JPH03505758A - Method for bleaching cellulose pulp - Google Patents
Method for bleaching cellulose pulpInfo
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- JPH03505758A JPH03505758A JP1502856A JP50285689A JPH03505758A JP H03505758 A JPH03505758 A JP H03505758A JP 1502856 A JP1502856 A JP 1502856A JP 50285689 A JP50285689 A JP 50285689A JP H03505758 A JPH03505758 A JP H03505758A
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- pulp
- bleaching
- chlorine
- enzyme
- treatment
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- 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
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- 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
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- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Paper (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Chemical And Physical Treatments For Wood And The Like (AREA)
- Hard Magnetic Materials (AREA)
- Agricultural Chemicals And Associated Chemicals (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Detergent Compositions (AREA)
Abstract
Description
【発明の詳細な説明】 セルロースバルブを漂白するための方法本発明は、広葉樹木材から得られるセル ロースバルブを、塩素を含有する漂白剤を用いて漂白するための方法に関する。[Detailed description of the invention] A method for bleaching cellulose bulbs. The present invention relates to a method for bleaching roast valves using a bleaching agent containing chlorine.
硫酸塩蒸解により得られるセルロースバルブは特に褐色であるが、これは主にバ ルブ中に残存するリグニンによるものである。現在では、この残存リグニンはヘ ミセルロースと共有結合で結合していると考えられている。The cellulose bulb obtained by sulphate digestion is particularly brown in color, which is mainly due to the This is due to the lignin remaining in the rub. Currently, this residual lignin is It is thought to be covalently bonded to micellulose.
漂白によりリグニンが除去され、上質紙や部組製品として使用可能となる。Bleaching removes the lignin, making it possible to use it as high-quality paper or other products.
通常漂白は多段階の工程で行なわれ、酸化剤、リグニン分解剤、及び分解生成物 として生じた物質を溶解する薬剤で交互にバルブが処理される。塩素を含有しな い別種の酸化漂白剤も知られてはいるが、酸化剤としてはとりわけて、純粋な塩 素ガス、二酸化塩素、次亜鉛素酸ナトリウムまたはカリウムの様な塩素を含有す る物質が使用されてきた。分解生成物を除去する抽出剤としては、アルカリ溶液 が使われてきた。Bleaching is usually a multi-step process that uses oxidizing agents, lignin-degrading agents, and decomposition products. The valves are alternately treated with agents that dissolve the resulting substances. Contains no chlorine Although other types of oxidizing bleaches are known, pure salt is the most important oxidizing agent. Chlorine containing gas, chlorine dioxide, sodium or potassium subzinc oxide substances have been used. An alkaline solution is used as an extractant to remove decomposition products. has been used.
反応の過程では、塩素含有薬剤は、バルブ中に存在する脂肪酸や樹脂酸のみなら ずリグニンをも塩素化する。In the process of reaction, chlorine-containing chemicals are only present in fatty acids and resin acids. It also chlorinates lignin.
したがって、漂白工程でリグニンからはりOロワエノール類が生じ、バルブ中か ら漂白廃液中へ放出される。塩素は更に、漂白完了後にセルロースバルブ中に残 存するリグニンや酸の残留物に結合している。近年にわかにこの残留塩素は、こ のバルブから作られた紙や厚紙製品が廃棄された際に相の環境を汚染するものと してみなされる様になり、近い将来、バルブ中の塩素含有饅が制限される見通し が出てきた。食品包装用厚紙は廃棄物焼却設備やこみ捨場に投棄されるので、用 いられるバルブにはこの様な制限が渠される可能性が高い。この問題は特に、カ バやユーカリ材の様な塩素含有抽出成分の含有量が高い広葉樹木材から作られた バルブの場合に深刻である。Therefore, during the bleaching process, lignin generates O-lowenols, which may be present in the bulb. is released into the bleach wastewater. Chlorine also remains in the cellulose bulb after bleaching is complete. It is bound to existing lignin and acid residues. In recent years, this residual chlorine has suddenly increased. Paper and cardboard products made from these valves do not pollute the environment when disposed of. It is expected that chlorine-containing rice in valves will be restricted in the near future. came out. Cardboard for food packaging is disposed of in waste incineration facilities and garbage dumps, so it should not be used. There is a high possibility that such restrictions will be imposed on valves that can be used. This problem is particularly Made from hardwoods with a high content of chlorine-containing extractives, such as oak and eucalyptus. Serious in case of valves.
本発明の目的は、広葉樹木材から作られた漂白セルロースバルブの残留塩素含有 量を現在のレベルより低減させることにより、前記問題点を解決することにある 。本発明は、バルブに酵素処理を施すことにより残留塩素含有量を低減すること を特徴とする。The purpose of this invention is to improve the residual chlorine content of bleached cellulose bulbs made from hardwood materials. The aim is to solve the above problems by reducing the amount from the current level. . The present invention reduces the residual chlorine content by subjecting the valve to enzyme treatment. It is characterized by
酵素の使用によりセルロースからリグニンを除去することが可能であることは、 早期の研究で既に認められていた。これから得られる結論としては、蒸解工程で 得られたバルブを先ず酵素で処理1れば、続いて行なわれる漂白工程での塩素含 有漂白剤の使用を、部分的にまたは全体的にさえも省くことができるということ である。本発明においては、酵素処理を実質的に従来と同様な塩素薬剤を用いた 漂白法と組み合わせることにより、得られるバルブ中の残留塩素含有量が、酵素 処理が行われなかった場合より低減されることが見出された。The possibility of removing lignin from cellulose by the use of enzymes It was already recognized in early studies. The conclusion that can be drawn from this is that in the cooking process The resulting bulbs are first treated with enzymes1 to remove chlorine from the subsequent bleaching process. The fact that the use of bleaching agents can be partially or even completely omitted It is. In the present invention, the enzymatic treatment is performed using substantially the same chlorine agent as in the conventional method. By combining with the bleaching method, the residual chlorine content in the resulting valve can be reduced by enzymes. It was found that the reduction was lower than that without the treatment.
本発明に従えば、漂白工程の任意の段階で酵素処理を行なうことができる。よっ て、バルブの酵素処理は、該工程中の酸化段階または抽出段階のうちの一つと組 み合わせて行うこともできるし、これらの各段階の間で行うこともでき、漂白工 程に先立って行ってもよく、これらの段階の後に行ってもよい。用いられる酵素 は、ヘミセルラーゼ、セルラーゼ、エステラーゼまたはこれらの混合物が好まし く、好適な酵素製品としては、HultifektL250及びHultife kt Kが挙げられる。H素処Nの’//A度は、10〜90℃の範囲内で行う ことができるが、40〜70℃の範囲内で行なうことが好ましく、pHは3.0 〜7.5、好ま()くは4.0〜6.0の範囲内で処理を行うことができる。According to the present invention, enzyme treatment can be carried out at any stage of the bleaching process. Okay In this case, the enzymatic treatment of the valve is combined with one of the oxidation or extraction steps in the process. It can be carried out together or between each of these stages, and the bleaching process This step may be performed prior to or after these steps. enzyme used is preferably a hemicellulase, cellulase, esterase or a mixture thereof. Suitable enzyme products include Hultifekt L250 and Hultife. kt K is mentioned. The temperature of H elementary treatment N is within the range of 10 to 90°C. However, it is preferably carried out within the range of 40 to 70°C, and the pH is 3.0. The treatment can be carried out within the range of 7.5 to 7.5, preferably 4.0 to 6.0.
本発明の更なる目的は、広葉樹木材から作られた漂白セルロースバルブの残留塩 素含有量を低減するための酵素の使用にある。好適な酵素としては、ヘミセルラ ーゼ類、セルラーゼ類、エステラーゼ類またはこれらの混合物、例えば酵素製品 Mu目1fekt L 250及びHultifektKが挙げられる。本発明 に従えば、r!s素は前述の漂白工程と同様にして用いられる。A further object of the invention is to provide a bleached cellulose bulb made from hardwood wood with residual salts. It consists in the use of enzymes to reduce the elemental content. Suitable enzymes include hemicellular enzymes, cellulases, esterases or mixtures thereof, e.g. enzyme products Examples include Mu order 1fekt L 250 and HultifektK. present invention If you follow, r! The sulfur element is used in the same manner as in the bleaching process described above.
特に具体的に言えば、本発明の教示する酵素の使用は、食品包装用の厚紙または 紙に加工されるべき漂白セル[J−スバルブの残留塩素含有量の低減に関する。Particularly specifically, the use of enzymes as taught by the present invention can be applied to cardboard for food packaging or Concerning the reduction of the residual chlorine content of bleaching cells [J-subalve] to be processed into paper.
その理由は、前記のF9紙や紙は廃棄物焼却設@マ処理される廃棄物となり、こ れらに塩素が含まれる場合には、燃焼時に猛毒のダイオキシンを生成するため、 残留塩素含有量に関して特に厳しい規制が果せられようとしてるからである。The reason for this is that the above-mentioned F9 papers and papers are treated as waste at waste incineration facilities. If these contain chlorine, they produce highly poisonous dioxins when burned. Particularly strict regulations regarding residual chlorine content are about to be implemented.
本発明で用いられる様々なカテゴリーの酵素の好適な酵素活性度は、以Fの範囲 内である。(Uは活性度の単位である。) ヘミセルラーゼ類: 例えばキシ5tゼ 質量1布あたり0〜10tJ”β−キシロシダーゼ O〜20,0OOU ”エステラーゼ類: 0〜100,0OOLJセルラーぜ類: フィルターペーパー活性度 〃 0〜20,0OOLI ”CMC活性度 〃 O〜500,0OOU ”β−グル」シダーゼ 0〜20.0OOU ”β−グルカナーゼ 〃 O〜5 00,0OOLJ 6)1) にhan、 A、l’1.、 Trelblay 、 D、、 LeDuy 、^、、 EnZyleHicrob、 Techn ol、、 8 (19861373−3772) F、 Delyn、 H, C1aeyssens、 J、 van Beeumen、 C,に。Suitable enzyme activities for the various categories of enzymes used in the present invention are in the following ranges: It is within. (U is the unit of activity.) Hemicellulases: For example, xylosidase 0 to 10 tJ” β-xylosidase per mass of cloth O ~ 20OOU "Esterase: 0~100,0OOLJ Cellulose: Filter paper activity 0~20,0OOLI"CMC activity 〃〃 0-20.0OOU” β-glucanase 00,0OOLJ 6) 1) han, A, l'1. , Trelblay , D, , LeDuy , ^, , EnZyleHicrob, Techn ol,, 8 (19861373-3772) F, Delyn, H, In C1aeyssens, J. and van Beemen, C.
de Bruyne、 Can、 J、 Biochei 5643 (198 7)3) Ghose、 T、に、、 Patnak、 八、N、、 B15aria、 V、S、。de Bruyne, Can, J, Biochei 5643 (198 7) 3) Ghose, T, Ni, Patnak, Eight, N,, B15aria, V, S,.
Sya+postum of Enzyiatic Hydrolysis o f Ce1lulose。Sya+postum of Enzyiatic Hydrolysis o f Ce1lulose.
Ba1ley、 H,、[nari、 T、 M、、 Linko 、 H,、 Eds。Balley, H,, [nari, T, M,, Linko, H,, Eds.
(SITRA、 Au1anko、 Finland、 1975)、 1 11−1364) Handels、 H,、Weber、 J、、Adv、 Chew、 Ser、 955) Ber□hem、Ler、pette rsson、Eur 、J、B10Chell 376) Sugar determination: Miller、G 、L、、Anal 、 Ches。(SITRA, Au1anko, Finland, 1975), 1 11-1364) Handels, H., Weber, J., Adv. Chew, Ser, 955) Ber□hem, Ler, pette rsson, Eur, J, B10Chell 376) Sugar Determination: Miller, G, L, Anal , Ches.
以下、実験結果に基づき2つの実施態様例を用いて、本発明をより詳細に説明す る。The present invention will be explained in more detail below using two embodiment examples based on experimental results. Ru.
実施例1 カバ材のTaM塩蒸解(バルブの乾燥重鰻含有率10%)から得られた乾燥バル ブ2209を、pH5の5+Hの硝酸ナトリウム緩衝液中に、混合物の最終濃度 が2.5%となる様に懸濁させた。酵素Hultifekt Kを、混合物のキ シラナーゼ活性度が乾燥パルプ1gあたり56LJとなる様に添加した。酵素処 理時の温度は39℃であり、処理時間は20時間とした。酵素処理後、ブツフナ ー漏斗でバルブを漏集し、こうして得られたバルブケーキを洗浄比(washi ng ratto )が28となる様にイオン交換水で洗浄した。Example 1 Dry bar obtained from TaM salt cooking of birch wood (dry barb content of barb 10%) 2209 in 5+H sodium nitrate buffer at pH 5 to the final concentration of the mixture. was suspended so that the concentration was 2.5%. Add the enzyme Hultifekt K to the mixture. It was added so that the silanase activity was 56 LJ per gram of dry pulp. Enzyme treatment The temperature during treatment was 39° C., and the treatment time was 20 hours. Buthufuna after enzyme treatment - Collect the valves in a funnel and wash the valve cake thus obtained. It was washed with ion-exchanged water so that the ng ratto was 28.
対照として、同様のバルブバッチに酵素を加えることなく同様の処理を行った。As a control, a similar batch of valves was subjected to a similar treatment without the addition of enzyme.
この処理工程において前記2種のバルブバッチについて測定を行った結果を第1 8表に示す。In this treatment step, the results of measurements on the two types of valve batches are shown in the first It is shown in Table 8.
第1a表 酵素処理 酵素処理なし く対照バッチ) カッパー価 16.8 21DKM抽出物含有量 0.27 0.23(乾燥分の%) 稠度(dm /ll) 1065 1280醇素処理パルプのバ ッチと比較のバッチは、次に5段階の連続鹸化と抽出段階にかけられる。薬剤と しては、第1の段階では塩素と二酸化塩素が、第2の段階では水酸化ナトリウム が、第3の段階では二酸化塩素が、第4の段階では水酸化ナトリウムが、第5の 段階では二酸化塩素が使用された。次の第1b表には、漂白に使われた塩素の総 量と漂白バルブのバッチを測定した結果が示されている。Table 1a Enzyme treatment No enzyme treatment control batch) Kappa number 16.8 21DKM extract content 0.27 0.23 (% of dry matter) Consistency (dm/ll) 1065 1280 Soluble treated pulp The batch and comparison batches were then subjected to five consecutive saponification and extraction stages. drugs and In the first stage, chlorine and chlorine dioxide are added, and in the second stage, sodium hydroxide is added. However, in the third stage chlorine dioxide, in the fourth stage sodium hydroxide, and in the fifth stage Chlorine dioxide was used in the step. Table 1b below shows the total amount of chlorine used in bleaching. The results of measuring the amount and batch of bleach bulbs are shown.
第1b表 酵素処理 酵素処理なし く対照バッチ) 活性塩素使用量 (乾燥パルプ19 33.6 42あたりの■数) (2Xカツパー) 収率 93.6% 97.5%DKH抽出物含抽出物 含有物の% 0.26 0.29稠度(dl /醇) 1035 1210残留塩素含有罎 (my/sN 0.845 1.270この結果から明ら かな様に、酵素処理されたセルロースバルブは、酵素処理されていないバルブに 比べて漂白後の残留塩素含有量が明らかに低い。更に、酵素処理バルブにおいて 強度の値が有意に低下することがないこともわかる。Table 1b Enzyme treatment No enzyme treatment control batch) Active chlorine consumption (Number of ■ per dry pulp 19 33.6 42) (2X cutlet par) Yield 93.6% 97.5% Extract containing DKH extract % of inclusions 0.26 0.29 Consistency (dl / 醇) 1035 1210 Residual chlorine containing bottle (my/sN 0.845 1.270 It is clear from this result that Like Kana, enzyme-treated cellulose valves are different from non-enzyme-treated valves. In comparison, the residual chlorine content after bleaching is clearly lower. Furthermore, in enzyme-treated valves It can also be seen that the intensity values do not decrease significantly.
実施例2 本実験では、カバ材の硫?[蒸解で桿られた3つのバルブバッチが用いられた。Example 2 In this experiment, birch wood sulfur? [Three bulb batches from the cooker were used.
これらのバルブバッチは、先の実施例1と同じ稠度を有しており、2つのバッチ は前述の様な酵素処理が施され、もう1つのバッチは対照バッチとした。酵素は 実施例1で用いられたものと次の点で異っていた。即ち、あるバッチ(バッチ1 )では、混合物について乾燥パルプ1gあたりのキシラナーゼ活性度を56tJ としたのに加えて、乾燥パルプ1gあたりのセルラーゼ活性度を1.5Uとした 。もう1つのバッチ(バッチ2)では、乾燥パルプ17あたりのキシラナーゼ活 性度を56tJとしたのに加えて、乾燥パルプ1gあたつのセルラーゼ活性度を 1.1Uとした。酵素処理後の結果を第1Ia表に示す。These valve batches had the same consistency as in Example 1 above, and the two batches were subjected to enzyme treatment as described above, and the other batch served as a control batch. The enzyme is It differed from that used in Example 1 in the following points. That is, a certain batch (batch 1 ), the xylanase activity per 1 g of dry pulp for the mixture is 56 tJ. In addition, the cellulase activity per 1 g of dry pulp was set at 1.5 U. . In another batch (batch 2), xylanase activity per dry pulp 17 In addition to setting the cellulase activity to 56 tJ, the cellulase activity per gram of dry pulp was It was set to 1.1U. The results after enzyme treatment are shown in Table 1Ia.
第[a表 酵素前処理 酵素前処理 酵素処理なしくバッチ1) (バッチ2) ( 対照バッチ)カッパー価 15.8 15.0 18.8DKH抽出物 含有量(乾燥 0.32 0.32 0.26分の%) 稠度 (da /#) 102.5 1130 130 5次いで、これらのバルブバッチを実施例1と同様に塩素薬剤と水酸化ナトリウ ムを用いて漂白した。各々の場合、塩素の総使用量(■/9)はカッパー価の2 倍とした。漂白後の結果を第nb表に示す。Table [a] Enzyme pretreatment Enzyme pretreatment Without enzyme treatment Batch 1) (Batch 2) ( Control batch) Kappa number 15.8 15.0 18.8 DKH extract Content (% of dry 0.32 0.32 0.26 min) consistency (da /#) 102.5 1130 130 5 These valve batches were then treated with a chlorine agent and sodium hydroxide in the same manner as in Example 1. Bleached using bleach. In each case, the total amount of chlorine used (■/9) is 2 of the kappa number. It was doubled. The results after bleaching are shown in Table nb.
第nb表 酵素IFJ 511!理 酸素前処理 酵素処理なしDKH抽出物 含有量(乾燥 0.36 0.35 0.37分の%) 稠度 (di+ /Kf) 980 1065 1210塩素の総合有量 この場合の結果からもわかる様に、漂白バルブの残留塩素含有量は酵素処理によ り有意に低減される。Table nb Enzyme IFJ 511! Process Oxygen pretreatment DKH extract without enzyme treatment Content (% of dry 0.36 0.35 0.37 minutes) consistency (di+ /Kf) 980 1065 1210 Total amount of chlorine As can be seen from the results in this case, the residual chlorine content of the bleach valve can be reduced by enzymatic treatment. significantly reduced.
実施例3 本実験ではカバの硫酸塩法バルブが漂白して用いられた。このバルブの漂白は、 漂白剤として第1の段階では塩素(90%)と二酸化塩素(10%)を、第2の 段階では水酸化ナトリウムを、第3の段階では酸素を用いて行った。Example 3 In this experiment, a bleached birch sulfate valve was used. The bleaching of this bulb is In the first step, chlorine (90%) and chlorine dioxide (10%) are used as bleaching agents, and in the second step, chlorine (90%) and chlorine dioxide (10%) are used. The first stage was carried out with sodium hydroxide and the third stage with oxygen.
この漂白バルブを、実施例1と同じ酵素を用いて同じ条件で酵素処理した。処理 後、バルブを水洗し室温で乾燥した。酵素処理バルブと未処理、即ち初めの漂白 硫酸塩法パルプの両方について、残留塩素含有量を測定した結果、前者は1.1 8、後者は1.56■/9であった。This bleached bulb was enzymatically treated using the same enzyme and under the same conditions as in Example 1. process After that, the bulb was washed with water and dried at room temperature. Enzyme treated valve and untreated, i.e. initial bleaching As a result of measuring the residual chlorine content of both sulfate method pulps, the former was 1.1 8, the latter was 1.56/9.
この様に、酵素処理により漂白バルブの残留塩素含有量を有意に低下させること ができた。Thus, the residual chlorine content of bleach valves can be significantly reduced by enzymatic treatment. was completed.
この試験により、セルロースバルブを先ず漂白しその後にのみ酵素で処理した場 合でも、本発明の望ましい結果が得られることが立証される。This test showed that cellulose bulbs were bleached first and only then treated with enzymes. It has been demonstrated that the desired results of the present invention can be obtained even when
本発明の他の実施態様が、以上に例として示したものに限定されることはなく、 以下に示す請求の範囲内で変更し得ることは、当業者には明らかである。例えば 、一般的な5段階塩素漂白の第1の段階では、塩素単独、または塩素を二酸化塩 素と混合して用いることができる。Other embodiments of the invention are not limited to those shown by way of example above, It will be apparent to those skilled in the art that modifications may be made within the scope of the claims below. for example , the first step of a typical five-step chlorine bleach process involves using chlorine alone or adding chlorine to salt dioxide. It can be used by mixing with the base.
また、酵素を作用させる時間を、前述の20時間より大幅に短縮することもでき る。用いる酵素とその活性麿に応じて、処理時間を数時間、更には1時間以下に することも考えられる。In addition, the time for the enzyme to act can be significantly shortened from the 20 hours mentioned above. Ru. Depending on the enzyme used and its activity level, the treatment time can be several hours or even less than an hour. It is also possible to do so.
国際調査報告international search report
Claims (10)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FI881192A FI81395B (en) | 1988-03-14 | 1988-03-14 | FOERFARANDE FOER BLEKNING AV CELLULOSAMASSA. |
FI881192 | 1988-03-14 |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH03505758A true JPH03505758A (en) | 1991-12-12 |
Family
ID=8526077
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP1502856A Pending JPH03505758A (en) | 1988-03-14 | 1989-03-13 | Method for bleaching cellulose pulp |
Country Status (12)
Country | Link |
---|---|
EP (1) | EP0407421B1 (en) |
JP (1) | JPH03505758A (en) |
AT (1) | ATE135429T1 (en) |
AU (1) | AU626846B2 (en) |
BR (1) | BR8907314A (en) |
CA (1) | CA1334581C (en) |
DE (1) | DE68925967T2 (en) |
DK (1) | DK175185B1 (en) |
FI (1) | FI81395B (en) |
NO (1) | NO174722C (en) |
NZ (1) | NZ228308A (en) |
WO (1) | WO1989008738A1 (en) |
Families Citing this family (21)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5298405A (en) * | 1986-04-30 | 1994-03-29 | Alko Limited | Enzyme preparations with recombinantly-altered cellulose profiles and methods for their production |
FI90888B (en) * | 1989-02-14 | 1993-12-31 | Enso Gutzeit Oy | Method for bleaching cellulose pulp |
FI86896B (en) * | 1989-05-04 | 1992-07-15 | Enso Gutzeit Oy | FOERFARANDE FOER BLEKNING AV CELLULOSAMASSA. |
DK420289D0 (en) * | 1989-08-25 | 1989-08-25 | Novo Nordisk As | METHOD OF TREATING LIGNOCELLULOSE PULP |
NZ235679A (en) * | 1989-10-18 | 1993-01-27 | Int Paper Co | Bleaching lignocellulosic pulp using (a) treatment with xylanase and (b) one or more chemical bleaching stages |
SE465320B (en) * | 1990-01-10 | 1991-08-26 | Korsnaes Ab | PREPARATIONS SUBMITTING ENZYMATIC DELIGNIFICATION ACTIVITY, MADE TO MAKE THE SAME AND APPLICATIONS THEREOF |
FI88315C (en) * | 1990-04-04 | 1993-04-26 | Enso Gutzeit Oy | FOERFARANDE FOER BLEKNING AV CELLULOSAMASSA |
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 |
NZ239500A (en) * | 1990-08-24 | 1993-08-26 | Novo Nordisk As | Xylanases obtained from bacillus pumilus and use in a lignocellulosic chemical pulping process |
DE4129739A1 (en) * | 1990-09-11 | 1992-03-12 | Sandoz Ag | Chlorine-free bleaching of paper pulp |
FI108800B (en) * | 1991-05-07 | 2002-03-28 | Iogen Corp | A method and apparatus for using an enzyme in the manufacture and bleaching of pulp |
US5369024A (en) * | 1992-03-25 | 1994-11-29 | The United States Of America As Represented By The Secretary Of Agriculture | Xylanase from streptomyces roseiscleroticus NRRL-11019 for removing color from kraft wood pulps |
US5498534A (en) * | 1992-03-25 | 1996-03-12 | The United States Of America As Represented By The Secretary Of Agriculture | Method of removing color from wood pulp using xylanase from streptomyces roseiscleroticus NRRL B-11019 |
US5871730A (en) * | 1994-07-29 | 1999-02-16 | Universite De Sherbrooke | Thermostable xylanase DNA, protein and methods of use |
US6300114B1 (en) | 1994-07-29 | 2001-10-09 | Rohm Enzyme Finland Oy | Sequences of xylanase and xylanase expression vectors |
US5935836A (en) * | 1994-07-29 | 1999-08-10 | Rohm Enzyme Finland Oy | Actinomadura xylanase sequences 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 |
WO2002057541A2 (en) | 2001-01-18 | 2002-07-25 | Iogen Bio-Products Corporation | Use of xylanase in pulp bleaching |
WO2003074780A1 (en) * | 2002-03-06 | 2003-09-12 | Iogen Bio-Products Corporation | Xylanase treatment of chemical pulp |
CN104963206A (en) * | 2014-12-11 | 2015-10-07 | 华东理工常熟研究院有限公司 | Enzyme modified paper pulp fiber, wood-plastic composite material and preparation method thereof |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
NZ216726A (en) * | 1985-07-15 | 1990-08-28 | Repligen Corp | Use of lignin-degrading enzymes from phanerochaete chrysosporium for treatment of wood pulp and e1 effluent |
ZA894239B (en) * | 1988-06-08 | 1990-03-28 | Int Paper Co | Enzymatic delignification of lignocellulosic material |
EP0373107B1 (en) * | 1988-11-23 | 1994-03-23 | Sandoz Ag | Use of enzymes of Aureobasidium pullulans in pulp bleaching |
-
1988
- 1988-03-14 FI FI881192A patent/FI81395B/en not_active Application Discontinuation
-
1989
- 1989-03-13 DE DE68925967T patent/DE68925967T2/en not_active Revoked
- 1989-03-13 EP EP89903748A patent/EP0407421B1/en not_active Revoked
- 1989-03-13 BR BR898907314A patent/BR8907314A/en not_active IP Right Cessation
- 1989-03-13 AU AU32923/89A patent/AU626846B2/en not_active Ceased
- 1989-03-13 WO PCT/FI1989/000045 patent/WO1989008738A1/en not_active Application Discontinuation
- 1989-03-13 CA CA000593523A patent/CA1334581C/en not_active Expired - Lifetime
- 1989-03-13 NZ NZ228308A patent/NZ228308A/en unknown
- 1989-03-13 AT AT89903748T patent/ATE135429T1/en active
- 1989-03-13 JP JP1502856A patent/JPH03505758A/en active Pending
-
1990
- 1990-09-04 DK DK199002119A patent/DK175185B1/en not_active IP Right Cessation
- 1990-09-07 NO NO903913A patent/NO174722C/en not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
ATE135429T1 (en) | 1996-03-15 |
DK211990A (en) | 1990-11-07 |
WO1989008738A1 (en) | 1989-09-21 |
BR8907314A (en) | 1991-03-19 |
NZ228308A (en) | 1990-06-26 |
DE68925967T2 (en) | 1996-09-12 |
NO174722C (en) | 1994-06-22 |
FI881192A0 (en) | 1988-03-14 |
AU626846B2 (en) | 1992-08-13 |
NO903913L (en) | 1990-09-07 |
DK175185B1 (en) | 2004-06-28 |
NO903913D0 (en) | 1990-09-07 |
NO174722B (en) | 1994-03-14 |
EP0407421A1 (en) | 1991-01-16 |
DE68925967D1 (en) | 1996-04-18 |
CA1334581C (en) | 1995-02-28 |
DK211990D0 (en) | 1990-09-04 |
FI81395B (en) | 1990-06-29 |
EP0407421B1 (en) | 1996-03-13 |
FI881192A (en) | 1989-09-15 |
AU3292389A (en) | 1989-10-05 |
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