WO2015039962A1 - Blanchiment enzymatique de pulpe de papier - Google Patents

Blanchiment enzymatique de pulpe de papier Download PDF

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Publication number
WO2015039962A1
WO2015039962A1 PCT/EP2014/069474 EP2014069474W WO2015039962A1 WO 2015039962 A1 WO2015039962 A1 WO 2015039962A1 EP 2014069474 W EP2014069474 W EP 2014069474W WO 2015039962 A1 WO2015039962 A1 WO 2015039962A1
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Prior art keywords
pulp
enzyme
identity
amino acid
acid sequence
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PCT/EP2014/069474
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English (en)
Inventor
Bjoern Lennart Pierre Alexander Cassland
Henrik Lund
Christiane LIERS
René ULLRICH
Marek Jan Pecyna
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Novozymes A/S
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Priority to US15/023,252 priority Critical patent/US20160237618A1/en
Priority to EP14766688.7A priority patent/EP3047065A1/fr
Publication of WO2015039962A1 publication Critical patent/WO2015039962A1/fr

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Classifications

    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005—Treatment of cellulose-containing material with microorganisms or enzymes
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor
    • D21C9/1063—Bleaching ; Apparatus therefor with compounds not otherwise provided for, e.g. activated gases
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor
    • D21C9/1026—Other features in bleaching processes
    • D21C9/1036—Use of compounds accelerating or improving the efficiency of the processes
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor
    • D21C9/12—Bleaching ; Apparatus therefor with halogens or halogen-containing compounds
    • D21C9/123—Bleaching ; Apparatus therefor with halogens or halogen-containing compounds with Cl2O
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor
    • D21C9/12—Bleaching ; Apparatus therefor with halogens or halogen-containing compounds
    • D21C9/14—Bleaching ; Apparatus therefor with halogens or halogen-containing compounds with ClO2 or chlorites
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor
    • D21C9/16—Bleaching ; Apparatus therefor with per compounds
    • D21C9/163—Bleaching ; Apparatus therefor with per compounds with peroxides

Definitions

  • the present invention relates to bleaching of pulp with a GH78 enzyme.
  • enzymes in the manufacture of paper materials.
  • examples of enzymes used for this purpose are proteases, lipases, xylanases, amylases, cellulases, as well as various oxidizing enzymes such as laccases and peroxidases.
  • the present invention provides a method for increasing the brightness and/or decreasing the kappa number of a paper pulp, comprising contacting the paper pulp with a GH78 enzyme.
  • the invention relates to a method for increasing the brightness and/or decreasing the kappa number of a paper pulp, comprising contacting the paper pulp with a GH78 enzyme, wherein the GH78 enzyme
  • glycoside hydrolase family 78 belongs to glycoside hydrolase family 78 and/or,
  • c) consists or comprises an amino acid sequence with at least 60% identity to the amino acid sequence of SEQ ID NO: 1 .
  • the invention in another aspect relates to a bleaching composition, comprising a paper pulp and a GH78 enzyme, wherein the GH78 enzyme
  • glycoside hydrolase family 78 belongs to glycoside hydrolase family 78 and/or
  • c) consists or comprises an amino acid sequence with at least 60% identity to the amino acid sequence of SEQ ID NO: 1 .
  • An additional aspect of the invention relates to use of a GH78 enzyme for bleaching and/or decreasing the kappa number of a paper pulp, wherein the GH78 enzyme a) belongs to glycoside hydrolase family 78 and/or
  • c) consists or comprises an amino acid sequence with at least 60% identity to the amino acid sequence of SEQ ID NO: 1 .
  • lignocellulosic materials e.g. pulp and the resulting paper material
  • a GH78 enzyme e.g. a GH78 enzyme
  • paper material refers to products, which can be made out of pulp, such as paper, linerboard, corrugated paperboard, tissue, towels, packaging materials, corrugated containers or boxes.
  • pulp or "paper pulp” means any pulp which can be used for the production of a paper material.
  • the pulp can be supplied as a virgin pulp, or can be derived from a recycled source.
  • the pulp may be a wood pulp, a non-wood pulp or a pulp made from waste paper.
  • a wood pulp may be made from softwood such as pine, redwood, fir, spruce, cedar and hemlock or from hardwood such as maple, alder, birch, hickory, beech, aspen, acacia and eucalyptus.
  • a non-wood pulp may be made, e.g., from flax, hemp, bagasse, bamboo, cotton or kenaf.
  • a waste paper pulp may be made by re-pulping waste paper such as newspaper, mixed office waste, computer print-out, white ledger, magazines, milk cartons, paper cups etc.
  • the pulp to be treated comprises both hardwood pulp and softwood pulp.
  • the wood pulp to be treated may be mechanical pulp (such as ground wood pulp, GP), chemical pulp (such as kraft pulp or sulfite pulp), semichemical pulp (SCP), thermomechanical pulp (TMP), chemithermomechanical pulp (CTMP), or bleached chemithermomechanical pulp (BCTMP).
  • mechanical pulp such as ground wood pulp, GP
  • chemical pulp such as kraft pulp or sulfite pulp
  • SCP semichemical pulp
  • TMP thermomechanical pulp
  • CMP chemithermomechanical pulp
  • BCTMP bleached chemithermomechanical pulp
  • TMP thermomechanical pulp
  • GW groundwood pulp
  • PGW pressurized groundwood pulp
  • RMP refiner mechanical pulp
  • PRMP pressurized refiner mechanical pulp
  • CTMP chemithermomechanical pulp.
  • Chemical pulp is manufactured by alkaline cooking whereby most of the lignin and hemicellulose components are removed.
  • kraft pulping or sulphate cooking sodium sulphide or sodium hydroxide are used as principal cooking chemicals.
  • the kraft pulp to be treated may be a bleached kraft pulp, which may consist of softwood bleached kraft (SWBK, also called NBKP (Nadel Holz Bleached Kraft Pulp)), hardwood bleached kraft (HWBK, also called LBKP (Laub Holz Bleached Kraft Pulp)) or a mixture of these.
  • SWBK softwood bleached kraft
  • HWBK also called LBKP (Laub Holz Bleached Kraft Pulp)
  • the pulp to be used in the process of the invention is a suspension of mechanical or chemical pulp or a combination thereof.
  • the pulp to be used in the process of the invention may comprise 0%, 10-20%, 20-30%, 30-40%, 40-50%, 50-60%, 60-70%, 70-80%, 80-90%, or 90-100% of chemical pulp.
  • a chemical pulp forms part of the pulp being used for manufacturing the paper material.
  • the expression "forms part of means that in the pulp to be used in the process of the invention, the percentage of chemical pulp lies within the range of 1 -99%.
  • the percentage of chemical pulp lies within the range of 2-98%, 3-97%, 4-96%, 5-95%, 6-94%, 7- 93%, 8-92%, 9-91 %, 10-90%, 15-85%, 20-80%, 25-75%, 30-70%, 40-60%, or 45-55%.
  • the chemical pulp is a kraft pulp, a sulfite pulp, a semichemical pulp (SCP), a thermomechanical pulp (TMP), a chemithermomechanical pulp (CTMP), a bleached chemithermomechanical pulp (BCTMP).
  • the kraft pulp is bleached kraft pulp, for example softwood bleached kraft (SWBK, also called NBKP (Nadel Holz Bleached Kraft Pulp)), hardwood bleached kraft (HWBK, also called LBKP (Laub Holz Bleached Kraft Pulp and)) or a mixture thereof.
  • a GH78 enzyme is a glycoside hydrolase exhibiting esterase and rhamnosidase activities; preferably exhibiting feruloyi esterase (EC 3.1 .1 .73) and oL-rhamnosidase (EC 3.2.1.40) activities.
  • the GH78 enzyme belongs to the glycoside hydrolase family 78, as defined by the CAZy classification (Henrissat B, Davies GJ (1997), Structural and sequence-based classification of glycoside hydrolases, Current Opinion in Structural Biology, 7:637-644).
  • the GH78 enzyme is derived from a Xylaria sp., preferably Xylaria polymorpha.
  • "derived from”, as in, e.g., "derived from Xylaria polymorpha” means a wild-type alpha-amylase enzyme and variants thereof. Such enzymes can also be prepared synthetically, as is well-known in the art.
  • the amino acid sequence of the GH78 enzyme has at least 60% identity, preferably at least 65% identity, more preferably at least 70% identity, more preferably at least 75% identity, more preferably at least 80% identity, more preferably at least 85% identity, more preferably at least 90% identity, more preferably at least 95%, 96%, 97%, 98%, 99%, and most preferably 100% identity to the amino acid sequence of SEQ ID NO: 1 , or to the amino acid sequence of a Xylaria sp. (preferably Xylaria polymorpha) GH78 enzyme.
  • the number of amino acid substitutions, deletions and/or insertions introduced into the mature GH78 polypeptide of SEQ ID NO: 1 is up to 10, e.g., 1 , 2, 3, 4, 5, 6, 7, 8, 9, or 10; or up to 5, e.g., 1 , 2, 3, 4, or 5.
  • the amino acid sequence of the GH78 enzyme has one or several substitutions, deletions or insertions compared to SEQ ID NO: 1.
  • the amino acid sequence of the GH78 enzyme is identical to SEQ ID NO: 1 .
  • amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, typically of 1 -30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue; a small linker peptide of up to 20- 25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding domain.
  • conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine).
  • Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H.
  • substitutions are Ala/Ser, Val/lle, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/lle, LeuA al, Ala/Glu, and Asp/Gly.
  • Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081 -1085). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resultant mutant molecules are tested for GH78 enzyme activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271 : 4699-4708.
  • the active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver ei a/., 1992, FEBS Lett. 309: 59-64.
  • the identity of essential amino acids can also be inferred from an alignment with a related polypeptide.
  • Single or multiple amino acid substitutions, deletions, and/or insertions can be made and tested using known methods of mutagenesis, recombination, and/or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241 : 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95/17413; or WO 95/22625.
  • Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991 , Biochemistry 30: 10832-10837; U.S. Patent No. 5,223,409; WO 92/06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner ei a/., 1988, DNA 7: 127).
  • sequence identity For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the Needle program of the Needle program
  • EMBOSS The European Molecular Biology Open Software Suite, Rice et a/., 2000, Trends Genet. 16: 276-277
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled "longest identity" is used as the percent identity and is calculated as follows: (Identical Residues x 100)/(Length of Alignment - Total Number of Gaps in Alignment).
  • the concentration of the GH78 enzyme is typically in the range of 0.01 -100 ppm enzyme protein, preferably 0.05-50 ppm enzyme protein, more preferably 0.1 -50 ppm enzyme protein, more preferably 0.1 -30 ppm enzyme protein, more preferably 0.5-20 ppm enzyme protein, and most preferably 0.5-10 ppm enzyme protein.
  • the concentration of the GH78 enzyme is typically in the range of 1 - 40 ppm enzyme protein, preferably 1 -20 ppm enzyme protein, more preferably 1 -10 ppm enzyme protein.
  • Feruloyl esterase (EC 3.1.1.73) activity
  • Feruloyl esterase activity is determined by hydrolytic demethylation of 1 mM methyl ferulate to ferulic acid in 100 mM MOPS buffer at pH 6.0. The reaction is initiated by the incubation of reaction mixtures at 37°C for a suitable time depending on enzyme sample (10- 30 min) and then terminated by an equal volume of acetic acid/acetonitrile (1 1 .3% v/v) as stop solution (see also Faulds & Williamson (1994), Microbiology, vol.140, pp.779-787).
  • the released ferulic acid is analyzed by HPLC using a reversed phase C18-column (Synergi Fusion-RP 80A, 4.6 mm x 125 mm, Phenomenex®,
  • a-L-rhamnosidase activity is measured using p-nitrophenyl a-L-rhamnopyranoside NPRP) as substrate (see also Gallego et al. (2001 ), J. Food Sci., vol. 66, pp. 204-209).
  • the assay is performed in a 48-well microtiter plate containing 160 ⁇ of the substrate (2.5 mM p-NPRP in 50 mM sodium acetate buffer, pH 5.0) and 40 ⁇ of enzyme sample.
  • the reaction is performed for 5-20 min at 40°C and stopped by adding 100 ⁇ of 1 M Na 2 C0 3 .
  • Bleaching is defined as a process aimed at removal of colour in pulps derived from residual lignin or other colored impurities. Native wood is only slightly colored, whereas residual lignin of a chemical pulp after cooking is highly colored. Traditional concepts for bleaching of pulp include chlorine and oxygen based oxidants which selectively remove chromophore structures present in the pulp. The progress in bleaching is followed by measuring the brightness, which is defined as the reflectance of visible blue light from a pad of pulp sheets using a defined spectral band of light having an effective wavelength of 457 nm. Official ISO standard methods are ISO 2469 or ISO 2470. Bleaching to full brightness (> 88% ISO) requires multi-stage application of bleaching chemicals.
  • the first stages in a bleaching sequence are often conceived as delignification, where the majority of residual lignin is removed.
  • the latter stages are often referred to brightening stages, in which the chromophores in the pulps are eliminated to attain a high brightness level.
  • the brightness of the pulp is determined according to TAPPI test method T 452 om-98.
  • the Kappa number is an indication of the residual lignin content or bleachability of pulp by a standardized analysis method.
  • the Kappa number is determined by ISO 302, which is applicable to all kinds of chemical and semi-chemical pulps and gives a Kappa number in the range of 1 -100.
  • the kappa number of the pulp is determined according to TAPPI test method T 236 om-06.
  • the process of the invention is particularly applicable to the bleaching of pulp in a process for making paper material.
  • the process according to the invention can be carried out at any pulp production stage.
  • the enzyme can be added to any holding tank, e.g. to a pulp storing container (storage chest), storage tower, mixing chest or metering chest.
  • the enzyme treatment can be performed before the bleaching of pulp, in connection with the pulp bleaching process or after the bleaching.
  • the enzyme preparation may be added together with bleaching chemicals such as chlorine or chlorine dioxide. Applying oxygen gas, hydrogen peroxide or ozone or combinations thereof may also carry out the bleaching of pulp.
  • the enzyme preparation may also be added together with these substances. Preferably the enzyme preparation is added prior to such bleaching steps.
  • the enzyme can also be added to the circulated process water (white water) originating from bleaching and process water (brown water) originating from the mechanical or chemimechanical pulping process. In a particular embodiment of a kraft pulping process, the enzyme is added during the brown-stock washing.
  • the term "process water” comprises inter alia 1 ) water added as a raw material to the paper manufacturing process; 2) intermediate water products resulting from any step of the process for manufacturing the paper material; as well as 3) waste water as an output or by-product of the process.
  • the process water is, has been, is being, or is intended for being circulated (re-circulated), i.e., re-used in another step of the process.
  • the term "water” in turn means any aqueous medium, solution, suspension, e.g. ordinary tap water, and tap water in admixture with various additives and adjuvants commonly used in paper manufacturing processes.
  • the process water has a low content of solid (dry) matter, e.g. below 20%, 18%, 16%, 14%, 12%, 10%, 8%, 7%, 6%, 5%, 4%, 3%, 20% or below 1 % dry matter.
  • the process of the invention may be carried out at conventional conditions in the paper and pulp processing.
  • the process conditions will be a function of the enzyme(s) applied, the reaction time and the conditions given.
  • the enzyme of the invention should be added in an effective amount.
  • effective amount is meant the amount sufficient to achieve the desired and expected effect, such as oxidizing pitch components, obtaining a desired bleaching and/or de-inking etc.
  • the dosage of the GH78 enzyme and additional enzymes, if any, is from about 0.1 mg enzyme protein to about 100,000 mg enzyme protein (of each enzyme) per ton of paper pulp.
  • the amount of the GH78 enzyme and additional enzymes, if any, is in the range of 0.00001 -20; or 0.0001 -20 mg of enzyme (calculated as pure enzyme protein) per gram (dry weight) of pulp material, such as 0.0001 -10 mg/g, 0.0001 -1 mg/g, 0.001 -1 mg/g, 0.001 -0.1 , or 0.01 -0.1 mg of enzyme per gram of pulp material. Again, these amounts refer to the amount of each enzyme.
  • the enzymatic treatment can be done at conventional consistency, e.g. 0.5-10% dry substance.
  • the consistency is within the range of 0.5-45%; 0.5-
  • the enzymatic treatment may be carried out at a temperature of from about 10°C to about 100°C. Further examples of temperature ranges (all "from about” and “to about”) are the following: 20-120°C, 30-120°C, 35-120°C, 37-120°C, 40-120°C, 50-120°C, 60-120°C, 70- 120°C, 10-100°C, 10-90°C, 10-80°C, 10-70°C, 10-60°C, and 30-60°C, as well as any combination of the upper and lower values here indicated.
  • a typical temperature is from about 20 to 90°C, or 20 to 95°C, preferably from about 40 to 70°C, or 40 to 75°C.
  • the enzymatic treatment is carried out at atmospheric pressure. But when the temperature exceeds 100°C, the treatment is carried out at a pressure of 1 -2 bar (up to 1 bar above atmospheric pressure).
  • the enzymatic treatment is carried out at a pH of from about 2 to about 7, preferably at a pH from about 2.5 to about 6, more preferably at a pH from about 3 to about 5.5, and most preferably at a pH from about 3.5 to about 5.
  • a suitable duration of the enzymatic treatment may be in the range from a few seconds to several hours, e.g. from about 30 seconds to about 48 hours, or from about 1 minute to about 24 hours, or from about 1 minute to about 18 hours, or from about 1 minute to about 12 hours, or from about 1 minute to 5 hours, or from about 1 minute to about 2 hours, or from about 1 minute to about 1 hour, or from about 1 minute to about 30 minutes.
  • a typical reaction time is from about 10 minutes to 3 hours, 10 minutes to 10 hours, preferably 15 minutes to 1 hour, or 15 minutes to 2 hours.
  • reaction may conveniently be carried out in an open reactor, i.e. at atmospheric pressure.
  • Surfactants and/or dispersants are often present in, and/or added to a pulp.
  • the process and use of the present invention may be carried out in the presence of an anionic, non-ionic, cationic and/or zwitterionic surfactant and/or dispersant conventionally used in a pulp.
  • anionic surfactants are carboxylates, sulphates, sulphonates or phosphates of alkyl, substituted alkyl or aryl.
  • non-ionic surfactants are polyoxyethylene compounds, such as alcohol ethoxylates, propoxylates or mixed ethoxy-/propoxylates, poly-glycerols and other polyols, as well as certain block-copolymers.
  • cationic surfactants are water-soluble cationic polymers, such as quartenary ammonium sulphates and certain amines, e.g.
  • EPI-DMA epichlorohydrin/dimethylamine polymers
  • DADMAC polydiallyl dimethyl ammonium chloride
  • ADMAC DADMAC/Acrylamide co-polymers
  • ionene polymers such as those disclosed in US patents nos. 5,681 ,862; and 5,575,993.
  • zwitterionic or amphoteric surfactants are betains, glycinates, amino propionates, imino propionates and various imidazolin-derivatives. Also the polymers disclosed in US patent no. 5,256,252 may be used.
  • surfactants such as the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any one of the above, including any
  • each surfactant in such composition may amount to from about 1 to about 1000 ppm of the composition.
  • the amount of each surfactant is from about 10 to about 1000 ppm, or from about 10 to about 500 ppm, or from about 50 to about 500 ppm.
  • each of the above ranges refers to the total amount of surfactants.
  • the GH78 enzyme is used in an amount of 0.005-50 ppm (mg/L), or 0.01 -40, 0.02- 30, 0.03-25, 0.04-20, 0.05-15, 0.05-10, 0.05-5, 0.05-1 , 0.05-0.8, 0.05-0.6, or 0.1 -0.5 ppm.
  • the amount of enzyme refers to mg of a well-defined enzyme preparation.
  • the GH78 enzyme may be applied alone or together with an additional enzyme.
  • an additional enzyme means at least one additional enzyme, e.g. one, two, three, four, five, six, seven, eight, nine, ten or even more additional enzymes.
  • the term “applied together with” means that the additional enzyme may be applied in the same, or in another step of the process of the invention.
  • the other process step may be upstream or downstream in the paper manufacturing process, as compared to the step in which the pulp is bleached with a GH78 enzyme.
  • the additional enzyme is an enzyme which has protease, lipase, xylanase, cutinase, oxidoreductase, cellulase, endoglucanase, amylase, mannanase, steryl esterase, and/or cholesterol esterase activity.
  • oxidoreductase enzymes are enzymes with laccase, and/or peroxidase activity.
  • the additional enzyme is lipase.
  • a step of a process means at least one step, and it could be one, two, three, four, five or even more process steps.
  • the GH78 enzyme may be applied in at least one process step, and the additional enzyme(s) may also be applied in at least one process step, which may be the same or a different process step as compared to the step where the GH78 enzyme is used.
  • the term "enzyme preparation” means a product containing at least one GH78 enzyme.
  • the enzyme preparation may also comprise enzymes having other enzyme activities, preferably lipolytic enzymes.
  • such a preparation preferably contains at least one adjuvant.
  • adjuvants which are used in enzyme preparations for the paper and pulp industry are buffers, polymers, surfactants and stabilizing agents.
  • the process of the invention also includes an alkaline peroxide bleaching stage (E stage and/or P stage), such as described by Camarero, S. et al., Enzyme and Microbial Technology, 35 (2004), pp. 1 13-120 (see in particular paragraph 2.4).
  • the alkaline peroxide bleaching is carried out after the enzymatic bleaching method of the invention.
  • Typical conditions for an alkaline peroxide bleaching stage are initial pH values in the range of 10-1 1 and end pH above 8.5; temperatures typical ranges from 70-90°C and peroxide charges from 0.5-1 % for 1 .5 hours.
  • Peroxide stabilizer may be added and metal management may be handled in previous stage or simultaneously with peroxide bleaching. Additional enzymes
  • Any enzyme having protease, lipase, xylanase, cutinase, oxidoreductase, cellulose, endoglucanase, amylase, mannanase, steryl esterase, and/or cholesterol esterase activity can be used as additional enzymes in the use and process of the invention. Below some non- limiting examples are listed of such additional enzymes.
  • the enzymes written in capitals are commercial enzymes available from Novozymes A S, Krogshoejvej 36, DK-2880 Bagsvaerd, Denmark. The activity of any of those additional enzymes can be analyzed using any method known in the art for the enzyme in question, including the methods mentioned in the
  • cutinases are those derived from Humicola insolens (US 5,827,719); from a strain of Fusarium, e.g. F. roseum culmorum, or particularly F. solani pisi (WO 90/09446; WO
  • the cutinase may also be derived from a strain of R izoctonia, e.g.
  • R. solani or a strain of Alternaria, e.g. A. brassicicola (WO 94/03578), or variants thereof such as those described in WO 00/34450, or WO 01/92502.
  • proteases examples include the ALCALASE, ESPERASE, SAVINASE, NEUTRASE and DURAZYM proteases.
  • Other proteases are derived from Nocardiopsis, Aspergillus, Rhizopus,
  • amylases are the BAN, AQUAZYM, TERMAMYL, and AQUAZYM Ultra amylases.
  • An example of a lipase is the RESINASE A2X lipase.
  • An example of a xylanase is the PULPZYME HC hemicellulase.
  • Examples of endoglucanases are the NOVOZYM 613, 342, and 476 enzyme products.
  • mannanases are the Trichoderma reesei endo-beta-mannanases described in Stahlbrand et al, J. Biotechnol. 29 (1993), 229-242.
  • oxidoreductases examples include the peroxidases and laccases disclosed in EP 730641 ; WO 01/98469; EP 719337; EP 765394; EP 767836; EP 7631 15; and EP 788547.
  • acceptors e.g. oxygen or hydrogenperoxide
  • enhancers e.g. enhancers, mediators and/or activators
  • enhancers and mediators are disclosed in EP 705327; WO 98/56899; EP 677102; EP 781328; and EP 707637. If desired a distinction could be made by defining an oxidoreductase enzyme system (e.g. a laccase, or a peroxidase enzyme system) as the combination of the enzyme in question and its acceptor, and optionally also an enhancer and/or mediator for the enzyme in question.
  • an oxidoreductase enzyme system e.g. a laccase, or a peroxidase enzyme system
  • compositions are compositions, methods and uses
  • the invention provides a method for increasing the brightness and/or decreasing the kappa number of a paper pulp, comprising contacting the paper pulp with a GH78 enzyme.
  • GH78 enzymes are described above.
  • the GH78 enzyme belongs to the glycoside hydrolase family 78, and exhibits esterase (feruloyl esterase) and rhamnosidase (a-L-rhamnosidase) activities.
  • esterase feruloyl esterase
  • rhamnosidase a-L-rhamnosidase
  • the amino acid sequence of the GH78 enzyme may have at least 60% identity, preferably at least 65% identity, more preferably at least 70% identity, more preferably at least 75% identity, more preferably at least 80% identity, more preferably at least 85% identity, more preferably at least 90% identity, more preferably at least 95%, 96%, 97%, 98%, 99%, and most preferably 100% identity to the amino acid sequence of SEQ ID NO: 1 .
  • the number of amino acid substitutions, deletions and/or insertions introduced into the mature polypeptide of SEQ ID NO: 1 is up to 10, e.g., 1 , 2, 3, 4, 5, 6, 7, 8, 9, or 10; or up to 5, e.g., 1 , 2, 3, 4, or 5.
  • the GH78 enzyme is derived from a Xylaria sp., such as Xylaria polymorph a.
  • the pulp is wood pulp.
  • the pulp is a chemical pulp, such as kraft pulp.
  • the method of the invention further comprises a step of chlorine dioxide treatment (D stage) and/or alkaline peroxide treatment (E stage).
  • the method of the invention further comprises contacting the pulp with one or more additional enzyme(s), such as a lipase.
  • the method of the invention further comprises a final step of preparing a paper material from the pulp.
  • the invention provides a bleaching composition, comprising a paper pulp and a GH78 enzyme.
  • a GH78 enzyme Suitable GH78 enzymes are described above.
  • the GH78 enzyme belongs to glycoside hydrolase family 78 and exhibits esterase (feruloyl esterase) and rhamnosidase (a-L- rhamnosidase) activities.
  • the amino acid sequence of the GH78 enzyme may have at least 60% identity, preferably at least 65% identity, more preferably at least 70% identity, more preferably at least 75% identity, more preferably at least 80% identity, more preferably at least 85% identity, more preferably at least 90% identity, more preferably at least 95%, 96%, 97%, 98%, 99%, and most preferably 100% identity to the amino acid sequence of SEQ ID NO: 1 .
  • the number of amino acid substitutions, deletions and/or insertions introduced into the mature polypeptide of SEQ ID NO: 1 is up to 10, e.g., 1 , 2, 3, 4, 5, 6, 7, 8, 9, or 10; or up to 5, e.g., 1 , 2, 3, 4, or 5.
  • the GH78 enzyme is derived from a Xylaria sp., such as Xylaria polymorph a.
  • the pulp is wood pulp.
  • the pulp is a chemical pulp, such as kraft pulp.
  • the invention provides a paper material, which is made from the bleaching composition of the invention, or which is made from a paper pulp subjected to the method of the invention.
  • the invention also provides for use of the methods and compositions above for bleaching and/or decreasing the kappa number of paper pulp
  • a method for increasing the brightness and/or decreasing the kappa number of a paper pulp comprising contacting the paper pulp with a GH78 enzyme.
  • the GH78 enzyme is a glycoside hydrolase exhibiting feruloyl esterase and a-L-rhamnosidase activities. 4. The method of any of items 1 to 3, wherein the amino acid sequence of the GH78 enzyme has at least 60% identity, preferably at least 65% identity, more preferably at least 70% identity, more preferably at least 75% identity, more preferably at least 80% identity, more preferably at least 85% identity, more preferably at least 90% identity, more preferably at least 95%, 96%, 97%, 98%, 99%, and most preferably 100% identity to the amino acid sequence of SEQ ID NO: 1.
  • a bleaching composition comprising a paper pulp and a GH78 enzyme.
  • composition of item 10 wherein the GH78 enzyme belongs to glycoside hydrolase family 78 and exhibits feruloyl esterase and a-L-rhamnosidase activities.
  • composition of item 10 or 1 1 wherein the amino acid sequence of the GH78 enzyme has at least 60% identity, preferably at least 65% identity, more preferably at least 70% identity, more preferably at least 75% identity, more preferably at least 80% identity, more preferably at least 85% identity, more preferably at least 90% identity, more preferably at least 95%, 96%, 97%, 98%, 99%, and most preferably 100% identity to the amino acid sequence of SEQ ID NO: 1.
  • Chemicals used as buffers and substrates were commercial products of at least reagent grade.
  • amino acid sequence of the Xylaria polymorpha GH78 enzyme is shown as SEQ ID NO: 1 .
  • the Xylaria polymorpha GH78 enzyme was assessed for its ability to bleach oxygen- bleached eucalyptus kraft pulp. Feruloyl esterase and a-L-rhamnosidase activities were tested for SEQ ID NO: 1.
  • Xylaria polymorpha GH78 enzyme treatment of oxygen-bleached eucalyptus kraft pulp was carried out in a 1000 ml Lab-O-Mat beaker (Werner Mathis AG, Zurich, Switzerland) at 4% consistency, pH 8 and 40°C for 18 hours.
  • the amount of pulp was 15 g and the enzyme dosage was 50 mg and 1000 mg of Xylaria polymorpha GH78 enzyme per kg dry pulp.
  • the reference pulp (negative control) was kept under the same conditions but without enzyme addition.
  • the water in the pulp was removed by filtration through a Buchner funnel and bleaching was conducted with a DEp-sequence, where D stands for chlorine dioxide and Ep stands for hydrogen peroxide reinforced alkaline extraction.
  • Pulp samples (8 g dry pulp) were DEp-bleached in BA 6040 standard stomacher bags (Seward).
  • the conditions for the D-stage were: 10% consistency, 1 1 .5 kg chlorine dioxide/ton (dry pulp) at 80°C initial pH 3.5 (final pH 2.5) for 1 10 min. After the bleaching, the chlorine dioxide was removed from the pulp samples by using a Buchner funnel. The samples were then washed with tap water thoroughly.
  • Conditions for the Ep-stage were 10% consistency, 5 kg H 2 0 2 /ton (dry pulp), 10.5 kg NaOH/ton (dry pulp) at 85°C for 80 min. After the Ep-stage, the samples were filtered by using a Buchner funnel.
  • TAPPI test method T 452 om-98 The kappa number of the pulp was determined according to TAPPI test method T 236 om-06. The results of the bleaching experiments are shown in Table 1 .
  • Table 1 Brightness and kappa number after DEp- (Reference) and GH78DEp-bleaching of oxygen-bleached eucalyptus kraft pulp.

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  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Chemical & Material Sciences (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • Paper (AREA)

Abstract

L'invention concerne l'utilisation de l'enzyme GH78 dans le blanchiment de pulpe pour préparer des matériaux de papier, comme le papier, le carton double, le carton ondulé, le tissu, les serviettes, les récipients ondulés et les boîtes.
PCT/EP2014/069474 2013-09-20 2014-09-12 Blanchiment enzymatique de pulpe de papier WO2015039962A1 (fr)

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US15/023,252 US20160237618A1 (en) 2013-09-20 2014-09-12 Enzymatic bleaching of paper pulp
EP14766688.7A EP3047065A1 (fr) 2013-09-20 2014-09-12 Blanchiment enzymatique de pulpe de papier

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Cited By (2)

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Publication number Priority date Publication date Assignee Title
CN105780568A (zh) * 2016-04-23 2016-07-20 李树泉 两次生物酶软化脱木素结合机械法制浆工艺
WO2021232840A1 (fr) * 2020-05-20 2021-11-25 江苏科技大学 MUTANT DE TRONCATURE D'α-L-RHAMNOSIDASE ET SON APPLICATION

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
SE543573C2 (en) * 2019-02-12 2021-03-30 Stora Enso Oyj Method of producing a molded fiber product and molded fiber product

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WO1994029425A2 (fr) * 1993-06-16 1994-12-22 Call Hans Peter Systeme de blanchiment a plusieurs composants
WO1998059108A2 (fr) * 1997-06-20 1998-12-30 Blume, Hildegard Systeme d'oxydation et de blanchiment comportant des agents d'oxydation produits par action enzymatique
WO1999039044A1 (fr) * 1998-01-30 1999-08-05 Iogen Corporation Procede et dispositif pour mesurer les besoins en blanchiment et l'aptitude au blanchiment d'une pate a papier, ainsi que l'efficacite d'un traitement enzymatique a l'hemicellulase sur une pate a papier
US20040112555A1 (en) * 2002-12-03 2004-06-17 Jeffrey Tolan Bleaching stage using xylanase with hydrogen peroxide, peracids, or a combination thereof
WO2006047713A2 (fr) * 2004-10-27 2006-05-04 Novozymes North America, Inc. Traitement au dioxyde de chlorure assiste par enzymes
WO2012018691A2 (fr) * 2010-07-31 2012-02-09 Dyadic International, Inc. Nouvelles enzymes fongiques
WO2012092676A1 (fr) * 2011-01-06 2012-07-12 Valorbec Societe En Commandite, Representee Par Gestion Valeo S.E.C. Nouvelles enzymes de déconstruction de parois cellulaires et leurs utilisations
WO2012129697A1 (fr) * 2011-04-01 2012-10-04 Adrian Tsang Nouvelles enzymes de déconstruction de parois cellulaires de talaromyces thermophilus et leurs utilisations

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Publication number Priority date Publication date Assignee Title
WO1994029425A2 (fr) * 1993-06-16 1994-12-22 Call Hans Peter Systeme de blanchiment a plusieurs composants
WO1998059108A2 (fr) * 1997-06-20 1998-12-30 Blume, Hildegard Systeme d'oxydation et de blanchiment comportant des agents d'oxydation produits par action enzymatique
WO1999039044A1 (fr) * 1998-01-30 1999-08-05 Iogen Corporation Procede et dispositif pour mesurer les besoins en blanchiment et l'aptitude au blanchiment d'une pate a papier, ainsi que l'efficacite d'un traitement enzymatique a l'hemicellulase sur une pate a papier
US20040112555A1 (en) * 2002-12-03 2004-06-17 Jeffrey Tolan Bleaching stage using xylanase with hydrogen peroxide, peracids, or a combination thereof
WO2006047713A2 (fr) * 2004-10-27 2006-05-04 Novozymes North America, Inc. Traitement au dioxyde de chlorure assiste par enzymes
WO2012018691A2 (fr) * 2010-07-31 2012-02-09 Dyadic International, Inc. Nouvelles enzymes fongiques
WO2012092676A1 (fr) * 2011-01-06 2012-07-12 Valorbec Societe En Commandite, Representee Par Gestion Valeo S.E.C. Nouvelles enzymes de déconstruction de parois cellulaires et leurs utilisations
WO2012129697A1 (fr) * 2011-04-01 2012-10-04 Adrian Tsang Nouvelles enzymes de déconstruction de parois cellulaires de talaromyces thermophilus et leurs utilisations

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN105780568A (zh) * 2016-04-23 2016-07-20 李树泉 两次生物酶软化脱木素结合机械法制浆工艺
CN105780568B (zh) * 2016-04-23 2017-07-07 上海锴晨实业有限公司 两次生物酶软化脱木素结合机械法制浆工艺
WO2021232840A1 (fr) * 2020-05-20 2021-11-25 江苏科技大学 MUTANT DE TRONCATURE D'α-L-RHAMNOSIDASE ET SON APPLICATION

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