EP0835927A2 - Enlèvement du peroxyde d'hydrogène dans les bains de blanchiment - Google Patents

Enlèvement du peroxyde d'hydrogène dans les bains de blanchiment Download PDF

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Publication number
EP0835927A2
EP0835927A2 EP97117009A EP97117009A EP0835927A2 EP 0835927 A2 EP0835927 A2 EP 0835927A2 EP 97117009 A EP97117009 A EP 97117009A EP 97117009 A EP97117009 A EP 97117009A EP 0835927 A2 EP0835927 A2 EP 0835927A2
Authority
EP
European Patent Office
Prior art keywords
buffer
catalase
weight
parts
mixture
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.)
Withdrawn
Application number
EP97117009A
Other languages
German (de)
English (en)
Other versions
EP0835927A3 (fr
Inventor
Uwe Dr. Vogt
Martin Dr. Riegels
Rainhard Dr. Koch
Bernd Könemund
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Bayer AG
Original Assignee
Bayer AG
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Bayer AG filed Critical Bayer AG
Publication of EP0835927A2 publication Critical patent/EP0835927A2/fr
Publication of EP0835927A3 publication Critical patent/EP0835927A3/fr
Withdrawn legal-status Critical Current

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Classifications

    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • DTEXTILES; PAPER
    • D06TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06LDRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L4/00Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
    • D06L4/10Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
    • D06L4/12Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen combined with specific additives

Definitions

  • a bleaching process is usually carried out before dyeing textile materials, especially if light and brilliant shades are to be achieved.
  • Oxidation systems such as H 2 O 2 / NaOH or corresponding peroxide derivatives are used for this.
  • Such alkaline bleaching treatments using hydrogen peroxide have the disadvantage that the excess of peroxide and alkali must be carefully removed from the substrate and from the liquor, since it leads to incorrect results in the subsequent dyeing (Melliand Textilberichte 71 (1990), 205 to 207 ).
  • the invention relates to an enzymatic process for removing Hydrogen peroxide from bleaching liquors in the textile industry, which is characterized is that after the bleaching process has ended the degradation of the in the fleet and on the hydrogen peroxide remaining in the textile material without previous partial or complete neutralization is carried out, a mixture of Catalase and a highly concentrated buffer is used.
  • the invention accordingly also relates to a mixture of an enzyme which is able to degrade peroxide, i.e. a catalase, and a highly concentrated one Buffer, in the presence of which the enzyme is stable and active, which in can buffer a pH range of 4-9 and even in small amounts Allows lowering the pH in the desired range.
  • an enzyme which is able to degrade peroxide, i.e. a catalase, and a highly concentrated one Buffer, in the presence of which the enzyme is stable and active, which in can buffer a pH range of 4-9 and even in small amounts Allows lowering the pH in the desired range.
  • the new mixture differs significantly from the buffered one Catalase mixtures, which are used for cleaning and storing contact lenses be used.
  • buffers are added with the aim of to set the optimal pH for the enzymes.
  • the person skilled in the art knows that the buffer concentrations used within the scope of the in the biochemical laboratory practice usual use amount of 20-200mM, for example emotional.
  • Enzymes that are able to break down H 2 O 2 to H 2 O and O 2 are called catalases. They have an iron porphyrin ring and occur in all aerobic organisms (animals, plants and microorganisms). Organisms that live without oxygen often have no catalase.
  • the catalase can be microbial, animal or vegetable Origin. It preferably comes from bacteria or fungi and is particularly preferred from the microorganism Aspergillus niger, as commercially available Catalases can very particularly preferably Terminox®, Terminox ultra®, Catazym® and Catalase T100® (manufacturer Genencor and Novo Nordisk) be used.
  • buffers are able to buffer a pH range of 3-9.
  • the one to be buffered is preferably located Range at 4-8.
  • the following buffers can be used according to the invention, for example: Citrate, acetate, phosphate, formate, carbonate, tris-hydroxymethyl-aminomethane, Triethanolamine, imidazole, oxalate, tartrate, fumarate, maleinate, phthalate, succinate, Ethylenediamine and mixtures of several of them.
  • Acetate, Phosphate and citrate are used as buffers.
  • the invention is particularly preferably Mixture of a catalase and acetate.
  • BU Baker Units
  • KCIU Kilo Catalase International Units
  • To standardize the different measurement methods was an activity determination as described below applied: 1000 ml of a standard bleaching liquor consisting of 1.25 ml / l sodium hydroxide solution 32%, 1.0 ml / l hydrogen peroxide 35% and 0.3 ml / l of a bleach stabilizer according to Example 6, at 40 ° C with stirring with a solution added from 4.9 ml of an acetate buffer of pH 5 and from a defined Amount of a commercially available catalase, e.g. 1.0 g, ordered.
  • the acetate buffer will prepared by a 7M aqueous acetic acid solution with 45% sodium hydroxide solution is adjusted to a pH of 5.
  • Catalase and buffer can be mixed in the following proportions (g / g): 1 Part of a commercial catalase and 1 to 100 parts of a highly concentrated one Buffer solution.
  • the mixture according to the invention consists of either 1 part of Novo Terminox Ultra 10L® and 1.5 to 15 parts of a highly concentrated one Acetate buffer or 5 to 23 parts of a highly concentrated citrate buffer or but from 1 part Genencor Catalase T 100® and 5 to 40 parts one highly concentrated acetate buffer or 20 to 80 parts of a highly concentrated Citrate buffers. All parts are parts by weight.
  • a highly concentrated buffer is one which can be produced by in the case of the acetate buffer a 5-16, preferably 7-15 M aqueous acetic acid solution with ammonium or an alkali hydroxide, e.g. Sodium hydroxide in the form a 45% aqueous solution, to a pH of 3 to 6, preferably 4 to 5.5, or in the case of the citrate buffer a 2-5, preferably 3-4 s aqueous citric acid solution with ammonium or an alkali hydroxide, such as e.g. Sodium hydroxide in the form of a 45% aqueous solution, to a pH of 3 to 6, preferably 4-5.5 is set.
  • aqueous acetic acid solution with ammonium or an alkali hydroxide e.g. Sodium hydroxide in the form a 45% aqueous solution
  • the usual quantities used for the mixture are between 0.5-10 g per liter Fleet.
  • the peroxide bleaching of textile materials is usually in the temperature range from 80-100 ° C and a pH of 10-12.
  • the amount of to be used Hydrogen peroxide depends, for example, on the amount of substrate, the whiteness to be achieved, the temperature and the amount of stabilizer used. These conditions are known to the person skilled in the art.
  • the inventive method of the simultaneous removal of residual peroxide and the adjustment of the pH value to an optimal enzyme activity and to subsequent ones Treatment processes, such as dyeing, are carried out in one Temperature of 20-70 ° C, preferably 30-65 ° C carried out.
  • a 10 molar aqueous acetic acid was initially charged and as long as 45% NaOH was added until a pH of 5 was reached. From this solution 9.4 parts by weight mixed with a part by weight of Catalase T100® (from Genencor).
  • a 7-molar aqueous acetic acid was initially charged and as long as 45% NaOH was added until a pH of 5 was reached. From this solution 11.7 parts by weight mixed with a part by weight of Catalase T100® (from Genencor).
  • a 7-molar aqueous acetic acid was initially charged and as long as 45% NaOH was added until a pH of 5 was reached. From this solution 3 parts by weight mixed with one part by weight of Terminox 10L® (from Novo Nordisk).
  • a 4-molar aqueous citric acid was introduced and as long as 45% NaOH was added until a pH of 5 was reached. From this solution 27.2 parts by weight with one part by weight of Catalase T100® (from Genencor) mixed.
  • a 4 molar, aqueous citric acid solution was presented and as long as 45% NaOH was added until a pH of 5 was reached. From this solution 7 parts by weight with one part by weight of Terminox Ultra 10L® (from Novo Nordisk) mixed.
  • the liquor ratio was 1:10. After a treatment time of 45 min 98 ° C was cooled to 80 ° C, the bleach was drained and with cold water replenished to the original volume. At a temperature of 55 ° C and a pH of 10.8, 2.6 g / l of a product was added according to Example 1. After 10 minutes of treatment, the test showed Peroxide test sticks from Merck that neither in the fleet nor on the Cotton hydrogen peroxide was detectable. The pH in the fleet and on the fiber showed a value of 6.
  • the liquor ratio was 1:10. After a treatment time of 45 min 95 ° C. was cooled to 80 ° C., the bleaching liquor was drained off and water was added replenished the original volume. This was followed by a rinsing step at 80 ° C. After draining the fleet and filling it with fresh water, one was carried out Temperature of 50 to 55 ° C and a pH of 10.6 the addition of 2.5 g / l of a product according to Example 2. After 10 minutes of treatment, the review showed with peroxide test sticks from Merck that neither in the fleet nor on which cotton hydrogen peroxide was detectable. The pH in the Brisk and on the fiber showed a value of 7.
  • Samples of a buffer catalase mixture according to Example 1 or 3 were 3 months stored at 25 ° C. None of the samples showed precipitations or after this time Cloudiness.
  • the activity of a buffer catalase mixture according to Example 1 or 3 was direct determined after production and after 3 months storage at 25 ° C.
  • the Activity determination was carried out by using a bleaching liquor consisting of

Landscapes

  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Textile Engineering (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Detergent Compositions (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)
EP97117009A 1996-10-14 1997-10-01 Enlèvement du peroxyde d'hydrogène dans les bains de blanchiment Withdrawn EP0835927A3 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE19642325 1996-10-14
DE19642325A DE19642325A1 (de) 1996-10-14 1996-10-14 Entfernung von Wasserstoffperoxid aus Bleichflotten

Publications (2)

Publication Number Publication Date
EP0835927A2 true EP0835927A2 (fr) 1998-04-15
EP0835927A3 EP0835927A3 (fr) 1999-01-13

Family

ID=7808700

Family Applications (1)

Application Number Title Priority Date Filing Date
EP97117009A Withdrawn EP0835927A3 (fr) 1996-10-14 1997-10-01 Enlèvement du peroxyde d'hydrogène dans les bains de blanchiment

Country Status (4)

Country Link
EP (1) EP0835927A3 (fr)
JP (1) JPH10130696A (fr)
DE (1) DE19642325A1 (fr)
TR (1) TR199701166A2 (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR3063498A1 (fr) * 2017-03-03 2018-09-07 Gina Gillieron Composition de nettoyage

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102004027371B4 (de) * 2004-06-06 2015-04-23 Chemische Fabrik Kreussler & Co. Gmbh Verfahren für die Wäscherei
KR101061436B1 (ko) * 2008-09-08 2011-09-02 (주)성환 타올의 염색 전처리 방법
BR112012000531A2 (pt) * 2009-07-09 2019-09-24 Procter & Gamble composição detergente para lavagem de roupas catalítica que compreende teores relativamente baixos de eletrólito solúvel em água
TWI630170B (zh) * 2016-12-16 2018-07-21 帆宣系統科技股份有限公司 高濃度過氧化氫水溶液之處理方法

Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR1403695A (fr) * 1964-04-30 1965-06-25 Sarget Ambrine Lab Procédé amélioré de préparation de la catalase de foie de cheval
US4136204A (en) * 1975-05-13 1979-01-23 Interox Chemicals Limited Process for bleaching dark fish meat
US5017194A (en) * 1989-01-19 1991-05-21 The United States Of America, As Represented By The Secretary Of Agriculture Sequential oxidative and reductive bleaching of pigmented and unpigmented fibers
US5071439A (en) * 1988-02-24 1991-12-10 Sandoz Ltd. Process for bleaching textile material
WO1992017571A1 (fr) * 1991-03-27 1992-10-15 Novo Nordisk A/S Catalase, sa production et son utilisation
EP0520239A1 (fr) * 1991-06-28 1992-12-30 AUSIMONT S.p.A. Détoxication d'eaux de végétation
WO1997013628A1 (fr) * 1995-10-06 1997-04-17 Novo Nordisk A/S Blanchiment et sterilisation d'articles en liege

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE3904449A1 (de) * 1988-02-24 1989-09-07 Sandoz Ag Verfahren zum bleichen von textilmaterialien
JPH02104781A (ja) * 1988-10-13 1990-04-17 Mitsubishi Gas Chem Co Inc 染色前処理法

Patent Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR1403695A (fr) * 1964-04-30 1965-06-25 Sarget Ambrine Lab Procédé amélioré de préparation de la catalase de foie de cheval
US4136204A (en) * 1975-05-13 1979-01-23 Interox Chemicals Limited Process for bleaching dark fish meat
US5071439A (en) * 1988-02-24 1991-12-10 Sandoz Ltd. Process for bleaching textile material
US5017194A (en) * 1989-01-19 1991-05-21 The United States Of America, As Represented By The Secretary Of Agriculture Sequential oxidative and reductive bleaching of pigmented and unpigmented fibers
WO1992017571A1 (fr) * 1991-03-27 1992-10-15 Novo Nordisk A/S Catalase, sa production et son utilisation
EP0520239A1 (fr) * 1991-06-28 1992-12-30 AUSIMONT S.p.A. Détoxication d'eaux de végétation
WO1997013628A1 (fr) * 1995-10-06 1997-04-17 Novo Nordisk A/S Blanchiment et sterilisation d'articles en liege

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
DATABASE WPI Section Ch, Week 9021 Derwent Publications Ltd., London, GB; Class A35, AN 90-161491 XP002085228 & JP 02 104781 A (MITSUBISHI GAS CHEM CO INC), 17. April 1990 *

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR3063498A1 (fr) * 2017-03-03 2018-09-07 Gina Gillieron Composition de nettoyage

Also Published As

Publication number Publication date
TR199701166A3 (tr) 1998-05-21
EP0835927A3 (fr) 1999-01-13
JPH10130696A (ja) 1998-05-19
DE19642325A1 (de) 1998-04-16
TR199701166A2 (xx) 1998-05-21

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