JPH02160984A - Deinking method of waste paper - Google Patents
Deinking method of waste paperInfo
- Publication number
- JPH02160984A JPH02160984A JP63310240A JP31024088A JPH02160984A JP H02160984 A JPH02160984 A JP H02160984A JP 63310240 A JP63310240 A JP 63310240A JP 31024088 A JP31024088 A JP 31024088A JP H02160984 A JPH02160984 A JP H02160984A
- Authority
- JP
- Japan
- Prior art keywords
- deinking
- lipase
- waste paper
- aspergillus oryzae
- pulp
- 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.)
- Pending
Links
- 239000002761 deinking Substances 0.000 title claims abstract description 39
- 238000000034 method Methods 0.000 title claims description 21
- 239000010893 paper waste Substances 0.000 title abstract description 19
- 239000004367 Lipase Substances 0.000 claims abstract description 30
- 108090001060 Lipase Proteins 0.000 claims abstract description 30
- 102000004882 Lipase Human genes 0.000 claims abstract description 30
- 235000019421 lipase Nutrition 0.000 claims abstract description 30
- 239000000126 substance Substances 0.000 claims abstract description 13
- 240000006439 Aspergillus oryzae Species 0.000 claims abstract description 7
- 235000002247 Aspergillus oryzae Nutrition 0.000 claims abstract description 7
- 241000223258 Thermomyces lanuginosus Species 0.000 claims abstract description 4
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 4
- 230000007935 neutral effect Effects 0.000 claims abstract 3
- 102000003886 Glycoproteins Human genes 0.000 claims description 2
- 108090000288 Glycoproteins Proteins 0.000 claims description 2
- 125000005457 triglyceride group Chemical group 0.000 claims 1
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 abstract description 18
- 230000000694 effects Effects 0.000 abstract description 11
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 abstract description 10
- 239000000835 fiber Substances 0.000 abstract description 9
- 235000011121 sodium hydroxide Nutrition 0.000 abstract description 6
- 239000004115 Sodium Silicate Substances 0.000 abstract description 5
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 abstract description 5
- 229910052911 sodium silicate Inorganic materials 0.000 abstract description 5
- 230000006866 deterioration Effects 0.000 abstract 1
- 239000000976 ink Substances 0.000 description 7
- 238000007639 printing Methods 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 4
- 108010059892 Cellulase Proteins 0.000 description 4
- 229940106157 cellulase Drugs 0.000 description 4
- 238000005188 flotation Methods 0.000 description 4
- WRIDQFICGBMAFQ-UHFFFAOYSA-N (E)-8-Octadecenoic acid Natural products CCCCCCCCCC=CCCCCCCC(O)=O WRIDQFICGBMAFQ-UHFFFAOYSA-N 0.000 description 3
- LQJBNNIYVWPHFW-UHFFFAOYSA-N 20:1omega9c fatty acid Natural products CCCCCCCCCCC=CCCCCCCCC(O)=O LQJBNNIYVWPHFW-UHFFFAOYSA-N 0.000 description 3
- QSBYPNXLFMSGKH-UHFFFAOYSA-N 9-Heptadecensaeure Natural products CCCCCCCC=CCCCCCCCC(O)=O QSBYPNXLFMSGKH-UHFFFAOYSA-N 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- ZQPPMHVWECSIRJ-UHFFFAOYSA-N Oleic acid Natural products CCCCCCCCC=CCCCCCCCC(O)=O ZQPPMHVWECSIRJ-UHFFFAOYSA-N 0.000 description 3
- 239000005642 Oleic acid Substances 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- QXJSBBXBKPUZAA-UHFFFAOYSA-N isooleic acid Natural products CCCCCCCC=CCCCCCCCCC(O)=O QXJSBBXBKPUZAA-UHFFFAOYSA-N 0.000 description 3
- 239000003921 oil Substances 0.000 description 3
- ZQPPMHVWECSIRJ-KTKRTIGZSA-N oleic acid Chemical compound CCCCCCCC\C=C/CCCCCCCC(O)=O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerol Natural products OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- UYXTWWCETRIEDR-UHFFFAOYSA-N Tributyrin Chemical compound CCCC(=O)OCC(OC(=O)CCC)COC(=O)CCC UYXTWWCETRIEDR-UHFFFAOYSA-N 0.000 description 2
- 239000002280 amphoteric surfactant Substances 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- 239000003945 anionic surfactant Substances 0.000 description 2
- 239000007844 bleaching agent Substances 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000002270 dispersing agent Substances 0.000 description 2
- 235000019197 fats Nutrition 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 239000002736 nonionic surfactant Substances 0.000 description 2
- 238000007645 offset printing Methods 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- OYHQOLUKZRVURQ-NTGFUMLPSA-N (9Z,12Z)-9,10,12,13-tetratritiooctadeca-9,12-dienoic acid Chemical compound C(CCCCCCC\C(=C(/C\C(=C(/CCCCC)\[3H])\[3H])\[3H])\[3H])(=O)O OYHQOLUKZRVURQ-NTGFUMLPSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000854711 Shinkai Species 0.000 description 1
- 239000004164 Wax ester Substances 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 239000012752 auxiliary agent Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 description 1
- 239000000920 calcium hydroxide Substances 0.000 description 1
- 229910001861 calcium hydroxide Inorganic materials 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000007644 letterpress printing Methods 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 235000019386 wax ester Nutrition 0.000 description 1
- 230000003313 weakening effect Effects 0.000 description 1
Classifications
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02W—CLIMATE CHANGE MITIGATION TECHNOLOGIES RELATED TO WASTEWATER TREATMENT OR WASTE MANAGEMENT
- Y02W30/00—Technologies for solid waste management
- Y02W30/50—Reuse, recycling or recovery technologies
- Y02W30/64—Paper recycling
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
この発明は、古紙再生のための脱インキ方法に関し、よ
り詳しくは、古紙を脱インキ薬品で処理して脱インキを
行うに際し、リパーゼを用いて脱インキ効果を高める方
法に関する。[Detailed Description of the Invention] [Field of Industrial Application] The present invention relates to a deinking method for recycling used paper, and more specifically, when deinking waste paper by treating it with a deinking chemical, lipase is used. This invention relates to a method for increasing the deinking effect.
新聞、雑誌などの古紙は、通常、脱インキ薬品で脱イン
キ処理を行ったうえ、再生利用されている。脱インキ薬
品は、一般に、カセイソーダ、炭酸ソーダ、ケイ酸ソー
ダなどのアルカリ剤、アニオン、ノニオンもしくは両性
界面活性剤の中から選ばれた一種または二種以上の界面
活性剤、過酸化水素などの漂白剤、ならびにｐＨ安定剤
、分散剤などの助剤からなる。脱インキ薬品を用いて、
フローテーション法、水洗浄法またはフローテーション
／水洗浄法によってパルプとインキとが分離され、脱イ
ンキバルブが紙の製造に利用される。Used paper such as newspapers and magazines is usually deinked using deinking chemicals and then recycled. Deinking chemicals generally include alkaline agents such as caustic soda, soda carbonate, and sodium silicate, one or more surfactants selected from anionic, nonionic, or amphoteric surfactants, and bleaching agents such as hydrogen peroxide. and auxiliary agents such as pH stabilizers and dispersants. Using deinking chemicals,
Pulp and ink are separated by flotation, water washing or flotation/water washing methods, and deinking valves are used in paper production.
近年、新聞印刷の急速なオフセット印刷化の例にみられ
るように、印刷方式および印刷インキはより早く、より
美しく、より強固な印刷へと向っており、そのため、印
刷インキは紙により強固に付着しており、従来の脱イン
キ技術では白色度の高い再生パルプを得ることはますま
す困難となっている。In recent years, printing methods and printing inks have been moving toward faster, more beautiful, and stronger printing, as seen in the rapid shift to offset printing in newspaper printing.As a result, printing inks have become more firmly attached to paper. Therefore, it is becoming increasingly difficult to obtain recycled pulp with high whiteness using conventional deinking techniques.
脱インキ効果を高めるため、脱インキ処理に際し、セル
ラーゼを用いることが提案されている（特開昭５９−９
２９９号および特開昭６３−５９４９４号）。In order to enhance the deinking effect, it has been proposed to use cellulase during the deinking process (Japanese Patent Application Laid-Open No. 1986-9
No. 299 and JP-A No. 63-59494).
すなわち、古紙にセルラーゼを作用させて繊維を部分的
に分解することにより脱インキを促進するものである。That is, deinking is promoted by causing cellulase to act on waste paper to partially decompose the fibers.
しかしながら、繊維の部分的分解は再生紙の強度低下を
もたらす。セルラーゼの使用量、使用時間などの処理条
件を適切に設定することにより、繊維の強度低下を成る
程度抑制できるものの、脱インキ作用も制限されるため
大巾な脱インキ効果は期待できない。However, partial decomposition of fibers results in reduced strength of recycled paper. By appropriately setting treatment conditions such as the amount and time of use of cellulase, it is possible to suppress the decrease in fiber strength to some extent, but the deinking effect is also limited, so a large deinking effect cannot be expected.
本発明の目的は、パルプ繊維の強度低下をもたらすこと
なく、白色度の高いパルプを得ることができる古紙の脱
インキ方法を提供するにある。An object of the present invention is to provide a method for deinking waste paper that can obtain pulp with high whiteness without causing a decrease in the strength of pulp fibers.
〔課題を解決するための手段および作用〕上記目的は、
古紙を脱インキ薬品で処理して脱インキを行うに際し、
古紙にリパーゼを作用せしめることによって達成される
。[Means and actions for solving the problem] The above purpose is
When deinking waste paper by treating it with deinking chemicals,
This is achieved by applying lipase to waste paper.
リパーゼは脂質分解酵素として知られている。Lipase is known as a lipolytic enzyme.
これまで衣料用洗剤とともにソノ４−ゼを用いて洗浄性
を高めることが行われているが、古紙の脱インキに用い
て高い脱インキ効果が達成されることは意外であった。Until now, Sono-4-ze has been used together with laundry detergents to improve cleaning performance, but it was surprising that a high deinking effect could be achieved when used to deink waste paper.
脱インキ処理に際しリパーゼを作用せしめることにより
、インキ中の油脂成分のグリセロールエステル結合が切
断され、インキの紙への結合力が弱められ、脱インキ作
用が促進されるものと考えられる。例えば、オフセット
印刷された新聞古紙の脱インキについてみると、紙面の
カラー化、美化、手の汚染防止などの目的で、新開印刷
は凸版印刷から急速にオフセント印刷へ移行しつつあり
、オフセット印刷の割合は現在５０％を超えていると言
われている。リパーゼは、新聞オフセント印刷インキに
使用されている乾性油（リノール酸、リルイン酸、オレ
イン酸などのトリグリセリド）やワックスエステルに作
用し、脱インキを促進すると考えられる。リパーゼはイ
ンキ中の油脂成分に直接作用するが、パルプ繊維自体に
は作用しないのでパルプ繊維の強度低下を招来しない。It is thought that the action of lipase during the deinking process cleaves the glycerol ester bonds of the oil and fat components in the ink, weakening the binding force of the ink to the paper and promoting the deinking effect. For example, when we look at deinking offset-printed used newspapers, Shinkai Printing is rapidly transitioning from letterpress printing to off-cent printing for purposes such as colorizing the paper, beautifying it, and preventing hand contamination. The proportion is said to be currently over 50%. Lipase is thought to act on drying oils (triglycerides such as linoleic acid, lyluic acid, and oleic acid) and wax esters used in newspaper offset printing inks to promote deinking. Lipase acts directly on the oil and fat components in the ink, but does not act on the pulp fiber itself, so it does not cause a decrease in the strength of the pulp fiber.
リパーゼとしては、広く動植物、微生物に由来するもの
が本発明の方法に使用でき格別限定されないが、中性な
いしアルカリ性の脱インキ処理条件下（ｐＨ６〜１４）
に十分な酵素活性を発現するアルカリリパーゼが好まし
い。Lipases derived from a wide variety of animals, plants, and microorganisms can be used in the method of the present invention, and are not particularly limited.
Alkaline lipase that expresses sufficient enzymatic activity is preferred.
好ましいリパーゼの例としては、デンマーク・ノボ・イ
ンダストリー社製のりポザイム（ＬｉｐｏｚｙｍｅＯ）
、リボラーゼ（Ｌｉｐｏｌａｓｅｅ ）、Ｓ Ｐ −２
８５、Ｓ Ｐ −３５６および５Ｐ−４００、ならびに
天野製薬■製のアマノーＰなどの市販品が挙げられる。An example of a preferable lipase is LipozymeO manufactured by Novo Industrie, Denmark.
, Ripolase, SP-2
Commercially available products include 85, S P-356 and 5P-400, and Amanor P manufactured by Amano Pharmaceutical Co., Ltd.
さらに、特開昭４８−６２．９９０号、同５３−２０．
４８７号および同６２７９．７８２号ならびにヨーロッ
パ特許筒２５８，０６８号、同第２１４，７６１号、同
第１３００６４号および英国特許筒１．３７２，０３４
号に記載される方法によって生産されるリパーゼが挙げ
られる。Furthermore, JP-A-48-62.990, JP-A No. 53-20.
487 and 6279.782 and European Patent No. 258,068, European Patent No. 214,761, European Patent No. 130064 and British Patent No. 1.372,034.
Examples include lipases produced by the method described in No.
使用するリパーゼは本来の生産菌によって生産されたも
のでもよいが、例えば、ヨーロッパ特許筒２３８．０２
３号に記載されているような方法で、リパーゼの構造遺
伝子を他の微生物に組込んだ組換え体によって生産され
たものでもよい。The lipase used may be one produced by the original producing bacteria, but for example,
It may also be produced by a recombinant organism in which a lipase structural gene is integrated into another microorganism by the method described in No. 3.
特に好ましいリパーゼはデンマーク・ノボ・インダスト
リー社製の５Ｐ−４００である。このリパーゼはデンマ
ーク特許２０５４／８８に記載されており、フミコーラ
・ラヌギノーサ（■ｕｍｉｃｏｌａ Ｌａｎｕｇｉｎｏ
ｓａ）由来のリパーゼをコードする遺伝子をアスペルギ
ルス・オリゼ（Ａｓｐｅｒｇｉｌｌｕｓ ｏｒｙｚａｅ
）に組込んで得られる組換え体アスペルギルス・オリゼ
が生産するアルカリ耐性リパーゼであって、至適ｐＨが
１０以上、至適温度が約４０℃、トリグリセライドの１
，３−位に特異的に作用し、分子置駒３５．０００、等
電点４，４の糖タンパクである。５Ｐ４００は１ｇ当り
３０．０００ ＬＵ （リパーゼ単位）の活性を示す
。ここで、ＩＬＵは測定条件下（温度３０°Ｃ１反応時
間５分、ｐＨ７，０）での酵素によるトリブチリン加水
分解における初速度で、酪酸化成によるｐｕの低下を常
に水酸化ナトリウム水溶液により補正した場合、１分間
に１μｍｏｌの滴定し得る酪酸を生成する速度に相当す
る酵素活性量である。A particularly preferred lipase is 5P-400 manufactured by Novo Industrie, Denmark. This lipase is described in Danish patent 2054/88 and is produced by Humicola Lanuginosa.
The gene encoding the lipase derived from Aspergillus oryzae
) is an alkali-resistant lipase produced by a recombinant Aspergillus oryzae, which has an optimum pH of 10 or more, an optimum temperature of about 40°C, and a triglyceride concentration of 1.
, 3-position, is a glycoprotein with a molecular position of 35,000 and an isoelectric point of 4.4. 5P400 exhibits an activity of 30.000 LU (lipase units) per gram. Here, ILU is the initial rate of tributyrin hydrolysis by the enzyme under the measurement conditions (temperature 30°C, reaction time 5 minutes, pH 7.0), and when the decrease in pu due to butyric acid formation is always corrected with an aqueous sodium hydroxide solution. , the amount of enzyme activity corresponding to the rate of production of 1 μmol of titratable butyric acid per minute.
古紙の脱インキ処理に際し使用するリパーゼの量は、古
紙乾燥重量１ ｋｇ当り１ 、０００Ｌｔ１以上、好ま
しくは１２．０００ＬＩＩ〜１，２００，０ＯＯＬＵで
ある。Ｓ Ｐ−４００の場合、その使用量は古紙乾燥重
量に基づき０．０４〜４．０重量％であることが望まし
い。The amount of lipase used in the deinking treatment of waste paper is 1,000 Lt1 or more, preferably 12,000 LII to 1,200,0 OOLU per kg of dry paper weight. In the case of SP-400, the amount used is preferably 0.04 to 4.0% by weight based on the dry weight of the waste paper.
リパーゼの脱インキ工程における作用時間は一般的に温
度２０〜６０℃にて５分間から５時間である。The action time of lipase in the deinking step is generally 5 minutes to 5 hours at a temperature of 20 to 60°C.
本発明で処理される古紙としては、新開古紙、雑誌古紙
、下級〜中級古紙、上質古紙など一般に言われる古紙全
てが挙げられる。The waste paper to be treated in the present invention includes all commonly used waste papers such as new paper, magazine waste paper, lower to middle grade waste paper, and high-quality waste paper.
本発明において、脱インキ薬品としては常用されるもの
が使用でき、代表的な脱インキ薬品は、アニオン、ノニ
オンもしくは両性界面活性剤の中から選ばれた一種また
は二種以上の界面活性剤、カセイソーダ、炭酸ソーダ、
ケイ酸ソーダ、リン酸ナトリウムなどのアルカリ剤、過
酸化水素などの漂白剤、その他必要に応じてｐＨ安定剤
、分散剤およびキレート剤などからなる。パルプ繊維の
強度低下が微かである少量のセルラーゼを併用すること
もできる。In the present invention, commonly used deinking chemicals can be used. Typical deinking chemicals include one or more surfactants selected from anionic, nonionic or amphoteric surfactants, caustic soda, , carbonated soda,
It consists of an alkaline agent such as sodium silicate and sodium phosphate, a bleaching agent such as hydrogen peroxide, and, if necessary, a pH stabilizer, a dispersing agent, and a chelating agent. It is also possible to use a small amount of cellulase that causes only a slight decrease in the strength of the pulp fibers.
リパーゼと古紙と接触は、脱インキ処理におけるいずれ
の湿式処理工程、すなわち、離解、熟成、フローテーシ
ョンなどのいずれの工程で行ってもよい。脱インキ薬品
の適用前もしくは適用後または脱インキ薬品と一緒にリ
パーゼを適用することができる。これまで、脱インキ工
程で試みられた各種改良方法において適用してもよい。The contact between the lipase and the waste paper may be carried out in any wet processing step in the deinking process, ie, in any step such as disintegration, aging, flotation, etc. The lipase can be applied before or after the application of the deinking chemicals or together with the deinking chemicals. It may be applied to various improvement methods that have been tried in the deinking process so far.
以下、実施例について本発明方法を具体的に説明する。 Hereinafter, the method of the present invention will be specifically explained with reference to Examples.
発行から２ケ月経過した新聞古紙を、水酸化カルシウム
で水質硬度１２度に調整した水を用い、パルプ濃度１０
重量％にて、乾燥パルプ重量に基づきカセイソーダ１％
、ケイ酸ソーダ２．５％、過酸化水素１．０５％、Ｓ
Ｐ−４０００，４％およびオレイン酸１．０８％を添加
しつつ、パルパーにて温度４０℃で６分間離解を行った
。Used newspapers that have been published for two months are processed to a pulp density of 10 using water that has been adjusted to a water hardness of 12 degrees with calcium hydroxide.
In weight percent, 1% caustic soda based on dry pulp weight
, Sodium silicate 2.5%, Hydrogen peroxide 1.05%, S
While adding 4% P-4000 and 1.08% oleic acid, disaggregation was carried out using a pulper at a temperature of 40° C. for 6 minutes.
なお、上記脱インキ薬品は以下の手順で加えた。The deinking chemicals mentioned above were added in the following procedure.
離解開始 １５秒後にカセイソーダ、ケイ酸ソーダ３０
秒後に過酸化水素
１分後に５Ｐ−４００
４分後にオレイン酸
次いで、４０”Ｃにて３５分間ソーキングを行った後に
パルプ濃度０．８５重量％に希釈し、８分間フローテー
ションを行った。最後に多量の水で洗浄し、ブフナーロ
ートを用いてバルブシートを作成した。15 seconds after starting disintegration, add caustic soda, sodium silicate 30
Seconds, hydrogen peroxide 1 minute later, 5P-400, 4 minutes later oleic acid, followed by soaking at 40"C for 35 minutes, diluting to a pulp concentration of 0.85% by weight, and flotation for 8 minutes.Finally. After washing with a large amount of water, a valve seat was created using a Buchner funnel.
比較のために、Ｓ Ｐ−４００を用いなかった他は上記
と同様な手法により古紙の脱インキ処理を行った。For comparison, waste paper was deinked using the same method as above except that SP-400 was not used.
作成したパルプの４５７ｎｍにおける反射率を測定する
ことにより白色度を評価した。その結果、Ｓ Ｐ−４０
０を用いたものの白色度は６０．５％であり、用いなか
ったものの白色度は５８．０％であった。The whiteness of the prepared pulp was evaluated by measuring the reflectance at 457 nm. As a result, SP-40
The whiteness of the sample using 0 was 60.5%, and the whiteness of the sample without 0 was 58.0%.
本発明の方法に従って、古紙の脱インキ処理を行うと、
パルプ繊維の強度低下をもたらすことなく、白色度の高
い再生パルプを得ることができる。When waste paper is deinked according to the method of the present invention,
Regenerated pulp with high whiteness can be obtained without reducing the strength of pulp fibers.
Claims (1)
品で処理して脱インキを行うに際し、古紙にリパーゼを
作用せしめることを特徴とする古紙の脱インキ方法。 ２、該リパーゼが、フミコーラ・ラヌギノーサ（Ｈｕｍ
ｉｃｏｌａＬａｎｕｇｉｎｏｓａ）由来のリパーゼをコ
ードする遺伝子をアスペルギルス・オリゼ（Ａｓｐｅｒ
ｇｉｌｌｕｓｏｒｙｚａｅ）に組込んで得られる組換え
体アスペルギルス・オリゼが生産するリパーゼであって
、至適ｐＨが１０以上、至適温度が約４０℃、トリグリ
セラードの１，３−位に特異的に作用し、分子量約３５
０００、等電点４、４の糖タンパクである請求項１記載
の方法。[Scope of Claims] 1. A method for deinking used paper, which comprises allowing lipase to act on the used paper when deinking the used paper by treating it with a deinking chemical under neutral or alkaline conditions. 2. The lipase is produced from Humicola lanuginosa (Humicola lanuginosa).
The gene encoding the lipase derived from Aspergillus oryzae
A lipase produced by a recombinant Aspergillus oryzae obtained by integrating into Aspergillus oryzae, which has an optimum pH of 10 or more, an optimum temperature of about 40°C, and specifically acts on the 1,3-position of triglyceride. and molecular weight approximately 35
The method according to claim 1, wherein the glycoprotein has an isoelectric point of 4.000 and an isoelectric point of 4.4.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP63310240A JPH02160984A (en) | 1988-12-09 | 1988-12-09 | Deinking method of waste paper |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP63310240A JPH02160984A (en) | 1988-12-09 | 1988-12-09 | Deinking method of waste paper |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH02160984A true JPH02160984A (en) | 1990-06-20 |
Family
ID=18002866
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP63310240A Pending JPH02160984A (en) | 1988-12-09 | 1988-12-09 | Deinking method of waste paper |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH02160984A (en) |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5370770A (en) * | 1992-11-09 | 1994-12-06 | The Mead Corporation | Method for deinking printed waste paper using soybean peroxidase |
| US6294047B1 (en) | 1999-07-30 | 2001-09-25 | Institute Of Paper | Methods for reducing fluorescence in paper-containing samples |
| WO2002055679A2 (en) | 2001-01-10 | 2002-07-18 | Novozymes A/S | Thermostable lipolytic enzyme variant |
| US6426200B1 (en) | 1994-09-15 | 2002-07-30 | University Of Georgia Research Foundation, Inc. | Methods for enzymatic deinking of waste paper |
| WO2002095127A3 (en) * | 2001-05-21 | 2003-05-01 | Novozymes As | Use of lipolytic enzymes for stickies control |
| EP1555322A1 (en) | 2000-04-28 | 2005-07-20 | Novozymes A/S | Lipolytic enzyme variant |
| KR100644267B1 (en) * | 2005-08-05 | 2006-11-10 | 한국화학연구원 | Flotation-deinking method with improving yield for waste paper |
| US7169257B2 (en) | 2003-11-12 | 2007-01-30 | Kemira Chemicals, Inc. | Method of deinking waste paper using a reduced alkali system |
| WO2007017889A1 (en) * | 2005-08-05 | 2007-02-15 | Council Of Scientific & Industrial Research | A process for enzymatic deinking of printed papers |
| JP2008526265A (en) * | 2005-01-19 | 2008-07-24 | コグニス・アイピー・マネージメント・ゲゼルシャフト・ミット・ベシュレンクテル・ハフツング | Process for the production and use of monoglycerides from triglycerides by alcohol treatment with Thermomyceslanunginosus lipase activated by alkali salts |
| US7645358B2 (en) | 2002-03-25 | 2010-01-12 | Council Of Scientific And Industrial Research | Process for biological deinking of office waste paper |
| US7951267B2 (en) | 2001-05-21 | 2011-05-31 | Kim Borch | Enzymatic hydrolysis of a polymer comprising vinyl acetate monomer |
-
1988
- 1988-12-09 JP JP63310240A patent/JPH02160984A/en active Pending
Cited By (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5370770A (en) * | 1992-11-09 | 1994-12-06 | The Mead Corporation | Method for deinking printed waste paper using soybean peroxidase |
| US6426200B1 (en) | 1994-09-15 | 2002-07-30 | University Of Georgia Research Foundation, Inc. | Methods for enzymatic deinking of waste paper |
| US6294047B1 (en) | 1999-07-30 | 2001-09-25 | Institute Of Paper | Methods for reducing fluorescence in paper-containing samples |
| US6387211B1 (en) | 1999-07-30 | 2002-05-14 | Institute Of Paper Science And Technology, Inc. | Methods for reducing fluorescence in paper-containing samples |
| EP1555322A1 (en) | 2000-04-28 | 2005-07-20 | Novozymes A/S | Lipolytic enzyme variant |
| EP2258853A1 (en) | 2000-04-28 | 2010-12-08 | Novozymes A/S | Lipolytic enzyme variant |
| EP2258852A1 (en) | 2000-04-28 | 2010-12-08 | Novozymes A/S | Lipolytic enzyme variant |
| EP2258835A1 (en) | 2000-04-28 | 2010-12-08 | Novozymes A/S | Lipolytic enzyme variant |
| EP2236611A1 (en) | 2000-04-28 | 2010-10-06 | Novozymes A/S | Lipolytic enzyme variant |
| WO2002055679A2 (en) | 2001-01-10 | 2002-07-18 | Novozymes A/S | Thermostable lipolytic enzyme variant |
| WO2002095127A3 (en) * | 2001-05-21 | 2003-05-01 | Novozymes As | Use of lipolytic enzymes for stickies control |
| US7951267B2 (en) | 2001-05-21 | 2011-05-31 | Kim Borch | Enzymatic hydrolysis of a polymer comprising vinyl acetate monomer |
| US7645358B2 (en) | 2002-03-25 | 2010-01-12 | Council Of Scientific And Industrial Research | Process for biological deinking of office waste paper |
| US7767057B2 (en) | 2003-11-12 | 2010-08-03 | Kemira Chemicals, Inc. | Deinking blends for use in reduced alkali systems |
| US7169257B2 (en) | 2003-11-12 | 2007-01-30 | Kemira Chemicals, Inc. | Method of deinking waste paper using a reduced alkali system |
| JP2008526265A (en) * | 2005-01-19 | 2008-07-24 | コグニス・アイピー・マネージメント・ゲゼルシャフト・ミット・ベシュレンクテル・ハフツング | Process for the production and use of monoglycerides from triglycerides by alcohol treatment with Thermomyceslanunginosus lipase activated by alkali salts |
| WO2007017889A1 (en) * | 2005-08-05 | 2007-02-15 | Council Of Scientific & Industrial Research | A process for enzymatic deinking of printed papers |
| WO2007018368A1 (en) * | 2005-08-05 | 2007-02-15 | Korea Research Institute Of Chemical Technology | Flotation-deinking method with improving yield for waste paper |
| KR100644267B1 (en) * | 2005-08-05 | 2006-11-10 | 한국화학연구원 | Flotation-deinking method with improving yield for waste paper |
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