EP1088128A1 - Procede de traitement enzymatique de la laine - Google Patents

Procede de traitement enzymatique de la laine

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Publication number
EP1088128A1
EP1088128A1 EP99922991A EP99922991A EP1088128A1 EP 1088128 A1 EP1088128 A1 EP 1088128A1 EP 99922991 A EP99922991 A EP 99922991A EP 99922991 A EP99922991 A EP 99922991A EP 1088128 A1 EP1088128 A1 EP 1088128A1
Authority
EP
European Patent Office
Prior art keywords
wool
transglutaminase
treatment
proteolytic enzyme
protease
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.)
Withdrawn
Application number
EP99922991A
Other languages
German (de)
English (en)
Inventor
Jason Patrick Mcdevitt
Jakob Winkler
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes North America Inc
Original Assignee
Novo Nordisk Biochem North America Inc
Novo Nordisk Biochem Inc
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Priority claimed from US09/161,824 external-priority patent/US6051033A/en
Application filed by Novo Nordisk Biochem North America Inc, Novo Nordisk Biochem Inc filed Critical Novo Nordisk Biochem North America Inc
Publication of EP1088128A1 publication Critical patent/EP1088128A1/fr
Withdrawn legal-status Critical Current

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Classifications

    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M15/00—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
    • D06M15/19—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment with synthetic macromolecular compounds
    • D06M15/37—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • D06M15/61—Polyamines polyimines
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M13/00—Treating fibres, threads, yarns, fabrics or fibrous goods made from such materials, with non-macromolecular organic compounds; Such treatment combined with mechanical treatment
    • D06M13/322—Treating fibres, threads, yarns, fabrics or fibrous goods made from such materials, with non-macromolecular organic compounds; Such treatment combined with mechanical treatment with compounds containing nitrogen
    • D06M13/325—Amines
    • D06M13/332—Di- or polyamines
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
    • D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M2101/00—Chemical constitution of the fibres, threads, yarns, fabrics or fibrous goods made from such materials, to be treated
    • D06M2101/02—Natural fibres, other than mineral fibres
    • D06M2101/10—Animal fibres
    • D06M2101/12—Keratin fibres or silk
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M2200/00—Functionality of the treatment composition and/or properties imparted to the textile material
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M2200/00—Functionality of the treatment composition and/or properties imparted to the textile material
    • D06M2200/35—Abrasion, pilling or fibrillation resistance
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M2200/00—Functionality of the treatment composition and/or properties imparted to the textile material
    • D06M2200/45—Shrinking resistance, anti-felting properties
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M2200/00—Functionality of the treatment composition and/or properties imparted to the textile material
    • D06M2200/50—Modified hand or grip properties; Softening compositions

Definitions

  • the present invention relates to a method of treating wool, wool fibers or animal hair with a transglutaminase and a proteolytic enzyme.
  • Plasma treatment is a dry process which involves treating wool fiber material with electrical gas discharges (so-called plasma).
  • plasma electrical gas discharges
  • JP-A 51099196 describes a process to treat wool fabrics with alkaline proteases.
  • JP-A 3213574 describes a method to treat wool using transglutaminase (an enzyme naturally found in wool follicles from sheep) or a solution containing transglutaminase.
  • WO 98/27264 describes a method for reducing the shrinkage of wool comprising contacting wool with an oxidase or a peroxidase solution under conditions suitable for reacting the enzyme with wool.
  • US 5,529,928 describes a process for obtaining a wool with a soft woolly handle and shrink-resistant properties by using an initial chemical oxidative step or an enzyme treatment (e.g.
  • EP 358386 A2 describes a method to treat wool which comprises a proteolytic treatment and one of or both an oxidative treatment (such as NaOCl) and a polymer treatment.
  • EP 134267 describes a method for treating animal fibers with an oxidizing agent, followed by a proteolytic enzyme in a salt-containing composition.
  • the object of the present invention is to provide improved enzyme-based methods for treating wool, wool fibers or animal hair, in particular methods which provide advantages with regard to improved shrink-resistance, and/or improvements of softness and handle which are highly desired by the end-user, while minimizing fiber damage relative to existing degradative treatments of wool and other animal hair materials.
  • the invention relates to a method of treating wool, wool fibers or animal hair, comprising contacting the wool, wool fibers or animal hair in aqueous solution with a proteolytic enzyme, either preceding or, preferably, simultaneously with a transglutaminase.
  • the scalar structure of wool is responsible to a large degree for many of its properties, both good and bad, and is primarily responsible for wool's tendency to shrink.
  • One way to achieve shrink-resistance is to remove the scales from the surface of wool. This process is not industrially practical for a number of reasons, in particular the extreme strength and weight losses that occur.
  • An ideal commercial process for imparting shrink- resistance would necessarily alter the physical structure of the fiber surface without significantly weakening the fiber.
  • many methods that alter the scale structure including conventional proteolytic enzyme treatment) do so via destructive means.
  • chemical bonds are ruptured, causing molecular weight degradation of the proteins. This molecular weight breakdown is responsible for the macroscopically observed reduction in strength and weight of the wool or animal hair textiles.
  • the present invention describes a method that uses two complementary enzymes to substantially modify the surface structure of the fiber while also minimizing degradation.
  • Proteolytic enzymes cleave amide bonds, while transglutaminases form amide bonds, albeit different ones.
  • proteolytic enzymes are primarily responsible for breaking down the surface structure, while transglutaminases aid in that process, and also prevent the excessive molecular weight breakdown associated with proteolytic enzyme treatments. Consequently, relative to conventional proteolytic treatments, the treatments described in the present invention provide superior shrink- resistance, with reduced fiber damage.
  • Other benefits are also achieved, either relative to untreated wool, wool treated with proteolytic enzymes, or wool treated with transglutaminases .
  • the benefits resulting from this treatment can be improved shrink-resistance, improved handle, improved appearance, improved wettability, reduction of felting tendency, increased whiteness, reduction of pilling, improved softness, tensile strength retention, improved stretch, improved burst strength, and improved dyeing characteristics such as dye uptake and dye washfastness. Furthermore, this combination reduces fiber damage, as manifested by reductions in fabric weight loss and burst strength, relative to protease treatments alone.
  • the wool, wool fibers or animal hair may have undergone an oxidative pre-treatment prior to any of the enzymatic treatments described above.
  • oxidative pre-treatments include acidic chlorination, DCCA, sodium hypochlorite, caroat, and permanganate, as well as enzymatic treatments using oxidoreductases such as peroxidase or haloperoxidase.
  • the term "shrinkage” refers to the felting shrinkage of fibers as defined in IWS TM 31, i.e., felting shrinkage is the irreversible shrinkage caused by progressive entanglement of the wool fibers induced by washing in an aqueous solution, and is defined as the reduction in length and/or width induced by washing. Shrinkage can be measured in accordance with IWS TM 31, or it can be measured using the following modification. Wool samples (24 cm x 24 cm) are sewed around the edges and inscribed with a rectangle (18 cm x 18 cm). Samples are treated, air-dried, then subjected to five cycles of machine washing and drying (warm wash, high heat of drying) in combination with external ballast such as towels and articles of clothing. The dimensions of the rectangle are measured after five cycles, and the shrinkage is defined as the change in dimensions of the rectangle, after accounting for initial relaxation shrinkage.
  • a reduction in shrinkage implies a reduction in felting, and thus all methods that provide improved shrink-resistance also provide "anti-felting" properties.
  • handle is a subjective term that refers to the sensation of touch or feel of a textile.
  • softness is a subjective term referring to the feel of a textile, and is a component of handle.
  • pilling refers to the entangling of fibers into balls (pills), which are visible on the surface of a fabric.
  • a pill is of sufficient density that it will cast a shadow. Resistance to pilling can be measured according to IWS Test Method 196, or can be inspected visually. Pilling is a major component of fabric appearance (along with other properties such as whiteness). Reduced pilling gives better appearance and improved resistance to pilling is implied herein wherever the term “superior appearance" is used.
  • stretch refers to the increase in length of a fibrous material when a fixed load is applied. In general, a higher value for stretch is preferred relative to a lower value.
  • elongation refers to the permanent increase in length (non-recoverable extension) of a fibrous material after application and removal of a fixed load. In general, a lower value for elongation is preferred relative to a higher value. Stretch and elongation have been measured in accordance with the following modification of IWS TM 179. Fabric strips (100 mm x 55 mm rectangles, with the longer dimension in the weft direction) were placed in the jaws of a suitable tensile strength machine such as an Instron ® 5564.
  • the distance between the jaws was set at 60 mm, and the load was increased to ION at a rate of extension of 100 mm/min. Once the desired load was reached, the direction of movement was immediately reversed, and the rate of contraction was equal to the rate of extension. Five cycles were performed.
  • burst strength refers to the pressure applied to a circular specimen in distending it to rupture. Burst strength can be measured (using a suitable apparatus such as the Mullen ® tester from B.F. Perkins) in accordance with IWS TM 29, and can be performed on either wet or dry fabric.
  • Dyeing characteristics refers to properties associated with dyeing of wool or animal hair material, including dye uptake and dye color fastness to wet alkaline contact (as defined in IWS TM 174).
  • Dye uptake is a measure of the capacity of wool or animal hair material immersed in a dye solution to absorb available dyestuff. This property can be measured by the following test.
  • wool or animal hair material is added to a buffered solution of acid black 172 (300 ml of 0.05 M NaOAc buffer, pH 4.5, plus 7.5 mL of a 1.0% w/w solution of acid black 172 in water). The vessel is incubated in a shaking water bath at 50°C for 15 minutes with mild agitation.
  • Dye uptake is determined by the L* reading, and changes in dye uptake are found by determining dL* relative to untreated material.
  • wool By the term “wool,” “wool fiber, “ “animal hair,” and the like, is meant any commercially useful animal hair product, for example, wool from sheep, camel, rabbit, goat, llama, and known as merino wool, Shetland wool, cashmere wool, alpaca wool, mohair, etc.
  • the method of the invention can be used with wool or animal hair material in the form of top, fiber, yarn, or woven or knitted fabric.
  • the enzymatic treatment can also be carried out on loose flock or on garments made from wool or animal hair material.
  • the treatment can be performed at many different stages of processing, including either before or after dyeing.
  • a range of different chemical additives can be added along with the enzymes, including wetting agents and softeners.
  • wool and other animal hair materials are products of biological origin.
  • the material may vary greatly, e.g., in chemical composition and morphological structure depending on the living conditions and health of the animal. Accordingly, the effect(s) obtained by subjecting wool or other animal hair products to the method of the present invention may vary in accordance with the properties of the starting material.
  • enzymatic treatments can take place either as stand-alone steps or in combination with other treatments such as scouring or dyeing of wool or animal hair material.
  • Wool or animal hair material is subjected to treatment with a transglutaminase either subsequent to or, preferably, simultaneously with a proteolytic enzyme treatment.
  • chemical additives such as surfactants and softeners can be included in enzyme treatment steps, or in separate steps.
  • Such treatments can produce wool textiles having a novel combination of physical properties, such as improved handle, shrink-resistance, and appearance while reducing strength losses and fiber damage commonly observed in degradative treatments of wool.
  • the enzymatic treatment steps are preferably carried out for a duration of at least 1 minute and less than 150 minutes; preferably at a temperature from about 15°C to about 90°C, more preferably from about 20°C to about 70°C, in particular from about 30°C to about 65°C.
  • the wool can be soaked in or padded with an aqueous treatment solution and then subjected to steaming at a conventional temperature and pressure. It is contemplated that the reaction rate of the enzyme treatment step can be increased by increasing the temperature of the enzyme bath during the treatment, i.e., the total treatment time can be reduced.
  • the enzyme treatment can be carried out in an acidic, neutral or alkaline medium, depending on the particular enzyme in question.
  • the medium may include a buffer. It may be advantageous to carry out the enzyme treatment step in the presence of one or more conventional anionic, non-ionic or cationic surfactants.
  • An example of a useful nonionic surfactant is Dobanol (from Henkel AG).
  • a useful proteolytic enzyme for the method of the present invention is any enzyme having proteolytic activity at the actual process conditions, including a combination of two or more such enzymes.
  • the enzyme may be a proteolytic enzyme of plant origin, e.g., papain, bromelain, ficin, or of animal origin, e.g. trypsin and chymotrypsin, or of microbial origin, i.e., bacterial or fungal origin or from yeasts. It is to be understood that any mixture of various proteolytic enzyme may be applicable in the process of the invention.
  • any proteolytic enzyme variant can be used in the process of the present invention, wherein the term "variant” means an enzyme produced by an organism expressing a gene encoding a proteolytic enzyme, and wherein said gene has been obtained by mutation of a naturally occurring proteolytic enzyme gene, the mutation being of either random or site-directed nature, including the generation of the mutated gene through gene shuffling.
  • the proteolytic enzyme is a serine- protease, a metallo-protease, or an aspartate-protease.
  • a serine protease is an enzyme that catalyzes the hydrolysis of peptide bonds, and contain an essential serine residue at the active site (White, Handler and Smith, 1973 "Principles of Biochemistry," Fifth Edition, McGraw-Hill Book Company, NY, pp. 271-272). They are inhibited by diisopropyl- fluorophosphate, but in contrast to metalloproteases, are resistant to ethylene diamino tetraacetic acid (EDTA) (although they are stabilized at high temperatures by calcium ions).
  • EDTA ethylene diamino tetraacetic acid
  • Serine proteases hydrolyze simple terminal esters and are similar in activity to eukaryotic chymotrypsin, also a serine protease.
  • a more narrow term, alkaline protease, covering a sub-group, reflects the high pH optimum of some of the serine proteases, from pH 9.0 to 11.0.
  • the serine proteases usually exhibit maximum proteolytic activity in the alkaline pH range, whereas the metallo-proteases and the aspartate-proteases usually exhibit maximum proteolytic activity in the neutral and the acidic pH range, respectively.
  • subtilases A sub-group of the serine proteases is commonly designated the subtilases (Siezen et al. , Protein Engng. 4 (1991) 719-737). They are defined by homology analysis of more than 40 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases. A subtilisin was previously defined as a serine protease produced by Gram- positive bacteria or fungi, and according to Siezen et al. , now is a subgroup of the subtilases.
  • subtilases The amino acid sequences of a number of subtilases have been determined, including at least six subtilases from Bacillus strains, namely, subtilisin 168, subtilisin BPN', subtilisin Carlsberg, subtilisin DY, subtilisin amylosacchariticus, and mesentericopeptidase, one subtilisin from an actinomycetales, thermitase from Thermoacti- nomyces vulgaris, and one fungal subtilisin, proteinase K from Tritirachium album.
  • subtilisins The long time recognized group of serine proteases, the subtilisins, have according to this more recent grouping been divided into two sub-groups.
  • subtilisin 168 subtilisin 168
  • subtilisin BPN' subtilisin Carlsberg
  • subtilisin DY subtilisin DY
  • the other subgroup, I-S2 is described as highly alkaline subtilisins and comprise enzymes such as subtilisin PB92 (MAXACAL ® , Genencor International, Inc.), subtilisin 309 (SAVINASE ® , Novo Nordisk A/S), subtilisin 147 (ESPERASE ® , Novo Nordisk A/S), and alkaline elastase YaB.
  • subtilisins of group I-S2 and variants thereof constitute a preferred class of proteases which are useful in the method of the invention.
  • An example of a useful subtilisin variant is a variant of subtilisin 309 (SAVIN ASE°) wherein, in position 195, glycine is substituted by phenylalanine (G195F or 195 Gly to 195 Phe).
  • conventional fermented commercial proteases are useful.
  • commercial proteases are Alcalase * (produced by submerged fermentation of a strain of Bacillus licheniformis) , Esperase * (produced by submerged fermentation of an alkalophi- lic species of Bacillus), Rennilase * (produced by submerged fermentation of a non- pathogenic strain of Mucor miehe ⁇ ), Savinase * (produced by submerged fermentation of a genetically modified strain of Bacillus), e.g., the variants disclosed in the International Patent Application published as WO 92/19729, and Durazym" (a protein-engineered variant of Savinase” .
  • proteases All the mentioned commercial proteases are produced and sold by Novo Nordisk A/S, DK-2880 Bagsvaerd, Denmark.
  • Other preferred serine proteases are proteases from Nocardiopsis , Aspergillus, Rhizopus, Bacillus alcalophilus, B. cereus, N. natto, B. vulgatus, B. mycoide, and subtilins from Bacillus, especially proteases from the species Nocardiopsis sp. and Nocardiopsis dassonvillei such as those disclosed in the International Patent Application published as WO 88/03947, especially proteases from the species Nocardiopsis sp. , NRRL 18262, and Nocardiopsis rougevillei, NRRL 18133.
  • proteases are the serine proteases from mutants of Bacillus subtilins disclosed in the International Patent Application Nos. PCT/DK89/00002 and PCT/DK97/00500, and in the International Patent Application published as WO 91/00345, and the proteases disclosed in EP 415 296 A2.
  • proteases are the metallo-proteases of microbial origin. Conveniently, conventional fermented commercial proteases are useful. An example of such a commercial protease is Neutrase * (Zn) (produced by submerged fermentation of a strain of Bacillus subtilis), which is produced and sold by Novo Nordisk A/S, DK-2880 Bagsvaerd, Denmark.
  • protease enzyme preparation is BactosolTM WO and Bac- tosolTM SI, available from Sandoz AG, Basle, Switzerland; ToyozymeTM, available from Toyo Boseki Co. Ltd., Japan; and Proteinase KTM (produced by submerged fermentation of a strain of Bacillus sp. KSM-K16), available from Kao Corporation Ltd. , Japan.
  • the amount of proteolytic enzyme used is preferably in the range 0.001 g to 20 g, preferably in the range 0.01 g to 10 g, more preferably in the range 0.05 g to 5 g per kg wool, fiber, or hair.
  • transglutaminase to be used according to the invention can be any transglutaminase, which includes both calcium-dependent and calcium-independent transglutaminases or mixtures of two or more transglutaminases.
  • Transglutaminases are protein-glutamine ⁇ -glutamyltransferases, and have been classified as enzymes having the number EC 2.3.2.13 according to Enzyme Nomenclature, Academic Press, Inc., 1992.
  • Transglutaminases are enzymes capable of catalyzing an acyl transfer reaction, in which a ⁇ -carboxamide group of a peptide-bound glutamine residue is the acyl donor.
  • Primary amino groups in a variety of compounds may function as acyl acceptors with the subsequent formation of monosubstituted gamma-amides of peptide-bound glutamic acid.
  • the transglutaminases form intramolecular or intermolecular ⁇ -( ⁇ -glutamyl)lysine cross-links.
  • transglutaminases A wide array of transglutaminases has been identified and isolated from a number of animals and a few plant species.
  • the most widely used animal-derived transglutaminase, Factor XHIa, is a multi-subunit enzyme.
  • transglutaminases may be of mammalian origin, such as of human or bovine origin, of marine origin, such as derived from sea squirt (Halocynthia roretzi), or of microbial origin, such as of bacterial, yeast of filamentous fungus origin, or variants thereof.
  • mammalian origin such as of human or bovine origin
  • marine origin such as derived from sea squirt (Halocynthia roretzi)
  • microbial origin such as of bacterial, yeast of filamentous fungus origin, or variants thereof.
  • the transglutaminase is Factor XHIa of human origin.
  • the transglutaminase is a microbial transglutaminase derived from Streptomyces lydicus (former Streptomyces libani), or variants thereof.
  • Other suitable microbial transglutaminases have been described, including a transglutaminase from Physarum polycephalum (Klein et al., Journal of Bacteriology, Vol.
  • transglutaminases from Streptoverticillium, in particular from Streptover- ticillium mobaraense, Streptoverticillium cinnamoneum, and Streptoverticillium griseocar- neum (Motoki et al. , U.S. 5,156,956), and from Streptomyces lavendulae (Andou et al., U.S. 5,252,469).
  • the transglutaminases described in EP 481 504-A1 (Amano Pharmaceutical Co. LTD.) and WO 96/06931 (Novo Nordisk A/S), which are hereby incorporated by references, may also be used.
  • transglutaminases derived from the class of fungi-like organisms Oomycetes, preferably from the genus Phytophthora, may be used.
  • Oomycetes preferably from the genus Phytophthora
  • Other relevant Oomycetes transglutaminases are described in PCT/DK96/00031 (Novo Nordisk A/S), which are hereby incorporated by reference.
  • Preferred transglutaminases are Phytophthora cactorum and Streptoverticillium mobaraense (available from Ajinomoto).
  • the amount of transglutaminase used is in the range 0.001 g to 10 g, preferably in the range 0.01 g to 5 g, more preferably in the range 0.02 g to 2 g per kg wool, fiber, or hair.
  • the transglutaminase is added together with a polyamino- containing compound R,NHR 2 NHR 3 , wherein R,, R 2 , and R 3 can be independently hydrogen, hydrocarbyl, or substituted hydrocarbyl, and any combination of R,, R 2 , and R 3 may or may not join together to form one or multiple rings, where the term "hydrocarbyl” means a linear, branched, or cyclic group which contains only carbon and hydrogen atoms; the term “heteroatom” refers to atoms other than carbon and hydrogen; and the term “substituted hydrocarbyl” refers to a hydrocarbyl substituted with one or more heteroatoms.
  • polyamino-containing compounds are 1,12-diaminododecane and polyethylenimine.
  • the softeners conventionally used on wool are usually cationic softeners, either organic cationic softeners or silicone- based products, but anionic or non-ionic softeners are also useful.
  • useful softeners are polyethylene softeners and silicone softeners, i.e., dimethyl polysiloxanes (si- licone oils), H-polysiloxanes, silicone elastomers, aminofunctional dimethyl polysiloxanes, aminofunctional silicone elastomers, and epoxyfunctional dimethyl polysiloxanes, and organic cationic softeners, e.g., alkyl quarternary ammonium derivatives.
  • silicone softeners i.e., dimethyl polysiloxanes (si- licone oils), H-polysiloxanes, silicone elastomers, aminofunctional dimethyl polysiloxanes, aminofunctional silicone elastomers, and epoxyfunctional dimethyl polysiloxanes
  • organic cationic softeners e.g., alkyl quarternary ammonium derivatives.
  • Swatches (24 cm x 24 cm, with 18 x 18 cm 2 rectangle inscribed on each, approximately 9 g each) of jersey knit wool (TestFabrics TF532) were sewn around the edges. Samples were placed in separate Launder-O-meter beakers containing 250 mL of a 0.04 M Tris buffer, pH 8.25 at 25°C, containing 5 mM calcium chloride. A solution of ESPERASE ® 8.0 L (200 ⁇ l) was added to the vessels, followed immediately by a solution of Phytophthora cactorum transglutaminase (containing 4 mg transglutaminase).
  • the vessels were placed in the Launder-O-meter and allowed to react for 40 minutes at 44°C, followed by a ten minute heating gradient up to 80°C, then held at that temperature for ten minutes to inactivate the enzymes.
  • the sample was removed from the solution, rinsed, dried, and measured, then subjected to five cycles of machine washing and drying, before being subjected to further property testing.
  • Two swatches (24 cm x 24 cm, with 18 x 18 cm 2 rectangle inscribed on each, approximately 9 g each) of jersey knit wool (TestFabrics TF532) were sewn around the edges.
  • the swatches were immersed in 500 ml of a 25 mM sodium acetate buffer containing 10 mM NaCl and 10 mM hydrogen peroxide, pH 5, and treated with Curvularia verruculosa haloperoxidase (3.3 mg pure enzyme) for 50 minutes at 40°C in an incubating shaker bath. After 30 minutes, sufficient hydrogen peroxide was added to boost the depleted peroxide concentration by 5 mM.
  • Two swatches (24 cm x 24 cm, with 18 x 18 cm 2 rectangle inscribed on each, approximately 9 g each) of jersey knit wool (TestFabrics TF532) were sewn around the edges.
  • the swatches were immersed in 500 ml of a 25 mM sodium acetate buffer containing 10 mM NaCl and 10 mM hydrogen peroxide, pH 5, and treated with Curvularia verruculosa haloperoxidase (3.3 mg pure enzyme) for 50 minutes at 40°C in an incubating shaker bath. After 30 minutes, sufficient hydrogen peroxide was added to boost the depleted peroxide concentration by 5 mM.
  • Two swatches (24 cm x 24 cm, with 18 x 18 cm 2 rectangle inscribed on each, approximately 9 g each) of jersey knit wool (TestFabrics TF532) were sewn around the edges.
  • the swatches were immersed in 500 ml of a 25 mM sodium acetate buffer containing 10 mM NaCl and 10 mM hydrogen peroxide, pH 5, and treated with Curvularia verruculosa haloperoxidase (3.3 mg pure enzyme) for 50 minutes at 40°C in an incubating shaker bath. After 30 minutes, sufficient hydrogen peroxide was added to boost the depleted peroxide concentration by 5 mM.
  • the sample had a very soft handle, a pleasing appearance as a result of increased whitening and reduced pilling, and an area shrinkage of only 12% after five wash-dry cycles, corresponding to a shrink-resistance of 64%.
  • Example 5 Treatment with Sodium hvpochlorite. Savinase, and Transglutaminase.
  • a swatch (24 cm x 24 cm, with inscribed 18 x 18 cm 2 rectangle, approximately 9 g) of jersey knit wool (TestFabrics TF532) was sewn around the edges.
  • the swatch was immersed in 250 ml of a 25 mM sodium acetate buffer containing 10 mM NaCl, pH 5, and treated with 1.5 ml of a commercial solution of sodium hypochlorite (Austin's ® bleach, 5.25% sodium hypochlorite).
  • the reaction was allowed to proceed for 50 minutes at 40°C in a Launder-O-meter, at which point the fabric was removed from solution and rinsed with water, then placed in a Launder-O-meter beaker containing 250 ml of a 0.04 M Tris buffer, 5 mM calcium chloride, pH 8.35 at 25°C.
  • a solution of SAVINASE ® 16.0L (200 ⁇ L) was added to the vessels, followed immediately by a solution of Phytophthora cactorum transglutaminase (containing 6 mg transglutaminase).
  • the vessels were placed in the Launder-O-meter and allowed to react for 40 minutes at 44°C, followed by a ten minute heating gradient up to 80°C, then held at that temperature for ten minutes to inactivate the enzyme.
  • the sample was removed from the solution, rinsed, dried, and measured, then subjected to five cycles of machine washing and drying, before being subjected to further property testing.
  • Wool swatches were subjected to a combined protease and transglutaminase treatment. The samples were thoroughly rinsed, wrung dry, then subjected to six machine wash/dry cycles, (two with cold wash and hot drying, four with warm wash and high heat drying), equilibrated in a constant temperature and humidity room, then tested.
  • Wool swatches were incubated individually in Launder-O- meter vessels in 250 mL buffer (40 mM Tris, pH 8.25 at 25°C) containing the specified amounts of Esperase 8.0L and Phytophthora cactorum transglutaminase solution (approximately 4% protein by weight in solution); for 40 minutes at 44°C, ramped up to 80°C over ten minutes, then held at 80°C for ten minutes.
  • Weight loss was measured after six wash-dry cycles. Shrinkage is measured after six machine wash/dry cycles. "Strength” is a measure of the dry burst strength of the wool fabric, with several tests per swatch.
  • transglutaminase is a cross-linking enzyme. It is critical to optimize the extent of cross-linking for every different set of reaction conditions, as too much cross-linking results in brittle, weak fibers. Thus, the optimized level of transglutaminase identified in this example is for a given transglutaminase, for use with the specified quantity of Esperase ® , at the specified temperature and time, with the specified wool. It is clear that changes in reaction conditions require changes in the optimal amount of transglutaminase (and obviously not all transglutaminases behave the same). Thus, we are unable to identify a universal preferred concentration ratio for all combination of proteases and transglutaminases under all possible reaction conditions.
  • Example 7 Weight loss, burst strength, whiteness and shrinkage of wool treated with Protease and Transglutaminase following a mild oxidative treatment
  • Wool swatches were subjected to a mild oxidative chlorination step using an acidified solution of sodium hypochlorite, then rinsed, wrung dry, and subjected to a combined protease and transglutaminase treatment.
  • the samples were thoroughly rinsed, wrung dry, subjected to five machine wash/dry cycles (warm wash, high heat drying), equilibrated in a constant temperature and humidity room, then tested.
  • Wool swatches were incubated in pairs in Launder-O-Meter vessels with 500 mL buffer (40 mM Tris, pH 8.30 at 25°C) containing 0.4 mL Savinase 16.0L and the indicated amount of Phytophthora cactorum transglutaminase solution (approximately 4% protein by weight in solution); for 40 minutes at 54°C, ramped up to 80°C over ten minutes, then held at 80°C for ten minutes.
  • buffer 40 mM Tris, pH 8.30 at 25°C
  • Savinase 16.0L the indicated amount of Phytophthora cactorum transglutaminase solution
  • treatment of wool with a selected combination of protease and transglutaminase gives superior shrink-resistance and whiteness relative to untreated or protease-treated wool, while conserving weight and strength losses relative to treatments with protease alone.

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  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Textile Engineering (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Or Physical Treatment Of Fibers (AREA)
  • Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)
  • Coloring (AREA)

Abstract

L'invention concerne un procédé de traitement de la laine, des fibres de laine et des pelages d'animaux par une enzyme protéolytique et une transglutaminase. Le procédé de l'invention permet d'obtenir une meilleure résistance au rétrécissement, une meilleure maniabilité, un meilleur aspect, une meilleure mouillabilité, une tendance au feutrage amoindrie, une blancheur plus prononcée, une réduction du boulochage, une douceur améliorée, une meilleure résistance à la traction, une meilleure élasticité, une meilleure résistance à l'éclatement, et de meilleures caractéristiques de teinture, notamment en termes d'absorption et de solidité au lavage de la teinture. En outre, par rapport aux traitements aux enzymes protéolytiques uniquement (sans transglutaminase), ledit procédé se caractérise par une perte de poids réduite, une détérioration des fibres réduite et une résistance accrue.
EP99922991A 1998-05-20 1999-05-12 Procede de traitement enzymatique de la laine Withdrawn EP1088128A1 (fr)

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US8221898A 1998-05-20 1998-05-20
US82218 1998-05-20
US161824 1998-09-28
US09/161,824 US6051033A (en) 1998-05-20 1998-09-28 Method for enzymatic treatment of wool
PCT/US1999/010496 WO1999060200A1 (fr) 1998-05-20 1999-05-12 Procede de traitement enzymatique de la laine

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DE19945486A1 (de) * 1999-09-22 2001-03-29 Henkel Kgaa Verfahren zur Färbung von keratinischen Fasern
DE19945487A1 (de) * 1999-09-22 2001-03-29 Henkel Kgaa Verfahren zur Restrukturierung keratinischer Fasern
GB0016914D0 (en) * 2000-07-10 2000-08-30 Univ Nottingham Trent A method for enzymatic treatment of wool
ATE390506T1 (de) * 2002-05-21 2008-04-15 Univ Do Minho Behandlung von tierischen haarfasern mit modifizierten proteasen
ES2223227B1 (es) 2002-05-31 2006-04-16 Consejo Sup. Investig. Cientificas Secuencia de nucleotidos de maiz codificante de una proteina con actividad transglutaminasa, y su uso.
FI119700B (fi) * 2002-12-16 2009-02-13 Suedwolle Gmbh & Co Kg Villan teollinen biotekninen viimeistysmenetelmä ja menetelmällä valmistettu villatekstiili
EP1657300A1 (fr) † 2004-11-10 2006-05-17 N-Zyme BioTec GmbH Boissons ayant un contenu réduit de prolamine et leur procédé de préparation
JP2009174111A (ja) * 2007-12-28 2009-08-06 Ist Corp 分枝状タンパク質繊維及びその製造方法、並びに綿状体、分枝状タンパク質繊維紡績糸、分枝状タンパク質繊維含有紡績糸、布帛、不織布
IT202000023929A1 (it) * 2020-10-12 2022-04-12 Alberto PESTELLI Metodo di finissaggio di un prodotto tessile laniero e relativo prodotto tessile
JP6889962B1 (ja) * 2021-01-07 2021-06-18 ミテジマ化学株式会社 獣毛の改質方法

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JPS58144105A (ja) * 1982-02-12 1983-08-27 Kurabo Ind Ltd スケ−ル除去獣毛繊維の製法
JPH03213574A (ja) * 1990-01-10 1991-09-18 Ajinomoto Co Inc 獣毛繊維の改質方法
JPH10511437A (ja) * 1994-12-21 1998-11-04 ノボ ノルディスク アクティーゼルスカブ ウールの酵素処理方法

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WO1999060200A1 (fr) 1999-11-25
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TR200003419T2 (tr) 2001-03-21
JP2002515555A (ja) 2002-05-28
WO1999060200A8 (fr) 2000-03-02

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