EP0351655B1 - Verfahren zur Zellstoffbehandlung - Google Patents

Verfahren zur Zellstoffbehandlung Download PDF

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Publication number
EP0351655B1
EP0351655B1 EP89112331A EP89112331A EP0351655B1 EP 0351655 B1 EP0351655 B1 EP 0351655B1 EP 89112331 A EP89112331 A EP 89112331A EP 89112331 A EP89112331 A EP 89112331A EP 0351655 B1 EP0351655 B1 EP 0351655B1
Authority
EP
European Patent Office
Prior art keywords
pulp
enzyme
dissolving
treatment
enzymes
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.)
Expired - Lifetime
Application number
EP89112331A
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English (en)
French (fr)
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EP0351655A1 (de
Inventor
Sakari Karsila
Ilkka Kruus
Outi Puuppo
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.)
Genencor International Europe Oy
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Genencor International Europe Oy
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Filing date
Publication date
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Priority to AT89112331T priority Critical patent/ATE82781T1/de
Publication of EP0351655A1 publication Critical patent/EP0351655A1/de
Application granted granted Critical
Publication of EP0351655B1 publication Critical patent/EP0351655B1/de
Anticipated expiration legal-status Critical
Expired - Lifetime legal-status Critical Current

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Classifications

    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21CPRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005Treatment of cellulose-containing material with microorganisms or enzymes

Definitions

  • the invention relates to a method for improving the drainability of mechanical pulp, such as a thermomechanical or deinked pulp, by treating the pulp by a hemicellulose-hydrolyzing enzyme.
  • the drainability of pulp is usually described by the freeness value. It is known that mechanical treatment and deinking deteriorate the drainability of pulp. The use of deinked pulp in particular is restricted due to its poor drainability. During mechanical treatment, a fibre is exposed to stresses, which results in an abundant formation of fine-grained material. For this reason, the drainage properties of finished pulp are not at optimum, which appears as a decreased freeness value. In many cases, the drainage properties, i.e. the practical value of a pulp would be substantially increased if the freeness value could be improved by 10 to 20 units.
  • fibres are separated from wood mechanically by means of heat only without any addition of chemicals.
  • the fibre is thereby subjected to stresses so that the lignin binding the fibres together is softened. Under continued mechanical stress, the elasticity of lignin fails and the fibres are detached from each other.
  • Mechanical pulps include groundwood pulp, refiner mechanical pulp, pressure groundwood pulp and thermomechanical pulp.
  • the required temperature rises in the above order, being at its lowest in the production of groundwood pulp and at its highest in the production of thermomechanical pulp.
  • thermomechanical pulp With groundwood pulp, the negative and positive properties of fine-grained material are substantially balanced, whereas the potential strength properties of thermomechanical pulp in particular are clearly superior to the drainage properties. However, the strength properties of groundwood pulp are relatively poor as compared with the properties of thermomechanical pulp.
  • Recycled pulp is manufactured of waste paper, whereby wood fibre utilized at least once in the form of paper is reused.
  • the main function of a recycled pulp process is to remove impurities contained in waste paper. Methods used for this purpose can be divided into three groups:
  • Recycled pulps can be deinked, if desired.
  • the basic idea of deinking is to separate ink from the fibre chemically and mechanically and to bring the separated ink to a hydrophilic state in a fibre-water slush.
  • the separated ink can be removed from the slush by flotation and/or by washing.
  • a deinking plant uses as raw material two kinds of waste paper: home waste paper and newsprint waste.
  • Home waste paper is unsorted and its composition varies. It typically contains 60 to 70% of newsprint, 20 to 30% of magazine paper and less than 10% of various kinds of paperboard and cardboard.
  • FR-A- 2,557,894 discloses a method in which chemical pulp is subjected to treatment with xylanase enzyme with the purpose of reducing the beating time.
  • Ca-A-758,488 relates to a method in which the beatability of pulp is improved by a cellulase/pectinase/lipase enzyme treatment.
  • FR-A-2,571,738 in turn discloses a method in which pulp is provided with special properties by cellulase treatment.
  • JP-B- 60,126,395 discloses a method for improving the beating process by enzyme addition.
  • JP-B- 59,009,299 discloses a method in which alkaline cellulase and a surface-active agent are added to a deinking process for making the removal of ink more efficient.
  • JP-A- 63,059,494 discloses a method for improving the whiteness of recycled pulp by means of alkaline cellulase.
  • FR-A- 2 604 198 discloses a method for improving the properties of previously beaten pulp, such as recycled pulp having a Schopper-Riegler (SR) number exceeding 25, by means of a cellulase/hemicellulase treatment.
  • SR Schopper-Riegler
  • the SR number can be decreased without affecting adversely the other properties of the pulp.
  • the SR number describes the drainability of pulp; the lower the SR value, the better the rate of dewatering is.
  • Said application describes mainly the treatment of recycled pulps containing plenty of chemical pulp.
  • enzyme treatment according to said application to recycled pulps containing mainly mechanical pulp, it has been found that treatment with enzyme mixtures containing substantial amounts of cellulase deteriorates the strength properties of the pulp; this appears from the examples set forth below.
  • the strength values are decreased even by minor amounts of cellulase especially if the pulp containing enzymes has to be stored for longer periods of time on account of process disturbances, for instance. Therefore it is preferable that the enzyme used in the treatment does not affect adversely the strength properties of pulp, not even during a long time of action (several hours).
  • the object of the present invention is to improve the drainability of mechanical pulp, particularly thermomechanical and/or deinked pulp, by means of enzyme treatment while maintaining the strength properties of the pulp.
  • the invention is characterized by adding to mechanical pulp or to pulp mainly containing mechanical pulp, such as thermomechanical or deinking pulp, at least one hemicellulose-dissolving enzyme or an enzyme preparation containing at least one hemicellulose-dissolving enzyme and being substantially free from cellulose-dissolving enzymes.
  • mechanical pulp such as thermomechanical or deinking pulp
  • at least one hemicellulose-dissolving enzyme or an enzyme preparation containing at least one hemicellulose-dissolving enzyme and being substantially free from cellulose-dissolving enzymes can be carried out in connection with the acidification of the pulp or thereafter.
  • Hemicellulose-dissolving enzymes include xylanases, beta xylosidase, acetyl esterase, alpha arabinosidase, alpha glucuronidase, arabinases and mannanases.
  • Particularly preferred enzymes are xylanases and mannanases.
  • Enzymes suited for the application according to the invention include hemicellulases and hemicellulase preparations, especially xylanases and mannanases, which are substantially free from cellulases.
  • the term "cellulases” refers to enzymes which are able to dissolve crystalline cellulose and to liberate therefrom remarkable amounts of sugars or oligosaccharides.
  • enzymes referred to in the invention are produced e.g. by actinomycetes (such as Streptomyces olivochromogenes) , bacteria (such as Bacillus sp. ) and fungi (such as Penicillium steckii) .
  • a suitable enzyme dosing is about 30 to 200,000 units/kg on the dry content of the pulp, preferably about 100 to 50,000 units/kg.
  • the treatment can be carried out within the pH range from about 2 to about 10, preferably from about 4 to about 8, depending e.g. on the origin and properties of the used hemicellulase enzyme.
  • the treating time depends on the enzyme dosage and the treatment conditions, ranging from 10 minutes to one day, preferably from half an hour to 8 hours.
  • the temperature during the enzyme treatment may vary from about 10 to about 90°C, preferably from about 25 to 70°.
  • the xylanase activity of the enzyme preparations was determined as follows:
  • xylan solution 1%, Sigma No: X-0376, prepared in 50 mM Na citrate buffer, pH 5.3
  • an enzyme suitably diluted in the same buffer was added.
  • the solution was incubated at +50°C in a water bath for 30 minutes.
  • the reaction was stopped by adding 3 ml of DNS reagent (3,5-dinitrosalicylate reagent), and the colour was developed by cooking the sample for 5 minutes.
  • the absorbance was measured at a wave length of 540 nm.
  • One enzyme unit liberates one micromole of reducing sugars calculated as xylose per one minute under the assay conditions.
  • the mannanase activity of the enzyme preparations was determined as follows:
  • locust bean gum solution (0.5%, Sigma No: G-0753, prepared in 50 mM Na-citrate buffer, pH 5.3) 1 ml of an enzyme suitably diluted in the same buffer was added. The solution was incubated at +50°C in a water bath for 10 minutes. The reaction was stopped by adding 3 ml of DNS reagent, and the colour was developed by cooking for 5 minutes. The absorbance was measured at a wave length of 540 nm. One enzyme unit liberates one micromole of reducing sugars calculated as mannose per one minute under the assay conditions.
  • the cellulase activity of the enzyme preparations was determined as filter paper activity (Ghose T.K. et al., Symposium of Enzymatic Hydrolysis of Cellulose, Bailey M., Enari T.M., Linko M., Eds. (SITRA, Aulanko, Finland, 1975), p. 111 to 136):
  • a piece of filter paper (Whatman 1, 50 mg) was added to 1 ml of acetate buffer (0.05 M NaAc, pH 4.8). 1 ml of a suitably diluted enzyme solution was added. The solution was incubated for one hour at 50°C. The reaction was stopped by adding 3 ml of DNS reagent, and the colour was developed and measured as in the xylanase determination. One activity unit liberates 1 micromole of reducing sugars calculated as glucose per one minute.
  • preparation 3 represents a useful enzyme preparation containing hemicellulose-dissolving enzyme (xylanase) and being substantially free from cellulose-dissolving enzymes.
  • Preparations 1 and 2 are reference preparations, which in addition to the hemicellulose activity contain varying amounts of cellulose-dissolving enzyme activities.
  • aqueous slurry having a dry matter content of 10% was prepared from dried deinked pulp (Keräyskuitu Oy, export grade) and allowed to stand overnight at room temperature. The slurry was then diluted with water to a dry content of 5% and defibered in a laboratory mixer (3,000 rpm, 15 min). The pH of the slurry was adjusted from the initial pH of about 7 to 5.4 by means of 1 M sulphuric acid.
  • the hemicellulase treatment clearly improved the drainability of the pulp.
  • Example 1 The results correspond to those obtained in Example 1.
  • the xylanase treatment improved the properties of the pulp. Even though its time of action was shortened, cellulase nevertheless degraded the strength properties of the pulp.
  • Unbleached, unacidified deinked pulp (Keräyskuitu Oy) having a dry matter content of about 7.5 % was allowed to stand overnight, whereafter it was diluted to a concentration of 20 g/l and was defibered and beaten in a hollander to a freeness value of 130. After the beating, the pH was adjusted to 5.5 by 1 M H2SO4.
  • Xylanase enzyme preparation (enzyme preparation 3) was added to the pulp in amounts that appear from Table 4. The pulp was heated by means of a steam coil to 50°C and it was incubated at 50°C in a water bath. The freeness was determined after the pulp had been incubated one hour and four hours. The results are shown in Table 4.
  • Bleached, acidified (pH 7.7) deinked pulp (Keräyskuitu Oy, normal grade) having a dry matter content of about 10% was allowed to stand overnight, whereafter it was diluted to a concentration of 20 g/l and defibered by a hollander. After defibering the pH was adjusted to 5.5 by 1 M H2SO4, whereafter beating was carried out. The freeness of the pulp before beating was 199 and after a beating time of 5 minutes 131.
  • Xylanase enzyme preparation (enzyme preparation 3) was added to the pulp in amounts that appear from Table 5.
  • the pulp was heated by means of a steam coil to 50°C and it was incubated at 50°C in a water bath. The freeness value was determined after the pulp had been incubated for one hour and four hours, respectively. The results are shown in Table 5.
  • the xylanase enzyme preparation free from cellulase activity increases the freeness value of a bleached, unacidified deinking pulp by 10 to 15 units depending on the dosing.
  • the enzyme When the enzyme is applied in an integrated plant, i.e. in a plant in which either a plant producing mechanical pulp or a deinking plant is connected to a paper mill, the enzyme addition can be carried out before the pulp is transferred to a paper machine. If the above-mentioned deinking plant is not integrated with a paper mill, the enzymes can be added to the slurry of the pulp and then allowed to act a suitable period of time, whereafter the pulp is dried and after-treated as desired. Enzymes can be alternatively added to the pulp slurry at the paper mill and then allowed to act, if the pulp has been purchased from elsewhere.
  • Enzyme treatment is also suitable for chemimechanical pulp, in which the separating of fibres is mainly carried out mechanically while using a weak chemical dosage as an aid for softening the lignin.
  • a typical example of such pulp is CTMP pulp (chemical thermomechanical pulp).

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • Paper (AREA)
  • Non-Adjustable Resistors (AREA)
  • Materials For Medical Uses (AREA)
  • Excavating Of Shafts Or Tunnels (AREA)
  • Electrical Discharge Machining, Electrochemical Machining, And Combined Machining (AREA)
  • Chemical Treatment Of Metals (AREA)
  • Noodles (AREA)
  • Polysaccharides And Polysaccharide Derivatives (AREA)

Claims (12)

  1. Verfahren zur Verbesserung der Entwässerbarkeit von mechanischem Papierzellstoff oder von Zellstoff, der hauptsächlich mechanischen Papierzellstoff enthält, durch Enzymbehandlung, gekennzeichnet durch Zuzatz von mindestens einem Hemicellulose auflösenden Enzym oder einer Enzymbereitung, die mindestens ein Hemicellulose auflösendes Enzym enthält und im wesentlichen frei von Cellulose auflösenden Enzymen ist.
  2. Verfahren nach Anspruch 1, dadurch gekennzeichnet, daß der mechanische Papierzellstoff thermomechanischer Zellstoff ist.
  3. Verfahren nach Anspruch 1, dadurch gekennzeichnet, daß der mechanische Papierzellstoff entfärbter Zellstoff ist.
  4. Verfahren nach Anspruch 1 oder 3, dadurch gekennzeichnet, daß das/die Enzym(e) zusammen mit oder nach der Säuerung zugesetzt werden.
  5. Verfahren nach beliebigen der vorstehenden Ansprüche, dadurch gekennzeichnet, daß das/die Hemicellulose auflösende Enzym oder Enzymbereitung in einer Menge von ca. 30 bis ca. 200.000 Enzymeinheiten/kg, berechnet auf die Trockensubstanz des Zellstoffs, zugesetzt werden.
  6. Verfahren nach Anspruch 5, dadurch gekennzeichnet, daß das/die Hemicellulose auflösende Enzym oder Enzymbereitung in einer Menge von ca. 100 bis ca. 50. 000 Enzymeinheiten/kg, berechnet auf die Trockensubstanz des Zellstoffs, zugesetzt werden.
  7. Verfahren nach einem beliebigen der vorstehenden Ansprüche, dadurch gekennzeichnet, daß Xylanase oder Xylanase-Bereitungen, die im wesentlichen frei von Cellulose auflösenden Enzymen sind, dem Zellstoff zugesetzt werden.
  8. Verfahren nach einem beliebigen der vorstehenden Ansprüche, dadurch gekennzeichnet, daß Mannanase oder Mannanase-Bereitung, die im wesentlichen frei von Cellulose auflösenden Enzymen sind, dem Zellstoff zugesetzt werden.
  9. Verfahren nach einem beliebigen der vorstehenden Ansprüche, dadurch gekennzeichnet, daß die Enzymbehandlung im pH-Bereich von ca. 2 bis ca. 10 durchgeführt wird.
  10. Verfahren nach Anspruch 9, dadurch gekennzeichnet, daß die Enzymbehandlung im pH-Bereich von ca. 4 bis ca. 8 durchgeführt wird.
  11. Verfahren nach einem beliebigen der vorstehenden Ansprüche, dadurch gekennzeichnet, daß die Enzymbehandlung bei ca. 10 bis 90°C durchgeführt wird.
  12. Verfahren nach Anspruch 11, dadurch gekennzeichnet, daß die Enzymbehandlung bei ca. 25 bis 70°C durchgeführt wird.
EP89112331A 1988-07-22 1989-07-06 Verfahren zur Zellstoffbehandlung Expired - Lifetime EP0351655B1 (de)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AT89112331T ATE82781T1 (de) 1988-07-22 1989-07-06 Verfahren zur zellstoffbehandlung.

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FI883491 1988-07-22
FI883491A FI81394C (fi) 1988-07-22 1988-07-22 Foerfarande foer behandling av massa med enzymer

Publications (2)

Publication Number Publication Date
EP0351655A1 EP0351655A1 (de) 1990-01-24
EP0351655B1 true EP0351655B1 (de) 1992-11-25

Family

ID=8526856

Family Applications (1)

Application Number Title Priority Date Filing Date
EP89112331A Expired - Lifetime EP0351655B1 (de) 1988-07-22 1989-07-06 Verfahren zur Zellstoffbehandlung

Country Status (9)

Country Link
EP (1) EP0351655B1 (de)
AT (1) ATE82781T1 (de)
BR (1) BR8903649A (de)
CA (1) CA1339605C (de)
DE (1) DE68903608T2 (de)
ES (1) ES2037341T3 (de)
FI (1) FI81394C (de)
GR (1) GR3006466T3 (de)
NZ (1) NZ229811A (de)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2004101889A2 (en) * 2003-05-06 2004-11-25 Novozymes North America, Inc. Use of hemicellulase composition in mechanical pulp production

Families Citing this family (23)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2604198B1 (fr) * 1986-09-22 1989-07-07 Du Pin Cellulose Procede de traitement d'une pate papetiere par une solution enzymatique.
FI87372C (fi) * 1989-03-30 1992-12-28 Genencor Int Europ Foerfarande foer framstaellning av fluffmassa med foerbaettrad rivbarhet
FI92414B (fi) * 1989-11-27 1994-07-29 Enso Gutzeit Oy Menetelmä massan valmistamiseksi
DK80390D0 (de) * 1990-03-29 1990-03-29 Novo Nordisk As
US5837515A (en) * 1990-05-16 1998-11-17 Alko-Yhtiot Oy Enzyme preparations and methods for their production
GB9018426D0 (en) * 1990-08-22 1990-10-03 Sandoz Ltd Improvements in or relating to novel compounds
EP0486125A1 (de) * 1990-11-13 1992-05-20 JAPAN PULP & PAPER RESEARCH INSTITUTE, INC. Lignocellulolytische Zusammensetzung, Verfahren zu deren Herstellung und deren Verwendung
US5616215A (en) * 1991-04-19 1997-04-01 Novo Nordisk A/S Method of making paper from pulp treated with lipase and an aluminum salt
US5169497A (en) * 1991-10-07 1992-12-08 Nalco Chemical Company Application of enzymes and flocculants for enhancing the freeness of paper making pulp
FI92500C (fi) * 1993-03-03 1994-11-25 Valtion Teknillinen Menetelmä mekaanisen massan valmistamiseksi
US7816129B2 (en) 1994-07-29 2010-10-19 Ab Enzymes Gmbh Production and secretion of proteins of bacterial origin in filamentous fungi
US6300114B1 (en) 1994-07-29 2001-10-09 Rohm Enzyme Finland Oy Sequences of xylanase and xylanase expression vectors
US5871730A (en) * 1994-07-29 1999-02-16 Universite De Sherbrooke Thermostable xylanase DNA, protein and methods of use
US5935836A (en) * 1994-07-29 1999-08-10 Rohm Enzyme Finland Oy Actinomadura xylanase sequences and methods of use
US5770012A (en) * 1994-11-18 1998-06-23 P. H. Glatfelter Co. Process for treating paper machine stock containing bleached hardwood pulp with an enzyme mixture to reduce vessel element picking
US5725732A (en) * 1994-11-18 1998-03-10 P. H. Glatfelter Company Process for treating hardwood pulp with an enzyme mixture to reduce vessel element picking
GB2296513B (en) * 1994-12-24 1998-07-29 Ciba Geigy Ag Paper treatment
US5961735A (en) * 1995-06-21 1999-10-05 North Carolina State University Method of cleaning papermaking felts with enzymes
WO1998006892A1 (en) * 1996-08-16 1998-02-19 International Paper Company Enzymatic freeness enhancement
US6939437B1 (en) 1999-11-19 2005-09-06 Buckman Laboratories International, Inc. Paper making processes using enzyme and polymer combinations
CN104631176B (zh) * 2015-02-09 2016-06-01 绍兴文理学院 一种黄麻纤维素的制备方法
CN104631175B (zh) * 2015-02-09 2016-06-01 绍兴文理学院 一种短流程黄麻纤维素的制备方法
CN104631178B (zh) * 2015-02-09 2016-08-24 绍兴文理学院 一种粗制纤维素的深度纯化方法

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2557894B1 (fr) * 1984-01-10 1986-12-12 Centre Tech Ind Papier Procede de traitement de pates papetieres par une solution enzymatique favorisant la fibrillation et pates ainsi traitees.
FR2604198B1 (fr) * 1986-09-22 1989-07-07 Du Pin Cellulose Procede de traitement d'une pate papetiere par une solution enzymatique.

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2004101889A2 (en) * 2003-05-06 2004-11-25 Novozymes North America, Inc. Use of hemicellulase composition in mechanical pulp production
WO2004101889A3 (en) * 2003-05-06 2005-12-15 Novozymes North America Inc Use of hemicellulase composition in mechanical pulp production

Also Published As

Publication number Publication date
GR3006466T3 (de) 1993-06-21
CA1339605C (en) 1997-12-30
NZ229811A (en) 1991-03-26
FI81394C (fi) 1993-07-20
ATE82781T1 (de) 1992-12-15
FI883491A (fi) 1990-01-23
DE68903608D1 (de) 1993-01-07
FI883491A0 (fi) 1988-07-22
BR8903649A (pt) 1990-03-13
EP0351655A1 (de) 1990-01-24
DE68903608T2 (de) 1993-04-01
FI81394B (fi) 1990-06-29
ES2037341T3 (es) 1993-06-16

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