EP0351655B1 - A method for the treatment of pulp - Google Patents
A method for the treatment of pulp Download PDFInfo
- 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
Links
- 238000000034 method Methods 0.000 title claims abstract description 31
- 238000011282 treatment Methods 0.000 title claims abstract description 29
- 108090000790 Enzymes Proteins 0.000 claims abstract description 77
- 102000004190 Enzymes Human genes 0.000 claims abstract description 77
- 229920001131 Pulp (paper) Polymers 0.000 claims abstract description 40
- 238000002360 preparation method Methods 0.000 claims abstract description 21
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 claims description 17
- 239000000126 substance Substances 0.000 claims description 7
- 102100032487 Beta-mannosidase Human genes 0.000 claims description 6
- 108010055059 beta-Mannosidase Proteins 0.000 claims description 6
- 230000020477 pH reduction Effects 0.000 claims description 2
- 229940088598 enzyme Drugs 0.000 description 51
- 230000000694 effects Effects 0.000 description 12
- 239000000123 paper Substances 0.000 description 12
- 108010059892 Cellulase Proteins 0.000 description 11
- 229940106157 cellulase Drugs 0.000 description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 239000002761 deinking Substances 0.000 description 8
- 239000000463 material Substances 0.000 description 7
- 239000002002 slurry Substances 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 241000196324 Embryophyta Species 0.000 description 6
- 238000010009 beating Methods 0.000 description 6
- 108010002430 hemicellulase Proteins 0.000 description 6
- 229920005610 lignin Polymers 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000010893 paper waste Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- LWFUFLREGJMOIZ-UHFFFAOYSA-N 3,5-dinitrosalicylic acid Chemical compound OC(=O)C1=CC([N+]([O-])=O)=CC([N+]([O-])=O)=C1O LWFUFLREGJMOIZ-UHFFFAOYSA-N 0.000 description 4
- 230000002411 adverse Effects 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 229940079919 digestives enzyme preparation Drugs 0.000 description 4
- 239000000835 fiber Substances 0.000 description 4
- 229940059442 hemicellulase Drugs 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 235000000346 sugar Nutrition 0.000 description 4
- 150000008163 sugars Chemical class 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 235000011149 sulphuric acid Nutrition 0.000 description 3
- 230000000930 thermomechanical effect Effects 0.000 description 3
- 108010084185 Cellulases Proteins 0.000 description 2
- 102000005575 Cellulases Human genes 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 101710166469 Endoglucanase Proteins 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 239000007979 citrate buffer Substances 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 108010013043 Acetylesterase Proteins 0.000 description 1
- 241000186361 Actinobacteria <class> Species 0.000 description 1
- 102100031260 Acyl-coenzyme A thioesterase THEM4 Human genes 0.000 description 1
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 229920002488 Hemicellulose Polymers 0.000 description 1
- 101000638510 Homo sapiens Acyl-coenzyme A thioesterase THEM4 Proteins 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 229920000161 Locust bean gum Polymers 0.000 description 1
- 102100036617 Monoacylglycerol lipase ABHD2 Human genes 0.000 description 1
- 241000906118 Penicillium steckii Species 0.000 description 1
- 108010059820 Polygalacturonase Proteins 0.000 description 1
- 241000187134 Streptomyces olivochromogenes Species 0.000 description 1
- 229920002522 Wood fibre Polymers 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 108010084650 alpha-N-arabinofuranosidase Proteins 0.000 description 1
- 108010061261 alpha-glucuronidase Proteins 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000011111 cardboard Substances 0.000 description 1
- 238000012993 chemical processing Methods 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 108010038658 exo-1,4-beta-D-xylosidase Proteins 0.000 description 1
- 108010093305 exopolygalacturonase Proteins 0.000 description 1
- 238000005188 flotation Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 239000000711 locust bean gum Substances 0.000 description 1
- 235000010420 locust bean gum Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000010297 mechanical methods and process Methods 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 239000011087 paperboard Substances 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 239000013055 pulp slurry Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000001117 sulphuric acid Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 229920001221 xylan Polymers 0.000 description 1
- 150000004823 xylans Chemical class 0.000 description 1
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
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).
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Paper (AREA)
- Electrical Discharge Machining, Electrochemical Machining, And Combined Machining (AREA)
- Chemical Treatment Of Metals (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Noodles (AREA)
- Materials For Medical Uses (AREA)
- Excavating Of Shafts Or Tunnels (AREA)
- Non-Adjustable Resistors (AREA)
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 |
---|---|---|---|
FI883491A FI81394C (fi) | 1988-07-22 | 1988-07-22 | Foerfarande foer behandling av massa med enzymer |
FI883491 | 1988-07-22 |
Publications (2)
Publication Number | Publication Date |
---|---|
EP0351655A1 EP0351655A1 (en) | 1990-01-24 |
EP0351655B1 true EP0351655B1 (en) | 1992-11-25 |
Family
ID=8526856
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP89112331A Expired - Lifetime EP0351655B1 (en) | 1988-07-22 | 1989-07-06 | A method for the treatment of pulp |
Country Status (9)
Country | Link |
---|---|
EP (1) | EP0351655B1 (cs) |
AT (1) | ATE82781T1 (cs) |
BR (1) | BR8903649A (cs) |
CA (1) | CA1339605C (cs) |
DE (1) | DE68903608T2 (cs) |
ES (1) | ES2037341T3 (cs) |
FI (1) | FI81394C (cs) |
GR (1) | GR3006466T3 (cs) |
NZ (1) | NZ229811A (cs) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2004101889A3 (en) * | 2003-05-06 | 2005-12-15 | Novozymes North America Inc | Use of hemicellulase composition in mechanical pulp production |
Families Citing this family (24)
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 (cs) * | 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 (en) * | 1990-11-13 | 1992-05-20 | JAPAN PULP & PAPER RESEARCH INSTITUTE, INC. | Lignocellulolytic composition, process of producing the same and use of the same |
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 |
US5871730A (en) * | 1994-07-29 | 1999-02-16 | Universite De Sherbrooke | Thermostable xylanase DNA, protein and methods of use |
US7816129B2 (en) | 1994-07-29 | 2010-10-19 | Ab Enzymes Gmbh | Production and secretion of proteins of bacterial origin in filamentous fungi |
US5935836A (en) * | 1994-07-29 | 1999-08-10 | Rohm Enzyme Finland Oy | Actinomadura xylanase sequences and methods of use |
US6300114B1 (en) | 1994-07-29 | 2001-10-09 | Rohm Enzyme Finland Oy | Sequences of xylanase and xylanase expression vectors |
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 |
US6066233A (en) * | 1996-08-16 | 2000-05-23 | International Paper Company | Method of improving pulp freeness using cellulase and pectinase enzymes |
US6939437B1 (en) | 1999-11-19 | 2005-09-06 | Buckman Laboratories International, Inc. | Paper making processes using enzyme and polymer combinations |
SE525872C2 (sv) * | 2002-09-06 | 2005-05-17 | Stora Enso Ab | Metod att tillverka mekanisk massa med reducerad energikonsumtion |
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 |
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 |
Family Cites Families (2)
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. |
-
1988
- 1988-07-22 FI FI883491A patent/FI81394C/fi not_active IP Right Cessation
-
1989
- 1989-07-04 NZ NZ229811A patent/NZ229811A/en unknown
- 1989-07-06 AT AT89112331T patent/ATE82781T1/de not_active IP Right Cessation
- 1989-07-06 EP EP89112331A patent/EP0351655B1/en not_active Expired - Lifetime
- 1989-07-06 ES ES198989112331T patent/ES2037341T3/es not_active Expired - Lifetime
- 1989-07-06 DE DE8989112331T patent/DE68903608T2/de not_active Expired - Fee Related
- 1989-07-21 CA CA000606351A patent/CA1339605C/en not_active Expired - Fee Related
- 1989-07-24 BR BR898903649A patent/BR8903649A/pt not_active IP Right Cessation
-
1992
- 1992-12-07 GR GR920402824T patent/GR3006466T3/el unknown
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
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 (cs) | 1993-06-21 |
NZ229811A (en) | 1991-03-26 |
EP0351655A1 (en) | 1990-01-24 |
FI81394B (fi) | 1990-06-29 |
FI883491A0 (fi) | 1988-07-22 |
ES2037341T3 (es) | 1993-06-16 |
CA1339605C (en) | 1997-12-30 |
FI81394C (fi) | 1993-07-20 |
DE68903608T2 (de) | 1993-04-01 |
BR8903649A (pt) | 1990-03-13 |
DE68903608D1 (de) | 1993-01-07 |
FI883491L (fi) | 1990-01-23 |
ATE82781T1 (de) | 1992-12-15 |
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