WO1993011296A1 - Method and enzymatic preparation for treatment of cellulose pulps - Google Patents
Method and enzymatic preparation for treatment of cellulose pulps Download PDFInfo
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- WO1993011296A1 WO1993011296A1 PCT/FI1992/000332 FI9200332W WO9311296A1 WO 1993011296 A1 WO1993011296 A1 WO 1993011296A1 FI 9200332 W FI9200332 W FI 9200332W WO 9311296 A1 WO9311296 A1 WO 9311296A1
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- glucuronidase
- pulp
- enzyme
- preparation
- enzyme preparation
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01139—Alpha-glucuronidase (3.2.1.139)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
-
- 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 present invention concerns a method in accordance with the preamble of claim 1 for treatment of lignocellulosic material, in particular cellulose pulps.
- the invention also concerns an enzymatic preparation which is useful for pulp treatment according to the preamble of claim 20.
- carboxylic groups present in cellulose pulps affect mainly the surface charge of the pulp (Sj ⁇ strom 1989). The number of these groups depends essentially on the pulping method used. Thus, the carboxylic groups in kraft as well as in mechanical pulps consist mainly of methylglucuronic acid groups in xylan (Sj ⁇ strom 1989). However, in sulphite pulps, in addition to the methyl glucuronic acid groups of xylan, the carboxylic groups comprise sulphonic acids present in lignin, formed during the sulphite pulping process.
- the strength and degree of dissociation of the carboxylic groups depends on the counter-ion of the carboxylic group (Scallan and Grumble 1979, Scallan 1983, Lindstr ⁇ m and Carlsson 1982).
- the counter-ion is hydrogen or a metal ion.
- a great part, in fact most of the metals present in the pulps are bound to these carboxylic groups. This is the case both with chemical and mechanical pulps.
- the metal-ions of cellulose pulps may be either useful or harmful to pulp processing.
- a kraft pulp which is deficient in metal counter-ions of the carboxylic groups is poorly suited to enzymatic treatments.
- the metal-ions present in the pulps may in many respects be undesirable for the processing of cellulose pulps.
- many metal-ions, especially iron and manganese are detrimental in the peroxide treatment and cause instability of the peroxide. These substances must be removed in order to achieve an optimal bleaching result.
- the removal of metal-ions is also essential in the production of certain special pulps.
- the metal content of pulps can be decreased either by lowering the pH of the pulp to a value, at which the metal-ions are dissociated, or by treating the pulps with known complexing agents, such as DTPA or EDTA (Basta et al. 1991).
- known complexing agents such as DTPA or EDTA
- DTPA EDTA
- EDTA EDTA
- considerable drawbacks are associated with these methods.
- a pulp is formed which is very resistant to the enzymatic treatment prior to bleaching.
- Some of the unnatural complexing agents may, on the other hand, cause problems e.g. in the waste water purification systems.
- the invention is based on the idea that by enzymatically removing the carboxylic groups of hemicelluloses from the cellulose pulps, both the surface charge and the metal-ion centent of the pulp can be changed. According to the method of the present invention, the carboxylic groups are therefore removed by treating the cellulose pulp with an enzyme preparation, having an essential glucuronidase enzyme activity.
- the enzyme preparation according to the present invention is characterized by what is stated in the characterizing part of claim 20.
- enzyme preparation denotes any product which contains at least one enzyme.
- an enzyme preparation may be a culture liquor containing one or more enzymes, an isolated enzyme or a mixture of one or more enzymes.
- essential glucuronidase activity means that the glucuronidase activity of the enzyme preparation is comparatively high when compared with the other enzyme activities in the preparation, in order for it to remove an essential part of glucuronic acid groups from the substrate.
- Glucuronic acid groups used in this application is an abbreviation of 4-O-methyl-D- glucuronic acid groups.
- the paper technical properties of pulps can be modified by enzymatically removing the carboxylic groups of the pulps.
- the glucuronidase treatment is conducted before the bleaching stage of cellulose pulp. In this way, the consumption of bleaching chemicals can be decreased. Because the glucuronidase treatment decreases the metal-ion content of pulps, hydrogen peroxide can be advantageously used as the bleaching chemical.
- the amounts of carboxylic groups in the pulp are modified by using glucuronidase in such a way that the action of enzymes on fibre materials can be optimized essentially without any hydrolyzation of the hemicelluloses in the fibres.
- TCF-puIps totally chlorine free pulps
- the glucuronidase treatment can be conducted separately, simultaneously with another enzymatic treatment, or before such a treatment.
- a hemicellulase e.g. xylanase, mannanase
- the glucuronidase treatment can also be combined with other cellulase and/or ligninase treatments.
- the method of the invention is also suitable for the treatment o any lignocellulosic pulps, i.e. mechanical or chemimechanical pulps.
- any lignocellulosic pulps i.e. mechanical or chemimechanical pulps.
- the enzyme preparation used comprises the cultivation liquid or medium of a glucuronidase-producing microorganism.
- a cultivation medium is concentrated before use.
- the enzyme preparation comprises a purified enzyme, isolated from a cultivation liquid.
- the glucuronidase enzyme is isolated from the cultivation liquid of the fungus Trichoderma reesei using anionic ion exchangers and purified by hydrophobic interaction chromatography. It has unexpectedly turned out that the enzyme can be easily isolated by means of these methods.
- the purified glucuronidase which is new, has a molecular weight of about 95 kDa according to the SDS-PAGE method.
- the glucuronidase can also be isolated by simple methods from cultivation liquids of Schizophyllum commune or Aspergillus niger strains. These enzymes, which also are new, are described in more detail in working examples 3 and 4.
- the enzyme preparation useful for treatment of lignocellulosic materials comprises an essential glucuronidase enzyme activity and contains only minor amounts, if any, of hemicellulases.
- the invention is not, however, limited to the indicated origins of the enzyme nor to the isolation method, and the enzyme can also be obtained by other methods.
- the enzyme can also be obtained by other methods.
- the glucuronidase preparation can be derived from a microorganism strain selected from the group essentially consisting of microorganisms of the genera Trichoderma (e.g. T. reesei), Aspergillus (e.g. A. niger, A. awamori, A. terreus, A. oryzae), Schizophyllum (e.g. S. commune), Aureobasidium (e.g. A. pullulans), Phanerochaete (e.g. P. chrysosporium), Fusarium (e.g. F. oxysporum), Agaricus (e.g. A. bisporus), Penicillium (e.g. P.
- a microorganism strain selected from the group essentially consisting of microorganisms of the genera Trichoderma (e.g. T. reesei), Aspergillus (e.g. A. niger, A. awamori, A. terre
- janthinellum P. digitatwn
- Streptomyces e.g. S. olivochromogenes, S. ⁇ avogriseus
- Bacillus e.g. B. subtilis, B. circulans
- It can also be derived from a microorganism strain selected from the group comprising Thermoascus auranticus, Curvularia inequalis, Tyromyces palustris, Cryptonectria parasitica, Myceliophthora thermophila, and Thermobacter auranticus.
- All these microorganisms can be used to produce glucuridases, which hydrolyze the glucuronic side groups of xylan.
- the enzyme preparations are prepared by cultivating on a cultivation medium comprising xylans any of the above-mentioned glucuronidase- producing microorganisms.
- the method according to the invention provides remarkable advantages.
- a glucuronidase as described herein prior to or simultaneously with the treatment of. the pulp with another enzyme (e.g. xylanase)
- the degree of hydrolysis can be increased and the xylanase treatment can be performed at a low pH-value.
- the effect of the treatment is based specifically on the removal of charged groups and not on the. total hydrolysis of hemicelluloses.
- the effect of the present method is based on the enzymatic removal of glucuronic acid groups in order to change the surface charge into an advantageous form with respect to further treatments either chemical or enzymatical.
- the action of, e.g., enzymes to affect the most advantageous parts of the fibre substrate can be regulated.
- factors such as surface charge
- these factors can be manipulated in order to achieve most efficient extraction of residual lignin from the fibres.
- the regulation of these factors with the method of invention also affects directly the type and amount of chemicals to be used for the industrial scale extraction of lignin from the fibres and can be further used to improve the low-chlorine or chlorine-free bleaching methods, thus reducing environmental pollution.
- the metal binding glucuronic acid groups can be hydrolyzed, which will enhance the removal of the metal-ions of the pulp.
- the enzymatic removal of glucuronic acid groups can be used to improve the production of certain pulps, such as metal-free pulps.
- the paper technical properties of the chemical and mechanical pulps can be modified by using the glucuronidase treatment.
- the number of carboxylic groups and of counter-ions bound to them affect the electric charge of the pulp. These factors can be described by different chemical and physical parameters and the surface charge of fibres (pulps) can be measured with the zeta-potential (Melzer 1972).
- the metal content of pulps can be measured by analyzing the metals in pulp with an atom absorption spectrophotometer.
- the carboxylic acid content of pulps can be measured e.g. by the method of Sj ⁇ str ⁇ m (KCL method 192:68).
- the action of enzymes in the fibres can be described by the liberation of sugars and by the extractability of lignin fragments after the enzymatic treatment.
- Another method is to measure the increase o brightness, which can be obtained after the enzymatic treatment which changes the surface charge, i.e. converts the zeta-potential and the carboxylic acid content into a desirable form.
- Example 1 Production of ⁇ -glucuronidase by different fungal strains.
- Medium A contained, in g l "1 : wheat bran 10, Solka floe cellulose 10, distiller's spent grain
- Medium B contained, in g l "1 : beech xylan (Lenzing AG, Austria) 10, birch glucuronoxylan (Roth 7500) 5, oligo- saccharides from steaming of birchwood 5, distiller's spent grain 10 and mineral salts as in medium A.
- This medium was considered potentially advantageous for the production of ⁇ - glucuronidase because of the presence of glucuronic acid-substituted xylo-oligosaccharides and xylans in the substrate.
- the screening cultivations were performed in 250 ml shake flasks containing 50 ml medium. Cultivation was carried out for 4 days, but samples were also taken from the cultivations after 2 days.
- the thermophilic fungus Myceliophthora thermophila was cultivated at 37 °C and all the other strains at 30 °C.
- ⁇ -glucuronidase was assayed in the culture supernatants by incubating 100 ⁇ with 900 ⁇ 1 % glucuronoxylan (Roth 7500) at pH 4.8 (0.05 M Na- acetate buffer) for 24 hours at 40 °C and measuring the organic acids produced as glucuronic acid using the method of Kandke et al (1989). The results were expressed as relative production units on the basis of the spectrophotometric absorbance of the reaction mixtures at 660 ⁇ m. The results of the screening test for production of ⁇ -glucuronidase are presented in Table 1.
- MEDIUM B Beech xylan (Lenzing) 10 Birch glucuronoxylan (Roth) 5
- Trichoderma. reesei RUT C 30 (VTT-D-86271, ATCC 56765) was cultivated in a bioreactor (Chemap LF 20, working volume 16 1) on a medium containing 30 g l "1 xylan (Lenzing AG, Lenz, Austria) and 15 g l "1 corn steep solids (Sigma C-8160) as the main carbon and nitroge sources, supplemented with 5 gl "1 KH 2 PO 4 and 5 gl *1 (NH 4 ) 2 SO 4 .
- Cultivation conditions were temperature 29 °C, pH controlled between 6.0 and 6.5, aeration about 9 1 min "1 and cultivation time 3 days. The mycelium was separated by centrifugation.
- the clarified supernatant was first fractionated by cation exchange chromatography.
- the sample was equilibrated at pH 4.5 by acetic acid and at a conductivity corresponding to 50 mM sodium acetate buffer, pH 4.5, containing 0.14 mol I "1 NaCl.
- the diluted supernatant was applied to a column (113 x 200 mm) of DEAE Sepharose FF (Pharmacia), pre- equilibrated with this buffer. Elution was performed first with the equilibrating buffer to remove unadsorbed proteins and thereafter with a linear addition of sodium chloride from 150 to 400 mM.
- Fractions (each 450 ml) which contained the or-glucuronidase eluting during the NaCl gradient were combined for the next purification step by hydrophobic interaction chromatography.
- the other adsorbed proteins were eluted by increasing the NaCl concentration to 1.0 M and the column was washed with 10 mM sodium hydroxide.
- the enzyme preparation obtained in the first chromatographic step was adjusted to pH 5.5 by sodium hydroxide and to a conductivity of 122 mScm "1 by adding (NH 4 ) 2 SO 4 .
- the sample was applied to a column (113 x 110 mm) of Phenyl Sepharose FF (Pharmacia), previously equilibrated with 25 mM sodium acetate buffer, pH 5.5, containing 0.8 mol l "1 (NH 4 ) 2 SO 4 .
- Elution was performed first with the equilibrating buffer and thereafter with a linear gradient of ammonium sulphate from 0.8 M to 0.6 M. Fractions which contained the or-glucuronidase eluted by 0.8 M ammonium sulphate and the decreasing gradient were combined. The other adsorbed proteins were eluted by decreasing the (NH 4 ) 2 SO 4 concentration to 0 M and the column was washed with 6 M urea.
- the preparation obtained by hydrophobic chromatography was concentrated in smaller batches (150 - 250 ml) to 20 ml by ultrafiltration (Amicon PM-10 membranes) and applied to a gel filtration column of Sephacryl S-100 HR (Pharmacia, 50 x 745 mm).
- the purified ⁇ - glucuronidase protein was eluted with 50 mM sodium acetate buffer, pH 5.0.
- ⁇ -Glucuronidase activity was assayed on the basis of the method of Khandke et al. (1989).
- the assay was performed by incubating 40 ⁇ l of methylated triuronic acid, 2'-O-(4-O- methyl- ⁇ r-(l,2)-glucuronic acid-jS-D-xylobiose (mGluAX 2 2.5 mg ml "1 , 5.3 mM) with 10 ⁇ l o appropriate enzyme dilution in 0.05 mM sodium acetate, pH 4.8 for 10 or 60 min.
- the reaction was stopped by adding 200 ⁇ l of the copper sulphate reagent of Milner and Avigad (1967) whereafter the mixture was heated in a boiling water bath for 10 min. After cooling,
- the characteristics of the purified or-glucuronidase were determined using standard methods of protein chemistry. These characteristics are described in Table 2. Xylanase activity was assayed as described by Bailey et al. (1992) using 1.0 % (w/v) birchwood 4-O-glucurono- xylan (Roth 7500) as substrate in 50 mM sodium citrate buffer, pH 5.3. 0-Xylosidase was assayed as described by Poutanen and Puls (1988). All enzymatic activities were expressed in SI units (katals).
- a sample of culture filtrate of T. reesei VTT-D-86271 was investigated for its content of or- glucuronidase proteins by gel filtration chromatography on a 1.5 litre column of Sephacryl S 100 HR (column height 74.5 cm).
- glucuronidase described with a molecular weight of 95 kDa
- two minor glucuronidase activities with apparent molecular weights below 50 kDa could be observed.
- - glucuronoxylan B (Sigma M-5144) 6.3 mg/1 a 50 ⁇ g ml "1 of enzyme protein in 50 mM sodium phosphate-citrate buffers, pH from 3.0 to 7.5; incubation at 40 °C for 24 h.
- substrate concentration in the hydrolysis study 4 mM for xylo-oligomers or 8 mg ml "1 for xylans; enzyme dosing: 6 mg protein mmol "1 xylo-oligomers or 3 mg protein g' 1 glucuronoxylan; incubation for 24 h at 40 °C at pH 4.8.
- Aspergillus niger VTT-D-77050 was cultivated in a bioreactor (Chemap CF
- Diatomaceous earth (Celite Standard Super Cel, Manville) was equilibrated with 50 mM sodium acetate buffer, pH 4.5, and the or-glucuronidase protei was adsorbed from the diluted supernatant to this carrier.
- the diatomaceous earth was washed once with 50 mM sodium acetate buffer after which the or-glucuronidase was eluted with 0.1 M sodium phosphate buffer containing sodium chloride up to a concentration of 0.5 M.
- the solution containing the eluted proteins was equilibrated with 10 mM sodium phosphate buffer, pH 6.5 using gel filtration and applied to a column of DEAE Sepharose F (Pharmacia), pre-equilibrated with the same buffer.
- Elution was performed first with the equilibrating buffer to remove unadsorbed proteins and thereafter with a linear addition of sodium chloride from 150 to 0.2 M. Fractions which contained the or-glucuronidase eluting during the NaCl gradient were combined for the next purification step by cation exchange chromatography. The other adsorbed proteins were eluted by increasing the NaCl concentration to 1.0 M.
- the enzyme preparation obtained in the first chromatographic step was equilibrated with 10 mM sodium acetate buffer, pH 4.4 using gel filtration and applied to a column of CM Sepharose FF (Pharmacia), pre-equilibrated with the same buffer. Elution was performed first with the equilibrating buffer to remove unadsorbed proteins and thereafter with a linear addition of sodium chloride from 0 to 0.2 M. Fractions which contained the or-glucuronidase eluting at the end of the NaCl gradient were combined and analysed by standard methods for or-glucuronidase, ⁇ -xylanase and ⁇ -xylosidase activities as described in example 2. The other adsorbed proteins were eluted by increasing the NaCl concentration to 1.0 M.
- the preparation obtained by cation exchange chromatography contained or-glucuronidase activity but did not show any detectable -xylanase activity toward glucuronoxylan (Roth 7500) or j ⁇ -xylosidase activity toward p-nitrophenyl-jS-D-xylopyranosidase. In SDS-PAGE it showed a major band corresponding to a molecular weight of about 120 kDa.
- Example 4 Purification of an or-glucuronidase from Schizophyllum commune
- Schizophyllum commune VTT-E-88362 was cultivated in a bioreactor (Chemap CF 2000, working volume 16 1) on a medium containing 10 g l "1 wheat bran, 10 g l "1 Solka floe cellulase and 10 gl “1 distiller's spent grain, supplemented with 5 gl "1 KH 2 PO 4 and 5 gl “1 (NH 4 ) 2 SO 4 .
- Cultivation conditions were: temperature 30 °C, pH controlled between 4.0 and 6.0, aeration about 4 1 min "1 and cultivation time 8 days.
- the mycelium was separated by centrifiigation and the supernatant concentrated 15 times by ultrafiltration (PM- 10 membranes, Romicon).
- the solids were removed from the supernatant by centrifugation after which it was fractionated by anion exchange chromatography.
- the sample at pH 5.6 was applied to a column of DEAE Sepharose FF (Pharmacia), previously equilibrated with 50 mM sodium acetate buffer, pH 5.6, containing 0.05 moll "1 sodium chloride. Elution was performed first with the equilibrating buffer to remove unadsorbed proteins and thereafter with a linear addition of sodium chloride from 200 to 450 mM. Fractions which contained the ⁇ r- glucuronidase eluting during the NaCl gradient were combined for the next purification step by hydrophobic interaction chromatography. The other adsorbed proteins were eluted by increasing the NaCl concentration to 1.0 M.
- the sodium chloride concentration of the enzyme preparation obtained in the first chromatographic step was adjusted 1.5 M.
- the sample was applied to a column of Phenyl Sepharose FF (Pharmacia), previously equilibrated with 10 mM sodium acetate buffer, pH 5.5, containing 1.5 moll "1 NaCl. Elution was performed first with the equilibrating buffer and thereafter with a linear gradient of sodium chloride from 1.5 M to 0 M. Fractions which contained the or-glucuronidase eluted during the gradient of decreasing salt concentration were combined and concentrated by ultrafiltration. The other adsorbed proteins were eluted by 10 mM sodium acetate buffer and the column was washed with 6 M urea.
- the concentrated fractions from hydrophobic interaction chromatography were assayed for or- glucuronidase, ⁇ - ⁇ ,4-xylanase and jS-xylosidase with standard methods as described in example 2. These activities in the or-glucuronidase preparation were 133 nkat/ml for or- glucuronidase, 22 nkat nkat/ml for xylanase and below 1 nkat/ml for ⁇ -xylosidase.
- Birch pulp (kappa number 15.5) was treated with T. reesei glucuronidase at pH 5 in 50 mM acetate buffer for 4 h.
- the enzyme dose was 100 nkat/g.
- the reference pulp was incubated in the buffer for 4 h. After the treatment the pulps were washed with distilled water and the amount of carboxylic groups present in the pulp was determined by conductometric titration as described by Katz et al (1984). The results are presented in Table 3.
- Example 6 Peroxide bleaching of kraft pulp pretreated with glucuronidase.
- Birch kraft pulp with kappa number of 14.8 was treated with T. reesei glucuronidase for 4 h at 5 % consistency, pH 5.
- the pH of the pulp was adjusted with 5 N H 2 SO 4 .
- Reference pulp was incubated at the same pH without enzyme addition.
- the glucuronidase dose was 500 nkat/g. After the treatments the pulps were washed with distilled water and bleached with peroxide.
- the dosages of chemicals were: 3 % H 2 O 2 , 1.5 % NaOH, 0.5 % MgSO 4 , 0.2 % DTPA.
- the chemicals were dosed as % per o.d. pulp.
- the bleaching was carried out for 1 h at 10 % consistency.
- the bleaching temperature was 80 °C. After the bleaching the pulps were acidified and made into handsheets for the measurement of kappa number (SCAN Cl:1977), Brightness (ISO 2470) and viscosity (SCAN-C-15:1988). The results are given in Table 4.
- Birch kraft pulp (kappa 14.8) was converted to hydrogen (metal-free) form at 2 % consistency in 0.1 M HC1 at room temperature. The pulp was washed after the acidification. After washing the pH of the pulp was adjusted with 5 N NaOH to pH 5. Enzymatic treatments were carried out at 5 % consistency for 4 h at 45 °C. The enzyme dosages were: T. reesei xylanase pl 9 200 nkat/g; T. reesei glucuronidase 500 nkat/g. After or between the enzymatic treatments the pulps were washed and bleached as described in Example 6. Table 5. Xylanase treatment of pulps pretreated with glucuronidase
- xylanases do not act effciently on metal-free pulp.
- glucuronidase prior to the xylanase treatment, it is possible to improve the action of xylanase treatment by removing the carboxylic groups from pulp.
- Example 8 The effect of glucuronidase treatment on the paper technical properties of mechanical and chemical pulps.
- the paper technical properties of cellulose pulps can be modified by treating the bleached or unbleached pulp with glucuronidase thus resulting in total or partial removal of carboxylic acid (methylglucuronic acid) groups from the surface of the fibres.
- Example 9 The effect of Agaricus bisporus glucuronidase treatment on the brightness reversion of mechanical pulp
- CTMP ja PGW pulps were treated with Agaricus bisporus glucuronidase in 0.2 M sodium acetate buffer (pH 5) at 40 °C for 20 hours.
- Hand sheets (95 cm 2 ) made from the pulps were irradiated at 27 °C and 47 % relative humidity for 3 hours in a Xenotest 150 S apparatus (Heraeus Hanau) equipped with a xenon lamp, total output 1.3 kW.
- the reflectances (R, and R 2 ) of the samples were measured with an Elrepho reflectance photometer with a 457 nm brightness filter. Post-color values were calculated as described by Janson and Forsskahl (1989). The results are indicated in tables 6 (PGW) and 7. It appears that glucuronidase treatment reduced the yellowing (PC 2 values) of both pulps.
- PGW pulp suspended in water was treated with Trichoderma reesei glucuronidase and xylanase at 40 °C, pH 4.5 for 20 hours. Hand sheets were irradiated and post-color values calculated as in Example 9. The glucuronidase treatment reduced the yellowing (PC 2 value) of the pulp.
- Birch kraft pulp was treated with T. reesei xylanase (Tenkanen et al 1992) and glucuromdase as described in example 5.
- the xylanase dosage was 300 nkat/g.
- the degree of the hydrolysis of pulp xylan was followed by measuring the reducing sugars. The results are presented in Table 10.
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Abstract
Description
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Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
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JP5509857A JPH07501587A (en) | 1991-12-05 | 1992-12-07 | Cellulose pulp processing method and enzyme preparation |
EP92924742A EP0615564A1 (en) | 1991-12-05 | 1992-12-07 | Method and enzymatic preparation for treatment of cellulose pulps |
BR9206860A BR9206860A (en) | 1991-12-05 | 1992-12-07 | Enzymatic process and preparation for cellulose pulp treatment |
NO942071A NO942071L (en) | 1991-12-05 | 1994-06-03 | Enzyme preparation and method for treating cellulose pulp |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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FI915755A FI89613C (en) | 1991-12-05 | 1991-12-05 | Process for enzymatic treatment of cellulose pulp |
FI915755 | 1991-12-05 |
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WO1993011296A1 true WO1993011296A1 (en) | 1993-06-10 |
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PCT/FI1992/000332 WO1993011296A1 (en) | 1991-12-05 | 1992-12-07 | Method and enzymatic preparation for treatment of cellulose pulps |
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EP (1) | EP0615564A1 (en) |
JP (1) | JPH07501587A (en) |
AU (1) | AU3088292A (en) |
BR (1) | BR9206860A (en) |
CA (1) | CA2125166A1 (en) |
FI (1) | FI89613C (en) |
NO (1) | NO942071L (en) |
WO (1) | WO1993011296A1 (en) |
Cited By (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1995033883A1 (en) * | 1994-06-03 | 1995-12-14 | Valtion Teknillinen Tutkimuskeskus | Method and enzymatic preparation for treatment of cellulose pulps |
WO1996012063A1 (en) * | 1994-10-13 | 1996-04-25 | Ahlstrom Machinery Oy | Method for removal of hexenuronic acid groups in cellulose pulp by heat treatment |
WO1997027292A1 (en) * | 1996-01-22 | 1997-07-31 | Novo Nordisk A/S | An enzyme with xylanase activity |
WO1997043423A2 (en) * | 1996-05-10 | 1997-11-20 | Danisco A/S | Alpha-glucuronidases of aspergillus, production thereof and their uses |
WO2002092809A1 (en) * | 2001-05-11 | 2002-11-21 | Oji Paper Co., Ltd. | Novel hexenuronidase, gene coding for the same, and use of these |
US6776876B1 (en) | 1994-10-13 | 2004-08-17 | Andritz Oy | Method of treating cellulosic pulp to remove hexenuronic acid |
EP1688535A1 (en) * | 2005-02-08 | 2006-08-09 | Mitsubishi Gas Chemical Company, Inc. | Method for removing unsaturated uronic acid in chemical pulp for papermaking |
WO2009065199A1 (en) * | 2007-11-19 | 2009-05-28 | Universidade Federal Do Rio De Janeiro - Ufrj | Enzyme composition from trichoderma reesei and aspergillus awamori |
CN116102382A (en) * | 2023-02-01 | 2023-05-12 | 山东蓬勃生物科技有限公司 | Fungus encapsulated fertilizer, preparation method and application |
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1991
- 1991-12-05 FI FI915755A patent/FI89613C/en not_active IP Right Cessation
-
1992
- 1992-12-07 WO PCT/FI1992/000332 patent/WO1993011296A1/en not_active Application Discontinuation
- 1992-12-07 EP EP92924742A patent/EP0615564A1/en not_active Ceased
- 1992-12-07 BR BR9206860A patent/BR9206860A/en not_active Application Discontinuation
- 1992-12-07 CA CA 2125166 patent/CA2125166A1/en not_active Abandoned
- 1992-12-07 JP JP5509857A patent/JPH07501587A/en active Pending
- 1992-12-07 AU AU30882/92A patent/AU3088292A/en not_active Abandoned
-
1994
- 1994-06-03 NO NO942071A patent/NO942071L/en unknown
Non-Patent Citations (4)
Title |
---|
Dialog Information Services, File 240, 408554, Paperchem No: 57-08554, PULS, J. et al.: "Alpha-1,2-Glucuronidase in the Hydrolysis of Hemicellulose", Int. Conf. Biotechnol. Pulp & Paper Ind. (Stockholm) 3rd: 93-95 (June 16-19, 1986). * |
Dialog Information Services, File 240, 433162, Paperchem No: 58-13162, ISHIHARA, M. et al.: "Alpha-(1-2)-Glucuronidase in the Enzymatic Saccharification of Hardwood Xylan. (1). Screening of Alpha-Glucuronidase Producing Fungi", J. Japan Wood Res. Soc., 34, No. 1: 58-64 (1988). * |
Dialog Information Services, File 240, 481137, Paperchem No: 61-01137, POUTANEN, K. et al.: "Xylanolytic Enzyme System of Trichoderma Reesei", Plant Cell Wall Polymers Biogenesis & Biodegradation (ACS Symp. Ser. No. 399, Lewis & Paice, ed.)/Symp. 125th ACS Mtg., Chap. 46: 630-640, (Toronto, June 5-11, 1988, 1989). * |
Dialog Information Services, File 240, 513482, Paperchem No: 62-13482, POUTANEN, K. et al.: "Accessory Enzymes Involved in the Hydrolysis of Xylans", ACS Symp. Ser. No. 460, Chap. 33: 426-436 (April 1991). * |
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WO1995033883A1 (en) * | 1994-06-03 | 1995-12-14 | Valtion Teknillinen Tutkimuskeskus | Method and enzymatic preparation for treatment of cellulose pulps |
WO1996012063A1 (en) * | 1994-10-13 | 1996-04-25 | Ahlstrom Machinery Oy | Method for removal of hexenuronic acid groups in cellulose pulp by heat treatment |
US6776876B1 (en) | 1994-10-13 | 2004-08-17 | Andritz Oy | Method of treating cellulosic pulp to remove hexenuronic acid |
WO1997027292A1 (en) * | 1996-01-22 | 1997-07-31 | Novo Nordisk A/S | An enzyme with xylanase activity |
WO1997043423A2 (en) * | 1996-05-10 | 1997-11-20 | Danisco A/S | Alpha-glucuronidases of aspergillus, production thereof and their uses |
WO1997043423A3 (en) * | 1996-05-10 | 1998-02-05 | Danisco | Alpha-glucuronidases of aspergillus, production thereof and their uses |
US6558728B1 (en) | 1996-05-10 | 2003-05-06 | Danisco A/S | α-glucuronidases of aspergillus, production thereof and their uses |
WO2002092809A1 (en) * | 2001-05-11 | 2002-11-21 | Oji Paper Co., Ltd. | Novel hexenuronidase, gene coding for the same, and use of these |
EP1688535A1 (en) * | 2005-02-08 | 2006-08-09 | Mitsubishi Gas Chemical Company, Inc. | Method for removing unsaturated uronic acid in chemical pulp for papermaking |
WO2009065199A1 (en) * | 2007-11-19 | 2009-05-28 | Universidade Federal Do Rio De Janeiro - Ufrj | Enzyme composition from trichoderma reesei and aspergillus awamori |
CN116102382A (en) * | 2023-02-01 | 2023-05-12 | 山东蓬勃生物科技有限公司 | Fungus encapsulated fertilizer, preparation method and application |
CN116102382B (en) * | 2023-02-01 | 2024-03-26 | 山东蓬勃生物科技有限公司 | Fungus encapsulated fertilizer, preparation method and application |
Also Published As
Publication number | Publication date |
---|---|
BR9206860A (en) | 1995-11-28 |
AU3088292A (en) | 1993-06-28 |
JPH07501587A (en) | 1995-02-16 |
CA2125166A1 (en) | 1993-06-10 |
FI89613B (en) | 1993-07-15 |
FI915755A0 (en) | 1991-12-05 |
EP0615564A1 (en) | 1994-09-21 |
NO942071L (en) | 1994-07-26 |
FI89613C (en) | 1993-10-25 |
NO942071D0 (en) | 1994-06-03 |
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