
Priority to CN200880009337A priority patent/CN101641433A/zh
Priority to KR1020097019430A priority patent/KR101443412B1/ko
Priority to BRPI0809150-1A priority patent/BRPI0809150A2/pt
Priority to EP08727093A priority patent/EP2126024A2/en
Priority to JP2010500947A priority patent/JP5230031B2/ja
Priority to MX2009009835A priority patent/MX2009009835A/es
Publication of US20080229514A1 publication Critical patent/US20080229514A1/en
Abandoned legal-status Critical Current

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    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • 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
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/222—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin
    • 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
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C12N9/1048—Glycosyltransferases (2.4)
    • C12N9/1051—Hexosyltransferases (2.4.1)
    • C12N9/107—1,4-Alpha-glucan branching enzyme (2.4.1.18)
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
    • D06L1/12—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using aqueous solvents
    • D06L1/14—De-sizing
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
    • D06L4/40—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using enzymes

Definitions

  • Detergent and other cleaning compositions often include a complex combination of active ingredients.
  • certain cleaning products contain a surfactant system, enzymes for cleaning, bleaching agents, builders, suds suppressors, soil-suspending agents, soil-release agents, optical brighteners, softening agents, dispersants, dye transfer inhibition compounds, abrasives, bactericides, and perfumes.
  • a surfactant system enzymes for cleaning, bleaching agents, builders, suds suppressors, soil-suspending agents, soil-release agents, optical brighteners, softening agents, dispersants, dye transfer inhibition compounds, abrasives, bactericides, and perfumes.
  • This disclosure relates to the use of transglucosidase as a cleaning agent.
  • compositions comprising: a) a transglucosidase enzyme; and b) a natural gum polysaccharide; wherein the natural gum polysaccharide is a substrate for the transglucosidase enzyme.
  • the natural gum polysaccharide may be, for example, a xanthan or guar gum.
  • the natural gum polysaccharide is present as a stain on an object, e.g., a fabric, or free in solution, for example.
  • the transglucosidase enzyme may be an amino acid sequence that is at least 70% identical to, e.g., at least 80% identical to, at least 85% identical to, at least 90% identical to, at least 95% identical to, or at least 98% identical to an Aspergillus transglucosidase.
  • the composition may further comprise a surfactant or other cleaning agent.
  • a cleaning method includes: a) contacting an object soiled with a natural gum polysaccharide with a cleaning composition comprising a transglucosidase enzyme; and b) maintaining the object and cleaning composition together under conditions sufficient to effect degradation of the natural gum polysaccharide and thereby clean the object.
  • the object (which may be a fabric, for example) may be soiled with a food that contains the natural gum polysaccharide, e.g., a food that contains a xanthan or guar gum.
  • the cleaning composition may contain a surfactant, other cleaning agents, or another enzyme, e.g., a protease, amylase, cellulase, lipase, cutinase, oxido-reductase, or the like, for the degradation of other stain components.
  • the cleaning composition used in the method may have a pH in the range of pH 5.0 to pH 11.5, and the transglucosidase enzyme may be present in the cleaning composition at a concentration in the range of 0.01 ppm to 100 ppm.
  • use of the subject method results in more efficient removal of stains that contain natural gum polysaccharides than equivalent methods that do not employ a transglucosidase enzyme.
  • an isolated enzyme containing an Aspergillus transglucosidase produced by a Trichoderma reesei host cell is provided.
  • Cleaning compositions, e.g., laundry detergents, containing the same are provided, as well as well as a method of using the same for cleaning an object, e.g., a fabric.
  • FIG. 1 shows a vector map of pTrex3(AGL51M).
  • FIG. 2 shows the nucleotide sequence of an expression cassette of pTrex3(AGL51M) (SEQ ID NO:1).
  • FIG. 3 is a graph showing the enzymatic activity of transglucosidase on 0.2% xanthan, as measured by a reducing sugar assay.
  • FIG. 4 presents graphs showing the cleaning performance of Trip-TG on guar soiled microswatches (top panel) and salad dressing soiled microswatches (bottom panel) in 50 mM Hepes buffer (pH 7.4) and in AATCC HDL Detergent (pH 7.4).
  • FIG. 5 is a graph of a dose response experiment showing that Trip-TG is active on salad dressing soiled microswatches at a concentration of 1 to 5 ppm in AATCC HDL.
  • FIG. 6 is a graph showing Trip-TG cleaning activity on salad dressing microswatches in heavy duty solid detergent (HDD).
  • FIG. 7 is a graph showing Trip-TG cleaning activity on marmalade stain in a Tergotometer assay using 0.15% AATCC HDL.
  • nucleic acids are written left to right in 5′ to 3′ orientation; amino acid sequences are written left to right in amino to carboxy orientation, respectively.
  • the headings provided herein are not limitations of the various aspects or embodiments of the invention that can be had by reference to the specification as a whole. Accordingly, the terms defined immediately below are more fully defined by reference to the Specification as a whole.
  • recombinant refers to a polynucleotide or polypeptide that does not naturally occur in a host cell.
  • a recombinant molecule may contain two or more naturally-occurring sequences that are linked together in a way that does not occur naturally.
  • a recombinant cell contains a recombinant polynucleotide or polypeptide.
  • heterologous refers to elements that are not normally associated with each other. For example, if a host cell produces a heterologous protein, that protein is not normally produced in that host cell. Likewise, a promoter that is operably linked to a heterologous coding sequence is a promoter that is operably linked to a coding sequence that it is not usually operably linked to in a wild-type host cell.
  • homologous with reference to a polynucleotide or protein, refers to a polynucleotide or protein that occurs naturally in a host cell.
  • protein and “polypeptide” are used interchangeably herein.
  • a “signal sequence” is a sequence of amino acids present at the N-terminal portion of a protein which facilitates the secretion of the mature form of the protein from the cell.
  • the definition of a signal sequence is a functional one.
  • the mature form of the extracellular protein lacks the signal sequence, which is cleaved off during the secretion process.
  • a “coding sequence” is a DNA segment that encodes a polypeptide.
  • nucleic acid encompasses DNA, RNA, single stranded or double stranded and chemical modifications thereof.
  • nucleic acid and polynucleotide are used interchangeably herein.
  • a “vector” refers to a polynucleotide designed to introduce nucleic acids into one or more host cells.
  • Vectors can autonomously replicate in different host cells and include: cloning vectors, expression vectors, shuttle vectors, plasmids, phage particles, cassettes and the like.
  • an “expression vector” as used herein means a DNA construct comprising a protein-coding region that is operably linked to a suitable control sequence that is capable of effecting expression of the protein in a suitable host cell.
  • control sequences may include a promoter to effect transcription, an optional operator sequence to control transcription to produce mRNA, a sequence encoding suitable ribosome binding sites on the mRNA, and enhancers and other sequences which control termination of transcription and translation.
  • a “promoter” is a regulatory sequence that initiates transcription of a downstream nucleic acid.
  • operably linked refers to an arrangement of elements that allows them to be functionally related.
  • a promoter is operably linked to a coding sequence if it controls the transcription of the sequence.
  • selectable marker refers to a protein capable of expression in a host that allows for ease of selection of those hosts containing an introduced nucleic acid or vector.
  • selectable markers include, but are not limited to, antimicrobials (e.g., hygromycin, bleomycin, or chloramphenicol) and/or genes that confer a metabolic advantage, such as a nutritional advantage on the host cell.
  • derived encompasses the terms “originated from”, “obtained” or “obtainable from”, and “isolated from”.
  • a “non-pathogenic” organism is an organism that is not pathogenic to humans.
  • recovered refers to a protein, cell, nucleic acid or amino acid that is removed from at least one component with which it is naturally associated.
  • the terms “transformed”, “stably transformed” and “transgenic” used in reference to a cell means the cell has a non-native (e.g., heterologous) nucleic acid sequence integrated into its genome or as an episomal plasmid that is maintained through multiple generations.
  • expression refers to the process by which a polypeptide is produced based on the nucleic acid sequence of a gene.
  • the process includes both transcription and translation.
  • the term “introduced” in the context of inserting a nucleic acid sequence into a cell means “transfection”, or “transformation” or “transduction” and includes reference to the incorporation of a nucleic acid sequence into a eukaryotic or prokaryotic cell wherein the nucleic acid sequence may be incorporated into the genome of the cell (e.g., chromosome, plasmid, plastid, or mitochondrial DNA), converted into an autonomous replicon, or transiently expressed (e.g., transfected mRNA).
  • the genome of the cell e.g., chromosome, plasmid, plastid, or mitochondrial DNA
  • transiently expressed e.g., transfected mRNA
  • hybridization refers to the process by which a strand of nucleic acid joins with a complementary strand through base pairing as known in the art.
  • a nucleic acid is considered to be “Selectively hybridizable” to a reference nucleic acid sequence if the two sequences specifically hybridize to one another under moderate to high stringency hybridization and wash conditions. Moderate and high stringency hybridization conditions are known (see, e.g., Ausubel, et al., Short Protocols in Molecular Biology, 3rd ed., Wiley & Sons 1995 and Sambrook et al., Molecular Cloning: A Laboratory Manual, Third Edition, 2001 Cold Spring Harbor, N.Y.).
  • high stringency conditions include hybridization at about 42 C in 50% formamide, 5 ⁇ SSC, 5 ⁇ Denhardt's solution, 0.5% SDS and 100 ug/ml denatured carrier DNA followed by washing two times in 2 ⁇ SSC and 0.5% SDS at room temperature and two additional times in 0.1 ⁇ SSC and 0.5% SDS at 42° C.
  • cleaning composition and “cleaning formulation” refer to a composition that finds use in the removal of undesired compounds (e.g., a stain) from items to be cleaned, such as fabric, dishes, contact lenses, other solid substrates, hair (shampoos), skin (soaps and creams), teeth (mouthwashes, toothpastes), etc.
  • the term encompasses any materials/compounds selected for the particular type of cleaning composition desired in the form of the product (e.g., liquid, gel, granule, or spray composition), as long as the composition is compatible with the subject enzyme in the composition.
  • the specific selection of cleaning composition materials are readily made by considering the surface, item or fabric to be cleaned, and the desired form of the composition for the cleaning conditions during use.
  • detergent compositions e.g., liquid and/or solid laundry detergents and fine fabric detergents; hard surface cleaning formulations, such as for glass, wood, ceramic and metal counter tops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile and laundry pre-spotters, as well as dish detergents).
  • cleaning composition includes, unless otherwise indicated, granular, tablet or powder-form all-purpose or heavy-duty washing agents, especially cleaning detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy-duty liquid (HDL) types; liquid fine-fabric detergents; hand dishwashing agents or light duty dishwashing agents, including those of the high-foaming type; machine dishwashing agents, including the various tablet, granular, liquid and rinse-aid types for household and institutional use; liquid cleaning and disinfecting agents, including antibacterial hand-wash types, cleaning bars, mouthwashes, denture cleaners, car or carpet shampoos, bathroom cleaners; hair shampoos and hair-rinses; shower gels and foam baths; metal cleaners; as well as cleaning auxiliaries such as bleach additives and “stain-stick”, pre-treat or laundry additive types.
  • HDL heavy-duty liquid
  • cleaning and disinfecting agents including antibacterial hand-wash types, cleaning bars, mouthwashes, denture cleaners, car or carpet shampoos, bathroom cleaners
  • detergent composition and “detergent formulation” are used in reference to compositions that are formulated for use in a wash medium for the cleaning of soiled objects.
  • the term is used in reference to laundering fabrics and/or garments (e.g., “laundry detergents”).
  • laundry detergents e.g., “laundry detergents”.
  • the term refers to other detergents, such as those used to clean dishes, cutlery, etc. (e.g., “dishwashing detergents”). It is not intended that the present invention be limited to any particular detergent formulation or composition.
  • a detergent composition may also contain surfactants, transferase(s), hydrolytic enzymes, oxido reductases, builders, bleaching agents, bleach activators, bluing agents and fluorescent dyes, caking inhibitors, masking agents, enzyme activators, antioxidants, and/or solubilizers, etc.
  • enhanced performance in a cleaning composition is defined as increasing cleaning (e.g., removal and/or decolorization) of stains (particularly those of, e.g., natural gum polysaccharide-related stains such as those of chocolate cream, salad dressing or guar, etc.), as determined by usual evaluation after a standard wash cycle.
  • hard surface cleaning composition refers to detergent compositions for cleaning hard surfaces such as floors, walls, tile, bath and kitchen fixtures, and the like. Such compositions are provided in any form, including but not limited to solids, liquids, emulsions, etc.
  • washwashing composition refers to all forms for compositions for cleaning dishes, including but not limited to granular and liquid forms.
  • fabric cleaning composition refers to all forms of detergent compositions for cleaning fabrics, including but not limited to, granular, liquid and bar forms.
  • textile refers to woven fabrics, as well as staple fibers and filaments suitable for conversion to or use as yarns, woven, knit, and non-woven fabrics.
  • the term encompasses yarns made from natural, as well as synthetic (e.g., manufactured) fibers.
  • textile materials is a general term for fibers, yarn intermediates, yarn, fabrics, and products made from fabrics (e.g., garments and other articles).
  • fabric encompasses any textile material. Thus, it is intended that the term encompass garments, as well as fabrics, yarns, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material.
  • “effective amount of transglucosidase” refers to the quantity of transglucosidase enzyme necessary to achieve the enzymatic activity required in the specific application (e.g., cleaning composition, etc.). Such effective amounts are readily ascertained by one of ordinary skill in the art and are based on many factors, such as the particular enzyme variant used, the cleaning application, the specific composition of the cleaning composition, and whether a liquid or dry (e.g., granular, bar) composition is required, and the like.
  • transglucosidase refers to an enzyme that transfers an ⁇ - D -glucosyl residue in a 1,4- ⁇ - D -glucan to the primary hydroxy group of glucose, free or combined in a 1,4- ⁇ - D -glucan.
  • the transglucosidase described herein has an activity described as EC 2.4.1.24, according to IUBMB enzyme nomenclature.
  • the systematic name for the transglucosidase described herein is 1,4- ⁇ - D -glucan: 1,4- ⁇ - D -glucan( D -glucose) 6- ⁇ - D -glucosyltransferase. This enzyme may be referred to as ⁇ -glucosidase in certain publications.
  • soiled object refers to an object, e.g., a fabric or dish, that is soiled, e.g., stained, with a second composition.
  • soiled object are dirty fabrics, such as dirty clothing, linens, and fabrics that are stained with foodstuffs containing a natural gum polysaccharide.
  • the stain may or may not have a visible color.
  • natural gum polysaccharide refers to a non-starch polysaccharide of natural origin that is capable of causing a large viscosity increase in solution at low concentration.
  • Such polysaccharides are commonly employed in the food industry and are used as thickening agents, gelling agents, emulsifiers and stabilizers in many foodstuffs, e.g., sauces, creams, dairy products, ice creams, mousses, milkshakes, salad dressings, etc.
  • Guar gum (food additive E412), an edible thickening agent extracted from the leguminous guar bean shrub, and xanthan gum (food additive E415), a polysaccharide that is produced by fermentation of glucose or sucrose, e.g., by the Xanthomonas campestris bacterium, are examples of natural gum polysaccharides.
  • Other natural gum polysaccharides include: agar (E406), alginic acid (E400), ⁇ -glucan, carrageenan (E407), chicle gum, dammar gum, gellan gum (E418), glucomannan (E425), gum arabic (E414), gum ghatti, gum tragacanth (E413), karaya gum (E416), locust bean gum (E410), mastic gum, sodium alginate (E401), spruce gum, and tara gum (E417).
  • non-starch food polysaccharide degrading enzyme refers to an enzyme that degrades non-starch food polysaccharides.
  • Exemplary enzymes include, but are not limited to, hemicellulase, mannanase, pectinase, xylanase, ⁇ -galactosidase and ⁇ -galactosidase.
  • working pH refers to the pH of a detergent during its use.
  • the working pH of a laundry detergent is the pH of the detergent when it is used to wash fabrics in a washing machine.
  • working pH of a dishwashing detergent is the pH of that detergent as it is being used in a dishwasher.
  • Detergents that are in concentrated or solid form may be diluted or dissolved before the pH of that detergent is at its working pH.
  • working concentration refers to the concentration of an enzyme in a detergent during its use.
  • the working concentration of an enzyme in a laundry detergent is the concentration of that enzyme when the laundry detergent is used to wash fabrics in a washing machine.
  • the working concentration of an enzyme in a dishwashing detergent is the concentration of that enzyme in the detergent as it is being used in a dishwasher.
  • Detergents that are in concentrated or solid form may be diluted or dissolved before the concentration of an enzyme in a detergent is at its working concentration.
  • compositions containing a transglucosidase enzyme are provided, as well as methods of using the same.
  • composition comprising a transglucosidase enzyme
  • the composition may comprise a) a transglucosidase enzyme, and b) a natural gum polysaccharide, where the natural gum polysaccharide is a substrate for the transglucosidase enzyme.
  • the transglucosidase enzyme generally has an activity defined as EC 2.4.1.24, according to IUBMB enzyme nomenclature, which activity transfers glucosyl residues in certain glucans to the primary hydroxy group of glucose.
  • the enzyme may also have an activity that degrades natural gum polysaccharide, e.g., xanthan and galactomannan-containing polysaccharides such as guar gum or lima bean gum, by clipping off sugar side chains or cleaving internal bonds to break the polysaccharide backbone.
  • Transglucosidase enzymes that may be employed in the subject compositions are generally described in Barker et al (Studies of Aspergillus niger . Part II. Transglycosidation by Aspergillus niger. J. Chem. Soc. 1953 3588-3593); Pazur et al (The glycoprotein nature and antigenicity of a fungal D-glucosyltransferase. Carbohydr. Res. 1986 149:137-47) and Nakamura et al (Cloning and sequencing of an alpha-glucosidase gene from Aspergillus niger and its expression in A. nidulans J. Biotechnol. 1997 53:75-84).
  • the transglucosidase enzyme that may be employed may be purchased from Megazyme (Co. Wicklow, Ireland) or Genencor Int. (Palo Alto, Calif.) under the trade name Transglucosidase L-500TM.
  • the enzyme may be an Aspergillus niger transglucosidase enzyme produced in Trichoderma reesei cells.
  • the transglucosidase enzyme may be a wild type fungal transglucosidase (e.g., a fungal transglucosidase having an amino acid sequence deposited in NCBI's Genbank database as accession numbers: D45356 (GID:2645159; Aspergillus niger ), BAD06006.1 (GID:4031328; Aspergillus awamori ), BAA08125.1 (GID:1054565; Aspergillus oryzae ), XP — 001210809.1 (GID:115492363; Aspergillus terreus ), XP — 001271891.1 (GID:121707620; Aspergillus clavatus ), XP — 001266999.1 (GID:119500484 ; Neosartorya fischeri ), XP — 751811.1 (GID:70993928 ; Aspergillus fumigatus
  • the enzyme is generally present in the composition at a concentration in the range of 0.01 ppm (parts per million, w/v) to 100 ppm, e.g., 0.01 ppm to 0.05 ppm, 0.05 ppm to 0.1 ppm, 0.1 ppm to 0.5 ppm, 0.5 ppm to 1 ppm, 1 ppm to 5 ppm, 5 ppm to 10 ppm, or 10 ppm to 100 ppm for example.
  • the composition may be a cleaning composition and, as such, the composition may further comprise a surfactant, other cleaning agents, and/or other fabric care agents described in greater detail below.
  • the natural gum polysaccharide may be in an aqueous solution, or affixed to an object, e.g., as a stain that is present on the surface of an object, e.g., a fabric.
  • the natural gum polysaccharide may be in dried form. Since natural gum polysaccharides are commonly employed in a variety of foodstuffs, the object may be, in particular embodiments, soiled with a foodstuff that contains a natural gum polysaccharide.
  • Exemplary foodstuffs that contain a natural gum polysaccharide include, e.g., sauces, creams, dairy products, ice creams, mousses, milkshakes, salad dressings, fruit juice beverages, canned fruit, jelly, soy sauce, oyster sauce, packaged meats, cheese, and bakery products.
  • the natural gum polysaccharide may be present in the foodstuff at a concentration of 0.1% to 1.5%, e.g., 0.1% to 0.5%, 0.5% to 1.0% or 1.0% or 1.5%, for example.
  • the subject transglucosidase enzyme may be produced using conventional methods. For example, it may be secreted into the periplasm (e.g., by Gram-negative organisms, such as E. coli ), or into the extracellular space e.g., by Gram-positive organisms, (such as Bacillus and Actinomyces ), or eukaryotic hosts (e.g., Trichoderma, Aspergillus, Saccharomyces , and Pichia ).
  • periplasm e.g., by Gram-negative organisms, such as E. coli
  • Gram-positive organisms such as Bacillus and Actinomyces
  • eukaryotic hosts e.g., Trichoderma, Aspergillus, Saccharomyces , and Pichia .
  • the subject transglucosidase enzyme may be produced by expressing a fusion protein containing a signal sequence operably linked to the transglucosidase enzyme in a T. reesei host cell.
  • the transglucosidase enzyme is secreted into culture medium, where it can be harvested.
  • the signal sequence of a subject fusion protein may be any signal sequence that facilitates protein secretion from the Trichoderma host cell.
  • the signal sequence employed may be endogenous or non-endogenous to the Trichoderma host cell and, in certain embodiments, may be a signal sequence of a protein that is known to be highly secreted from a Trichoderma sp. host cell.
  • Such signal sequence include, but are not limited to: the signal sequence of cellobiohydrolase I, cellobiohydrolase II, endoglucanases I, endoglucanases II, endoglucanases III, ⁇ -amylase, aspartyl proteases, glucoamylase, mannanase, glycosidase and barley endopeptidase B (see Saarelainen, Appl. Environ. Microbiol. 1997 63: 4938-4940), for example.
  • the transglucosidase may be secreted using its own signal sequence (i.e., the AGL1, AGL2 or AGL3 signal sequences, as described in Margolles-Clark et al supra).
  • its own signal sequence i.e., the AGL1, AGL2 or AGL3 signal sequences, as described in Margolles-Clark et al supra.
  • the transglucosidase may be produced using a nucleic acid which may comprise: a signal sequence-encoding nucleic acid operably linked to an transglucosidase-encoding nucleic acid, where translation of the nucleic acid produces a fusion protein comprising an transglucosidase portion having an N-terminal signal sequence for secretion of the transglucosidase portion from a Trichoderma host cell.
  • a nucleic acid which may comprise: a signal sequence-encoding nucleic acid operably linked to an transglucosidase-encoding nucleic acid, where translation of the nucleic acid produces a fusion protein comprising an transglucosidase portion having an N-terminal signal sequence for secretion of the transglucosidase portion from a Trichoderma host cell.
  • the fusion protein may further contain, in addition to a signal sequence, a “carrier protein” that is a portion of a protein that is endogenous to and highly secreted by the T. reesei sp. host cell.
  • carrier proteins include those of T. reesei mannanase I (Man5A, or MANI), T. reesei cellobiohydrolase II (Cel6A, or CBHII) (see, e.g., Paloheimo et al Appl. Environ. Microbiol. 2003 December; 69(12): 7073-7082) or T. reesei cellobiohydrolase I (CBHI).
  • the carrier protein is a truncated T. reesei CBH1 protein that includes the CBH1 core region and part of the CBH1 linker region.
  • a nucleic acid encoding a fusion protein containing, from amino-terminus to carboxy-terminus, a signal sequence, a carrier protein and a subject phytase in operable linkage may therefore be employed.
  • the coding sequence of the transglucosidase may be codon optimized for expression of the transglucosidase in the host cell used. Since codon usage tables listing the usage of each codon in many host cells, including Trichoderma reesei , are known in the art (see, e.g., Nakamura et al, Nucl. Acids Res. 2000 28: 292) or readily derivable, such nucleic acids can be readily designed giving the amino acid sequence of a transglucosidase to be expressed.
  • the nucleic acid may further contain other elements that are necessary for expression of the transglucosidase enzyme in the host cell.
  • the nucleic acid may contain a promoter for transcription of the coding sequence, and a transcriptional terminator.
  • Exemplary promoters that may be employed in T. reesei include the T. reesei cbh1, cbh2, egl1, egl2, eg5, xln1 and xln2 promoters, or a hybrid or truncated version thereof.
  • the promoter may be a T. reesei cbh1 promoter.
  • Suitable terminators include the T.
  • the promoter and/or terminator may be native or non-endogenous to the Trichoderma sp. host cell.
  • the cell may be genetically modified to reduce expression of secreted proteins that are endogenous to the cell.
  • the cell may contain one or more native genes, particularly genes that encode secreted proteins, that have been deleted or inactivated.
  • one or more protease-encoding genes e.g. an aspartyl protease-encoding gene; see Berka et al, Gene 1990 86:153-162 and U.S. Pat. No. 6,509,171
  • cellulase-encoding genes may be deleted or inactivated.
  • the Trichoderma sp. host cell may be a T.
  • reesei host cell contain inactivating deletions in the cbh1, cbh2 and egl1, and egl2 genes, as described in WO 05/001036.
  • the above-described nucleic acid may be present in the nuclear genome of the Trichoderma sp. host cell or may be present in a plasmid that replicates in the Trichoderma host cell, for example.
  • a nucleic acid may be introduced into the Trichoderma host cell using any one of a number of different techniques, e.g., electroporation, nuclear microinjection, transduction, transfection, (e.g., lipofection mediated and DEAE-Dextrin mediated transfection), incubation with calcium phosphate DNA precipitate, high velocity bombardment with DNA-coated microprojectiles, and protoplast fusion.
  • General transformation techniques are known in the art (See, e.g., Ausubel et al., (1987), supra, chapter 9; and Sambrook (1989) supra, and Campbell et al., (1989) Curr. Genet. 16:53-56). See also WO 05/001036; U.S. Pat. No.
  • the preparation of Trichoderma for transformation includes the preparation of protoplasts from fungal mycelia. (See, Campbell et al., (1989) Curr. Genet. 16:53-56). In certain embodiments, the mycelia are obtained from germinated vegetative spores.
  • the transglucosidase enzyme may be recovered by any convenient method, e.g., by precipitation, centrifugation, affinity, filtration or any other method known in the art.
  • affinity chromatography Tit al., (1984) FEBS Lett. 16:215
  • ion-exchange chromatographic methods Goyal et al., (1991) Biores. Technol. 36:37
  • Fliess et al. (1983) Eur. J. Appl. Microbiol. Biotechnol. 17:314
  • Bhikhabhai et al. (1984) J. Appl. Biochem.
  • transglucosidase may be used without purification from the other components of the culture medium.
  • the culture medium may simply be concentrated, for example, and then used without further purification of the protein from the components of the growth medium, or used without any further modification.
  • a method of degrading a natural gum polysaccharide includes combining (e.g., mixing) a transglucosidase enzyme with a natural gum polysaccharide to degrade the natural gum polysaccharide.
  • Conditions suitable for the activity of the transglucosidase enzymes e.g., the temperature range, pH range, and other reaction components suitable for the activity of a transglucosidase enzyme are known in the art.
  • cleaning methods are also provided. These methods generally include: a) contacting an object soiled with a natural gum polysaccharide with a cleaning composition comprising a transglucosidase enzyme; and b) maintaining the object and cleaning composition together under conditions sufficient to effect degradation of the natural gum polysaccharide and thereby clean the object.
  • the cleaning composition employed in this method may be, e.g., a fabric cleaning composition (e.g., a laundry detergent), a surface cleaning composition, a dish cleaning composition, an automatic dishwasher detergent composition or the like.
  • a fabric cleaning composition e.g., a laundry detergent
  • a surface cleaning composition e.g., a dish cleaning composition
  • an automatic dishwasher detergent composition e.g., a dishwasher detergent composition
  • Formulations for exemplary cleaning compositions are described in great detail in WO0001826, which is incorporated by reference herein.
  • the subject cleaning composition e.g., laundry detergent
  • the subject cleaning composition may contain from about 1% to 80%, e.g., 5% to 50% (by weight) of surfactant, which may be a non-ionic surfactant, cationic surfactant, an anionic surfactant or a zwitterionic surfactant, or any mixture thereof, e.g., a mixture of anionic and nonionic surfactants.
  • Exemplary surfactants include: alkyl benzene sulfonate (ABS), including linear alkyl benzene sulfonate and linear alkyl sodium sulfonate, alkyl phenoxy polyethoxy ethanol (e.g., nonyl phenoxy ethoxylate or nonyl phenol), diethanolamine, triethanolamine and monoethanolamine.
  • ABS alkyl benzene sulfonate
  • alkyl phenoxy polyethoxy ethanol e.g., nonyl phenoxy ethoxylate or nonyl phenol
  • diethanolamine e.g., nonyl phenoxy ethoxylate or nonyl phenol
  • diethanolamine e.g., nonyl phenoxy ethoxylate or nonyl phenol
  • triethanolamine e.g., triethanolamine
  • the subject cleaning composition may be in solid (e.g., in powder or tablet form), liquid form or gel, and may further contain a buffer such as sodium carbonate, sodium bicarbonate, or detergent builder, bleach, bleach activator, an enzyme, an enzyme stabilizing agent, suds booster, suppresser, anti-tarnish agent, anti-corrosion agent, soil suspending agent, soil release agent, germicide, pH adjusting agent, non-builder alkalinity source, chelating agent, organic or inorganic filler, solvent, hydrotrope, optical brightener, dye or perfumes.
  • a buffer such as sodium carbonate, sodium bicarbonate, or detergent builder, bleach, bleach activator, an enzyme, an enzyme stabilizing agent, suds booster, suppresser, anti-tarnish agent, anti-corrosion agent, soil suspending agent, soil release agent, germicide, pH adjusting agent, non-builder alkalinity source, chelating agent, organic or inorganic filler, solvent, hydrotrope, optical brightener, dye or perfumes.
  • the subject cleaning composition may contain a further non-starch food polysaccharide degrading enzyme, e.g., hemicellulase, mannanase, pectinase, xylanase, or pectate lyase and, optionally, one or more other enzymes such as a protease for instance a subtilisin protease and/or SSI protein, or a lipase, amylase, cellulase, cutinase, lipase, oxidoreductase, etc., for the removal of other stains.
  • a further non-starch food polysaccharide degrading enzyme e.g., hemicellulase, mannanase, pectinase, xylanase, or pectate lyase and, optionally, one or more other enzymes such as a protease for instance a subtilisin protease
  • compositions herein A wide variety of other ingredients useful in detergent cleaning compositions can be included in the compositions herein, including: other active ingredients, carriers, hydrotropes, processing aids, dyes or pigments, solvents for liquid formulations, etc. If an additional increment of sudsing is desired, suds boosters such as the C 10 -C 16 alkolamides can be incorporated into the compositions, typically at about 1% to about 10% of the composition by weight.
  • a detergent composition can contain water and other solvents as carriers.
  • Low molecular weight primary or secondary alcohols exemplified by methanol, ethanol, propanol, and isopropanol are suitable.
  • Monohydric alcohols are preferred for solubilizing surfactants, but polyols, such as those containing from about 2 to about 6 carbon atoms and from about 2 to about 6 hydroxy groups (e.g., 1,3-propanediol, ethylene glycol, glycerine, and 1,2-propanediol) can also be used.
  • the compositions may contain from about 5% to about 90%, typically from about 10% to about 50% of such carriers.
  • the detergent compositions herein can be formulated such that during use in aqueous cleaning operations, the wash water may have a pH between about 5.0 and about 11.5. Finished products, thus, are typically formulated at this range. Techniques for controlling pH at recommended usage levels include the use of buffers, alkalis, acids, etc., and are well known to those skilled in the art.
  • the cleaning composition may be an automatic dishwashing detergent that has a working pH in the range of pH 9.0 to pH 11.5, e.g., pH 9.0 to pH 9.5, pH 9.5 to pH 10.0, pH 10.0 to pH 10.5, pH 10.5 to pH 11.0 or pH 11.0 to pH 11.5.
  • the cleaning composition may be a liquid laundry detergent that has a working pH in the range of pH 7.5 to pH 8.5, e.g., pH 7.5 to pH 8.0 or pH 8.0 to pH 8.5.
  • the cleaning composition may be a solid laundry detergent that has a working pH in the range of pH 9.5 to pH 10.5, e.g., pH 9.5 to pH 10.0 or pH 10.0 to pH 10.5.
  • bleaching compounds such as the percarbonates, perborates and the like
  • percarbonates, perborates and the like can be used in such compositions, typically at levels from about 1% to about 15% by weight.
  • such compositions can also contain bleach activators such as tetraacetyl ethylenediamine, nonanoyloxybenzene sulfonate, and the like, which are also known in the art. Usage levels typically range from about 1% to about 10% by weight.
  • Various soil release agents especially of the anionic oligoester type, various chelating agents, especially the aminophosphonates and ethylenediaminedisuccinates, various clay soil removal agents, especially ethoxylated tetraethylene pentamine, various dispersing agents, especially polyacrylates and polyasparatates, various brighteners, especially anionic brighteners, various suds suppressors, especially silicones and secondary alcohols, various fabric softeners, especially smectite clays, and the like can all be used in such compositions at levels ranging from about 1% to about 35% by weight. Standard formularies and published patents contain multiple, detailed descriptions of such conventional materials.
  • Enzyme stabilizers may also be used in the cleaning compositions.
  • Such stabilizers include propylene glycol (preferably from about 1% to about 10%), sodium formate (preferably from about 0.1% to about 1%) and calcium formate (preferably from about 0.1% to about 1%).
  • the formulator may wish to employ various builders at levels from about 5% to about 50% by weight.
  • Typical builders include the 1-10 micron zeolites, polycarboxylates such as citrate and oxydisuccinates, layered silicates, phosphates, and the like.
  • Other conventional builders are listed in standard formularies.
  • chelating agents include chelating agents, clay soil removal/anti redeposition agents, polymeric dispersing agents, bleaches, brighteners, suds suppressors, solvents and aesthetic agents.
  • the cleaning method described herein is more effective at removal of certain stains, e.g., stains from foodstuffs containing natural gum polysaccharides, than equivalent methods that do not employ a transglucosidase enzyme.
  • the subject cleaning composition in comparison to an otherwise equivalent method that does not contain a transglucosidase enzyme, is more effective at stain removal.
  • the subject method removes and/or discolors at least 20%, at least 40%, at least 60%, at least 80% or, in certain embodiments, at least 90% more stain than an equivalent method that does not employ a transglucosidase enzyme.
  • a nucleic acid encoding the mature transglucosidase enzyme of A. niger protein was amplified from the genomic DNA of A. niger by PCR and cloned into the vector pTrex3 to make pTrex3(AGL51M).
  • pTrex3(AGL51M) is illustrated in FIG. 1 .
  • the transglucosidase protein encoded by this vector is operably linked to the CBH1 signal sequence to facilitate its secretion into the growth medium.
  • the transglucosidase coding sequence is flanked by the T. reesei cbh1 promoter and terminator.
  • the nucleotide sequence of the expression cassette of pTrex3(AGL51M) vector is set forth in FIG. 2 .
  • the 7.57 kb XbaI-XbaI fragment of the plasmid pTrex3(AGL51M) was purified by agarose gel electrophoresis and used to transform the spores of the T. reesei Morph 1.1. pyr + strain by electroporation.
  • the electroporation parameters were as follows: voltage—16 kV/cm, capacitance—25 ⁇ F, resistance—50 ⁇ . Electroporation was carried out using a suspension of freshly harvested T. reesei spores suspended in ice-cold 1.2 M sorbitol.
  • the spores were incubated overnight in a rotary shaker (30° C., 200 rpm) in a medium containing 1 M sorbitol, 0.3% glucose, 0.3% Bacto peptone and 0.15% yeast extract.
  • the germinating spores were plated on a selective medium containing acetamide as a sole source of nitrogen (acetamide 0.6 g/l; cesium chloride 1.68 g/l; glucose 20 g/l; potassium dihydrogen phosphate 15 g/l; magnesium sulfate heptahydrate 0.6 g/l; calcium chloride dihydrate 0.6 g/l; iron (II) sulfate 5 mg/l; zinc sulfate 1.4 mg/l; cobalt (II) chloride 1 mg/l; manganese (II) sulfate 1.6 mg/l; agar 20 g/l; pH 4.25). Transformant colonies appeared in about 1 week. Individual transformants were transferred onto fresh acetamide selective plates and allowed to grow for 3-4 days.
  • Isolates showing stable growth on selective medium were used to inoculate 5 ml of Lactose defined medium (WO 2005/001036, p. 60) in 20 ⁇ 175 mm test tubes.
  • the tubes were fixed in a rotary shaker at about 45° angle and shaken at 200 rpm and 28° C. for 4-5 days.
  • Electrophoretic analysis (not shown) of the culture supernatants demonstrated the presence of a new protein band of approximately expected molecular weight.
  • transglucosidase activity by the transformants was also confirmed using an enzymatic assay.
  • the assay was carried out in 100 mM sodium acetate buffer, pH 4.5, containing 4 mM para-nitrophenyl- ⁇ -glucoside and 1 mg/ml BSA. After 30 min incubation at 30° C. the reaction was terminated by the addition of an equal volume 1 M sodium carbonate and OD 405 was recorded.
  • transformants expressed 1-2 U transglucosidase activity (expressed as micromoles of para-nitrophenol liberated per min) per ml of culture broth. In untransformed controls, the activity was below detection limit.
  • Transglucosidase Degrades Xanthan Gum
  • Hydrolytic activity by enzymes on xanthan gum was measured by the reducing sugar assay using the PAHBAH (para-hydroxybenzoic acid hydrazide) reagent (Lever et al, Anal. Biochem. 1972 47: 273).
  • PAHBAH para-hydroxybenzoic acid hydrazide
  • Xanthan gum (CAS 111 38-66-2) was purchased from Sigma Chemicals, St. Louis Mo. and dissolved in 50 mM sodium acetate buffer pH 6.0 at a concentration of 0.2%.
  • AATCC standard heavy duty liquid detergent was added at 1.5 ml per liter (0.15%).
  • the AATCC HDL liquid detergent contained 12% linear alkyl sulfonates, 8% alcohol ethoxylates, 8% propanediol, 1.2% citric acid, 4% fatty acid and 4% sodium hydroxide with the balance being water.
  • the assay was performed as follows in a 24 well microplate (COSTAR 3526, Corning Incorporated, Corning, N.Y.): one ml of buffer was added to well 1, one ml of buffer plus enzyme was added to well 2, one ml of buffer and substrate to well 3, and one ml of buffer, plus substrate and enzyme was added to well 4. For statistical purposes, each well may be set up 2 to 4 times. Enzymes to be tested are usually diluted in reaction buffer from 1 to 10 to 1 to 1000. After all reagents were added, a plastic cover was place over the microplate and the cover and plate intersection was wrapped tightly with several layers of Parafilm (Pechiney Plastic Packing, Menasha, Wis.) to prevent evaporation. The reaction plate was incubated for 1 to 16 hr, at 37 C on a shaker rotating at 100 rpm.
  • Parafilm Parafilm
  • Reducing sugar activity was measured using an Eppendorf Mastercycler Gradient (Eppendorf Scientific, Westbury, N.Y.) thermal cycler and 0.2 ml disposable PCR (polymerase chain reaction) strip tubes and caps purchased from VWR International, West Chester, Pa.
  • Reducing sugar reagent was prepared as follows: to 10 ml of 2% sodium hydroxide in distilled water, add 0.15 g of sodium potassium tartrate tetrahydrate (Rochelle Salt, Sigma Chemical Co.) and 0.15 g of parahydroxybenzoic acid hydrazide (H-9882, Sigma Chemical Co.). The solution called PAHBAH reagent was swirled to solubilize all ingredients and put on ice in the dark until used. This reagent was made fresh daily.
  • PAHBAH reagent 0.160 ml was added to each tube of a PCR strip followed by 5 to 20 ul of enzyme samples and controls. All tubes were capped tightly, placed in the thermal cycler, and incubated for 15 min at 99 C followed by cooling at 4 C for at least 15 min. After cooling, strip tube caps were removed and 0.15 ml of each sample was placed in a 96 well flat bottomed microplate (COSTAR 9017, Corning Inc. Corning, N.Y.) and read by a Spectra Max 250 Plate Reader (Molecular Devices, Sunnyvale, Calif.) at 405 nm against a blank of distilled water.
  • COSTAR 9017 Corning Inc. Corning, N.Y.
  • Each enzyme sample was analyzed as follows: the optical density (OD) of the control sample was subtracted from the OD of the buffer sample and this value was added to the substrate buffer control. The O.D. of the enzyme plus substrate reaction was compared to the sum of the substrate and sample controls.
  • FIG. 3 shows that transglucosidases produced in Trichoderma (Trip-TG) and in Aspergillus (Mega-TG) showed significant reducing sugar activity on xanthan gum in 50 mM acetate buffer plus AATCC heavy duty liquid detergent at pH 6.0.
  • Salad dressing with pigment STC CFT CS-6
  • guar-pigment STC CFT CS-43
  • soiled cotton swatches were obtained from Test Fabrics, Inc. West Pittston, Pa., USA. Swatches for the microplate assay were cut into 15 mm circles (disks) with textile Punch Press Model B equipped with a 5 ⁇ 8′′ die cutter. Single swatch disks were placed into each well of a 24-well microplate (Costar 3526).
  • One (1) ml of washing solution containing per liter, 1.5 ml AATCC HDL detergent, 50 mM Hepes buffer, and 6 to 60 ppm enzyme diluted in 50 mM Hepes buffer pH 7.4 was added to each well.
  • microplate was covered with a plastic lid and aluminum foil and incubated at 37° C. with 100 rpm gentle rotation for 4-16 hr. The plates were removed from the shaker and the detergent solution was removed by aspiration. Each microplate well was washed three (3) times with 1.5 ml of Dulbecco's PBS pH 7.3 and three (3) times with 1.5 ml of distilled water. Each disk was removed from its well and dried overnight between sheets of paper towels and not exposed to direct light. Disks were inspected visually and then analyzed with a Minolta Reflectometer CR-200 calibrated on a standard white tile. The average L values with standard deviations were calculated.
  • the graphs of FIG. 4 show that Trip-TG (diluted 1/50 in 50 mM Hepes buffer) removes soil from both salad dressing stains and guar-pigment stains in 50 mM Hepes buffer pH 7.4 and in 50 mM Hepes buffer pH 7.4 plus 0.15% AATCC HDL.
  • FIG. 5 shows the results obtained in a Trip-TG dose response microswatch experiment.
  • Trip-TG removed salad dressing soils at 1 ppm in 0.15% AATCC heavy duty liquid.
  • FIG. 6 shows that Trip-TG removed salad dressing soil in a microswatch cleaning experiment in 0.1% North American AATCC-1993 HDD standard without brightner.
  • This detergent contained 18% linear alkyl sulfonates, 25% Zeolite A, 18% soda ash, 0.5% sodium silicate, 22% sodium sulfate, 10% moisture, and a 6.3% n hole for copolymer or other additives.
  • Tergotometer studies used a 6 pot Tergotometer Model 7243S (U.S. Testing, Co. Inc. Hoboken, N.J.) maintained at 30° C. Agitation speed was set to 100 rpm.
  • Cotton swatches (5 per each tergotometer pot) obtained from Warwick Equest Limited, Consett, County Durham, England, stained with circles of foodstuffs were added to 1 liter of 0.15% AATCC HDL detergent containing 6 gpg hardness (diluted from stock 15000 gpg hardness solution containing 1.735 M calcium chloride and 0.67 M magnesium chloride) and 25 mM Hepes buffer pH 7.4 After a 30 min wash cycle, the swatches were washed three times in 1.5 l of cold tap water, spun for 7 min in a spin cycle to remove excess water, and dried overnight at room temperature.
  • % SRI Percent soil release
  • transglucosidase effectively degrades xanthan, and removes certain soils from cotton swatches.

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WO2010115664A2 (en) 2009-03-30 2010-10-14 Unilever Nv Fabric conditioning composition
US20100304468A1 (en) * 2007-05-21 2010-12-02 Danisco Us, Inc., Genencor Division Method for introducing nucleic acids into fungal cells
US9458441B2 (en) 2012-05-07 2016-10-04 Novozymes A/S Polypeptides having xanthan degrading activity and polynucleotides encoding same
US9982284B2 (en) 2014-02-27 2018-05-29 E I Du Pont De Nemours And Company Enzymatic hydrolysis of disaccharides and oligosaccharides using alpha-glucosidase enzymes
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Families Citing this family (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2597660B2 (ja) 1988-07-11 1997-04-09 王子製紙株式会社 静電気防止方法
US20120107872A1 (en) 2010-10-20 2012-05-03 Andrei Miasnikov Thermostable trichoderma cellulase
CN113834757B (zh) * 2021-07-30 2024-02-23 广东美味鲜调味食品有限公司 一种对蚝油原料的耐高温淀粉酶微量残留的快速检测方法

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6410498B1 (en) * 1999-04-30 2002-06-25 Procter & Gamble Company Laundry detergent and/or fabric care compositions comprising a modified transferase
US6486112B1 (en) * 1997-08-14 2002-11-26 The Procter & Gamble Company Laundry detergent compositions comprising a saccharide gum degrading enzyme
US7498318B1 (en) * 1999-11-11 2009-03-03 N.V. Nutricia Food for diabetics

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
HU213043B (en) * 1990-09-28 1997-01-28 Procter & Gamble Detergent increasing the enzymatic activity and comprising polyhydroxy fatty acid amides
EP0896998A1 (en) * 1997-08-14 1999-02-17 The Procter & Gamble Company Laundry detergent compositions comprising a saccharide gum degrading enzyme
CA2330687A1 (en) * 1998-04-29 1999-11-04 Christian Leo Marie Vermote Laundry detergent and/or fabric care compositions comprising a transferase
JP2002513563A (ja) * 1998-05-01 2002-05-14 ザ、プロクター、エンド、ギャンブル、カンパニー 修飾トランスフェラーゼを含有した洗濯洗剤および／または布帛ケア組成物

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6486112B1 (en) * 1997-08-14 2002-11-26 The Procter & Gamble Company Laundry detergent compositions comprising a saccharide gum degrading enzyme
US6410498B1 (en) * 1999-04-30 2002-06-25 Procter & Gamble Company Laundry detergent and/or fabric care compositions comprising a modified transferase
US7498318B1 (en) * 1999-11-11 2009-03-03 N.V. Nutricia Food for diabetics

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US9988657B2 (en) 2014-02-27 2018-06-05 E I Du Pont De Nemours And Company Enzymatic hydrolysis of disaccharides and oligosaccharides using alpha-glucosidase enzymes
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WO2025198996A1 (en) 2024-03-19 2025-09-25 Danisco Us Inc. Method for improving flavor in foodstuff
WO2026015598A2 (en) 2024-07-11 2026-01-15 International N&H Denmark Aps Method to provide improved texture and stable sucrose levels in foodstuff with glucosyltransferase

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JP5230031B2 (ja) 2013-07-10
KR20090122448A (ko) 2009-11-30
CN101641433A (zh) 2010-02-03
BRPI0809150A2 (pt) 2014-09-16
RU2501855C2 (ru) 2013-12-20
JP2010522271A (ja) 2010-07-01
WO2008118382A2 (en) 2008-10-02
WO2008118382A3 (en) 2009-02-26
CA2681657A1 (en) 2008-10-02
EP2126024A2 (en) 2009-12-02
KR101443412B1 (ko) 2014-10-07
RU2009138938A (ru) 2011-04-27

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