Classifications

• • 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
  • C12N9/14—Hydrolases (3)
  • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
  • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
  • C12N9/2405—Glucanases
  • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
  • C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
• • 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

Definitions

• the present invention relates to a method for desizing cel ⁇ lulose-containing textiles or fabric, and an enzyme composi ⁇ tion for use in the method.
• the threads are exposed to considerable mechanical strain.
• they are usually reinforced by coating (sizing) with a gelatinous substance (size) .
• the most common sizing agent is starch in native or modified form, yet other polymeric com ⁇ pounds such as polyvinylalcohol (PVA) , polyvinylpyrrolidone (PVP) , polyacrylic acid (PAA) or derivatives of cellulose (e.g. carboxymethylcellulose(CMC) , hydroxyethylcellulose, hydroxypropylcellulose or methylcellulose) may also be abun- dant in the size.
• PVA polyvinylalcohol
• PVP polyvinylpyrrolidone
• PAA polyacrylic acid
• derivatives of cellulose e.g. carboxymethylcellulose(CMC) , hydroxyethylcellulose, hydroxypropylcellulose or methylcellulose
• CMC carboxymethylcellulose
• hydroxyethylcellulose hydroxypropylcellulose or methylcellulose
• the threads are not able to absorb water or finishing agents or compositions (bleaching, dyeing, crease-proofing etc.) to a sufficient degree.
• a uni ⁇ form and durable finishing can thus be obtained only after removal of the size from the fabric, the so-called desizing.
• the desizing treatment may be carried out with a cellulolytic enzyme, either alone or in combination with other substances, optionally in combination with other enzymes, e.g. starch-degrading enzymes such as a ylases.
• a cellulolytic enzyme may, in case of sized fabric or textile containing cellulose or cel ⁇ lulose-derivatives, not only fully or partly degrade the size but also degrade the textile or fabric, thus resulting in a desized fabric or textile having a strength loss and/or a weight loss as compared to the strength or weight of the unsized textile or fabric.
• the object of the present invention is to provide a method for desizing cellulose-containing textile or fabric essen ⁇ tially without damaging the fabric, i.e. without inducing to the fabric a strength loss or a weight loss or both.
• the present invention provides a method for desizing cellulose-containing fabric or textile, wherein the fabric or textile is treated with a cellulolytic enzyme hav ⁇ ing an activity on carboxymethylcellulose (CMC) and a cata ⁇ lytic activity on cellotriose at pH 8.5 corresponding to k c , t of at least 0.01 per sec.
• CMC carboxymethylcellulose
• compositions for use in the method of the invention comprising a cellulolytic enzyme having an activity on carboxymethylcel ⁇ lulose (CMC) and a catalytic activity on cellotriose at pH 8.5 corresponding to k clt of at least 0.01 per sec. It is to be understood that the composition should not comprise any cellulase component capable of inducing fabric damage.
• deizing is intended to be understood in a con ⁇ ventional manner, i.e. the removal of size from the fabric.
• cellulolytic enzyme In the present specification and claims, the terms “cellulolytic enzyme”, “cellulase” and “cellulase component” are intended to mean an enzyme that hydrolyses cellulose.
• the cellulolytic enzyme, cellulase or cellulase component may be a component occurring in a cellulase system produced by a given microorganism, such a cellulase system mostly comprising several different cellulase enzyme components including those usually identified as e.g. cellobiohydrolases, exo-cellobiohydrolases, endo-/3-l,4- glucanases, 3-glucosidases.
• the cellulase component may be a single component, i.e.
• the host is preferably a heterologous host, but the host may under certain conditions also be the homologous host.
• the native or unmodified cellulase or cellulase component may be derived from microorganisms which are known to be capable of producing cellulolytic enzymes, e.g. species of Humicola, Thermomyce ⁇ , Bacillus, Tr ⁇ hoderma, Fu ⁇ arium, Myceliophthora, Phanerochaete , Irpex, Scytalidium, Schizo- phyllum, Penicillium, Aspergillus , and Geotricum .
• the derived component may be either homologous or heterologous component. Preferably, the component is homologous.
• the cellulolytic enzyme is obtainable by or derived from a strain selected from the group consisting of Humicola, Trichoderma, Myceliophthora, Penicillium, Irpex, Aspergillus, Scytalidium or Fusariu . More preferably, the enzyme is obtainable by or derivable from a strain of Humicola insolens , Fusarium oxysporum or Trichoderma reesei .
• the term "derivable” or “derived from” is intended not only to indicate a cellulase produced by a strain of the organism in question, but also a cellulase encoded by a DNA sequence isolated from such strain and produced in a host organism transformed with said DNA sequence. Furthermore, the term is intended to indicate a cellulase which is encoded by a DNA sequence of synthetic and/or cDNA origin and which has the identifying character ⁇ istics of the cellulase in question.
• the cellulolytic enzyme to be used in the method of the invention is a recombinant cellulase, i.e. a cellulase essentially free from other proteins or cellulase proteins.
• a recombinant cellulase component may be cloned and expressed according to standard techniques conventional to the skilled person.
• a parent cellulase of fungal origin may be used, e.g. a cellulase derivable from a strain of the fungal genus Humicola or Fusarium.
• the parent cellulase may be derivable from a strain of the fungal spe ⁇ cies H . insolens or F. oxysporum.
• Many of these cellulases are all well characterized and their entire a ino acid sequence are described.
• the parent cellulase is selected from the group consisting of a H . insolens, F . oxysporum and Trichoderma reesei cellulase, or is a functional analogue of any of said parent cellulases which
• i) comprises an amino acid sequence being at least 60% homologous with the amino acid sequence of the parent cellulase
• iii) is encoded by a DNA sequence which hybridizes with the same probe as a DNA sequence encoding the parent cellulase.
• Property i) of the analogue is intended to indicate the degree of identity between the analogue and the parent cellulase indicating a derivation of the first sequence from the second.
• a polypeptide is considered to be homologous to the parent cellulase if a comparison of the respective amino acid sequences reveals an identity of greater than about 60%, such as above 70%, 80%, 85%, 90% or even 95%. Sequence comparisons can be performed via known algorithms, such as the one described by Lipman and Pearson (1985) .
• the homologous cellulase may be a genetically engineered cellulase, e.g. prepared in order to improve one or more properties such as thermostability, acid/alkaline stability, temperature or pH optimum and the like.
• the additional properties ii) and iii) of the analogue of the parent cellulase may be determined as follows:
• Property ii) i.e. the immunological cross reactivity
• the antibody which may either be monoclonal or polyclonal, may be pro- prised by methods known in the art, e.g. as described by Hudson et al., 1989.
• the immunological cross-reactivity may be determined using assays known in the art, examples of which are Western Blotting or radial immunodiffusion assay, e.g. as described by Hudson et al., 1989.
• the oligonucleotide probe used in the characterization of the analogue in accordance with property iii) defined above may suitably be prepared on the basis of the full or partial nucleotide or amino acid sequence of the parent cellulase.
• the hybridization may be carried out under any suitable
• conditions allowing the DNA sequences to hybridize are hybridization under specified conditions, e.g. involving presoaking in 5xSSC and prehybri- dizing for lh at -40°C in a solution of 20% formamide, SxDenhardt's solution, 50mM sodium phosphate, pH 6.8, and
• cellulolytic enzyme useful according to the 20 invention are:
• An endoglucanase component which is immunoreactive with an antibody raised against a highly purified ⁇ 50kD endoglucanase derived from Humicola insolens , DSM 1800, or which is a homologue or derivative of the ⁇ 50kD endoglucanase exhibiting
• a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. W091/17244, Fig. 14A-E, which is shown in the appended SEQ ID NO:2, or a variant of said endoglucanase having an amino acid sequence being at least 60%, preferably at least
• the endoglucanase component is referred to as EG I; and an endoglucanase component which is immunoreactive with an antibody raised against a highly purified ⁇ 50kD (apparent molecular weight, the amino acid composition corresponds to 45kD with 2n glycosylation sites) endoglucanase derived from Fusarium oxysporum, DSM 2672, or which is a homologue or derivative of the ⁇ 50kD endoglucanase exhibiting cellulase activity.
• ⁇ 50kD apparent molecular weight, the amino acid composition corresponds to 45kD with 2n glycosylation sites
• a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No.
• EG I-F the endoglucanase component
• the EG I-F cellulase component is producible by Aspergillus oryzae after transformation with a plasmid containing the DNA sequence corresponding to the amino acid sequence of the appended SEQ ID NO:3 and using the conven ⁇ tional Taka promoter and AMG terminator.
• the EG I-F may be purified to homogeneity using cationic chromatography and has a pi >9.
• the calculated pi is 9 based on the amino acid composition using the PHKa values from Adv . Protein Chem . 17, p . 69-165 (1962) (C . Tanford) .
• the molar extinction coefficient is calculated to be 58180;
• NDI non-degrading index
• KSM-534, FERM BP 1508 alkaline cellulase K- 539 (produced by Bacillus sp. KSM-539, FERM BP 1509); alka- line cellulase K-577 (produced by Bacillus sp. KSM-577, FERM BP 1510) ; alkaline cellulase K-521 (produced by Bacillus sp. KSM-521, FERM BP 1507); alkaline cellulase K-580 (produced by Bacillus sp. KSM-580, FERM BP 1511) ; alkaline cellulase K-588 (produced by Bacillus sp.
• KSM-588, FERM BP 1513 alkaline cellulase K-597 (produced by Bacillus sp. KSM-597, FERM BP 1514) ; alkaline cellulase K-522 (produced by Bacil ⁇ lus sp. KSM-522, FERM BP 1512); CMCase I, CMCase II (both produced by Bacillus sp. KSM-635, FERM BP 1485); alkaline cellulase E-II and alkaline cellulase E-III (both produced by Bacillus sp. KSM-522, FERM BP 1512).
• cellulose-containing textile/fabric and "cellulosic textile/fabric” are intended to indicate any type of fabric, in particular woven fabric, prepared from a cellulose-containing material, containing cellulose or cellulose derivatives, e.g. from wood pulp, and cotton.
• the main part of the cellulose or cellulose derivatives present on the fabric is normally size with which the yarns, nor ⁇ mally warp yarns, have been coated prior to weaving.
• fabric is also intended to include garments and other types of processed fabrics.
• cellulosic fabric is cotton, viscose (rayon) ; lyocell; all blends of viscose, cotton or lyocell with other fibers such as polyester; viscose/cotton blends, lyocell/cotton blends, viscose/wool blends, lyocell/wool blends, cotton/wool blends; flax (linen) , ramie and other fabrics based on cellulose fibers, including all blends of cellulosic fibers with other fibers such as wool, polyamide, acrylic and polyester fibers, e.g. viscose/cotton/polyester blends, wool/cotton/polyester blends, flax/cotton blends etc.
• the method of the invention may be performed in accordance with any suitable desizing pro- cess known in the art, e.g. as described by Olson, E.S. (1983), and Peter, M. and Rouette H.K. (1988).
• the process conditions to be used in performing the present invention may be selected so as to match a particular equip ⁇ ment or a particular type of process which it is desirable to use.
• Preferred examples of process types to be used in connection with the present invention include Jigger/Winch, Pad-Roll and Pad-Steam types. These types are dealt with in further detail below.
• the method of the invention may be carried out as a batch, semi-continuous or continuous process.
• the method may comprise the following steps:
• the useful cellulase may conveniently be mixed with other components which are conventionally used in the desizing process.
• components are other enzymes, preferably such commer ⁇ cially available amylases which conventionally are used for desizing such as the microbial amylases, especially amylases producible by Bacillus , e.g. B . licheniformis, B . amyloliquefaciens, B . ⁇ ubtilis, B . stearothermophilu ⁇ , or Aspergillus ; or mutants thereof, e.g. as described in WO 91/00353 or WO 91/16423.
• amylases for desizing are Aquazym * , Aquazym Ultra, Dezyme * , Thermozyme TM and Termamyl * from Novo Nordisk A/S. Further preferred amylases are the oxidation-stable ⁇ -amylase mutants dis ⁇ closed in International Patent Application PCT/DK94/00371, which is hereby incorporated by reference.
• composition of the present invention it may be advantageous to incorporate an ⁇ -amylase having improved ocidation stability so as to make the composition useful in a combined desizing and bleaching process (performed in a single operation) , e.g. a process using sodium chlorite in combination with a strong base, a surfactant, an activator, an amylolytic enzyme and optionally a cellulolytic enzyme; or a process using sodium tetraborate dexahydrate as a buffer in a bath containing hydrogen peroxide, a sequester ⁇ ing agent, a surfactant, an amylolytic enzyme and optionally a cellulolytic enzyme.
• a process using sodium chlorite in combination with a strong base, a surfactant, an activator, an amylolytic enzyme and optionally a cellulolytic enzyme or a process using sodium tetraborate dexahydrate as a buffer in a bath containing hydrogen peroxide, a sequester ⁇ ing agent,
• Such components include a stabilizer and a wetting agent.
• the stabilizer may be an agent stabilizing the cellulolytic enzyme.
• the wetting agent serves to improve the wettability of the fibre whereby a rapid and even desizing may be obtained.
• the wetting agent is preferably of an oxidation stable type.
• the useful cellulase is used in an amount exceeding 1 g/1, preferably in an amount of 1-20 g/1, such as 1-10 g/1, 1-5 g/1 or 1-3 g/1, corresponding to a cellulase activity in the range of between 10 and 5000 ECU per litre of desizing liquor, preferably between 50 and 500 ECU per litre of desizing liquor. It will be understood that the amount of cellulase to be used depend on the formulation of the cellulase product in question.
• the method of the inven ⁇ tion is normally performed at a temperature in the range of 30-100°C, such as 35-60°C, and a pH in the range of 3-11, preferably 7-9.
• a temperature in the range of 30-100°C such as 35-60°C
• a pH in the range of 3-11 preferably 7-9.
• the actual process conditions may vary widely within these ranges as will be apparent from the following disclosure.
• Preferred examples of the process conditions to be used in connection with the present invention include:
• a batch type process e.g. of the Jigger/Winch type, using 1-5 g/1 of a useful cellulase, and 0.25-5 g/1 of a wetting agent, e.g. the commercial product Arbyl R available from Gr ⁇ nau, Germany, the process being performed at a pH in the range of 7-9 (obtained by addition of NaOH) and a tempera ⁇ ture in the range of 40-55°C, typically for 1-2 hours.
• a wetting agent e.g. the commercial product Arbyl R available from Gr ⁇ nau, Germany
• a semi-continuous process e.g. of the Pad-Roll type, using 1-5 g/1 of a useful cellulase, 0.25-5 g/1 of a wetting agent, e.g. Arbyl R, the process being performed at a pH in the range of 7-9 (possibly obtained by addition of NaOH) and a temperature in the range of 30-50°C, typically for 12-24 hours.
• a wetting agent e.g. Arbyl R
• the method may be performed in any equipment sufficiently tolerant towards the conditions of the method.
• this cellulase should preferably be one which is active at a pH of above 3, such as above about pH 7.
• the cellulase has a high activity in the pH range of 7- 9.
• the method of the invention may be used prior to or after another desizing treatment step which may supplement the cellulase treatment, the supplementing treatment preferably being an enzymatic desizing treatment with an amylase.
• the useful cellulase may be added as such it is preferred that it is formulated into a suitable desizing composition preferably further comprising other desizing enzymes, e.g. amylases as described above.
• the desizing composition of the invention may be a mixture of each enzyme in the form of a granulate, preferably a non- dusting granulate, a liquid, in particular a stabilized liquid, a slurry, or in a protected form.
• Dust free granu ⁇ lates may be produced, e.g. as disclosed in US 4,106,991 and US 4,661,452 (both to Novo Nordisk A/S) and may optionally be coated by methods known in the art.
• Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as e.g. propylene glycol, a sugar or sugar alcohol or acetic acid, according to established methods. Other enzyme stabilizers are well known in the art. Protected enzymes may be prepared according to the method disclosed in EP 238 216.
• a polyol such as e.g. propylene glycol, a sugar or sugar alcohol or acetic acid
• composition of the invention comprising a cellulolytic enzyme having an activity on carboxymethylcel ⁇ lulose (CMC) and a catalytic activity on cellotriose at pH 8.5 corresponding to k clt of at least 0.01 per sec. and optionally an amylase may contain any other agent to be used in the combined process of the invention.
• CMC carboxymethylcel ⁇ lulose
• an amylase may contain any other agent to be used in the combined process of the invention.
• the composition is free from a bleaching agent and other highly oxidizing agents.
• composition of the invention may comprise one or more further components selected from the group consisting of wetting agents, dispersing agents, sequestering agents and emulsifying agents.
• wetting agents examples include water, dispersing agents, sequestering agents and emulsifying agents.
• suitable wetting agents are disclosed above.
• the emulsifying agent serves to emulsify hydrophobic impurities present on the fabric.
• the dispersing agent serves to prevent that extracted impurities redeposit on the fabric.
• the sequestering agent serve to remove ions such as Ca, Mg and Fe, which may have a negative impact on the process and preferred examples include caustic soda (sodium hydroxide) and soda ash (sodium carbonate) .
• the cellulase activity on cellotriose in terms of k ⁇ , (s" 1 ) , may be determined by a coupled assay:
• the GOD-Perid Test Kit (available from Boehringer Mannheim, art. 124 036) was used.
• the buffer-enzyme solution in the test kit was dissolved in 500 ml milli Q water. pH of the solution was adjusted to 8.5 (NaOH).
• 80 mg of ABTS R (available from Boehringer Mannheim, art. 756 407) was dissolved in 10 ml GOD-Perid corresponding to a total concentration of ABTS R of 10 mg/ l.
• a substrate stock solution of 5 mmole (2.52 mg/ml) of cello- triose (available from Merck art. 24741) in water was pre ⁇ pared. Diluted solutions in water corresponding to 1000 ⁇ - mole, 500 ⁇ mole, 376 ⁇ mole, 250 ⁇ mole, lOO ⁇ mole and 60 ⁇ mole were prepared.
• the reaction mixture was prepared by mixing 1 part of sub- strate solution with 1 part of GOD-Perid.
• a solution of the cellulase enzyme to be determined in a concentration of 1.0 - 3.0 ⁇ mole was prepared.
• the measurements were carried out on a HP 8452A Diode Array Spectrophotometer thermostated at 40°C, 1 cm cuvette, at a wavelength of 418 nm. The reaction was followed by measuring the oxidation of ABTS every 20 sec for 600 sec in total.
• the cellulolytic activity of endoglucanase is determined relative to an analytical standard and may be expressed in the unit ECU.
• Cellulolytic enzymes hydrolyse CMC, thereby decreasing the viscosity of the incubation mixture.
• the resulting reduction in viscosity may be determined by a vibration viscosimeter (e.g. MIVI 3000 from Sofraser, France) .
• Determination of the cellulolytic activity may be determined according to the analysis method AF 301.1 which is available from the Applicant upon request.
• the ECU assay quantifies the amount of catalytic activity present in the sample by measuring the ability of the sample to reduce the viscosity of a solution of carboxy-methylcel- lulose (CMC).
• CMC carboxy-methylcel- lulose
• the assay is carried out at 40°C, pH 7.5 using a relative enzyme standard for reducing the viscosity of the CMC substrate.
• Liquor volume 140 ml (LQR 1:20)
• Weight loss is defined as follows:
• Size compositions made up of pure carboxymethylcellulose (CMC) or that are very rich in CMC will usually tend to be largely soluble in water, i.e. the main part of a CMC size may be dissolved rapidly just by contacting the sized fabric with an aquous solution. Still, a minor part of the CMC-size will stick strongly to the fabric and give the fabric a very stiff hand. This stiffness will make the fabric unsuitable for further finishing.
• CMC carboxymethylcellulose
• the fabric used in these experiments was a 100% cotton interlock jersey.
• the fabric had prior to the desizing experiments been sized with either pure CMC (Blanose 7LFD available from Aqualon GmbH, Germany) or a mixed size made up of 1:1 (w/w) blend of CMC (Blanose 7LFD available from Aqualon GmbH, Germany) and carboxymethylated starch (CMS, Solvitose C5 available from Lamberti S.p.a., Italy).
• the amount of size on the fabric was approximately 6.5% (on weigth of the fabric) for the CMC-size , and approximately 5.6% (on weight of the fabric) for the CMC/CMS-size.
• the fabrics were cut into swatches of 12cm x 14cm (weigth of approximately 3.54 g/swatch without size).
• the swatches were weighed after climatization and then incu ⁇ bated for 30 mins in 250 ml glass beakers containing 200 ml 2g/l K-phoshate buffer pH 7.0 at 50°C including enzyme according the table below:
• Cellulase EG I from H . insolen ⁇ (as in example 1) .
• Amylase Aquazym 120L (activity: 120 KNU/g) , bacterial amylase commercially available from Novo Nordisk A/S.
• the cellulase do in both cases - with CMC- size and CMC/CMS-size, respectively - facilitate the size removal.
• CMC-size a large removal is seen also when the swatches are incubated in buffer without cellulase, yet from the fabric handle it was obvious that the remaining CMC (about 20 mg/swatch) had a pronounced effect on the fabric stiffness.
• Note 1 was given to the stiffest fabrics and Note 4 to the softest (best desizing result) .

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• 1995
  • 1995-08-10 TR TR95/00988A patent/TR199500988A2/xx unknown
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  • 1995-08-14 MX MX9701113A patent/MX9701113A/es not_active Application Discontinuation
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  • 1995-08-14 EP EP95927659A patent/EP0777779A1/en not_active Withdrawn
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