WO2005001056A2 - Procedes de regulation de catalase - Google Patents

Procedes de regulation de catalase Download PDF

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Publication number
WO2005001056A2
WO2005001056A2 PCT/US2004/018861 US2004018861W WO2005001056A2 WO 2005001056 A2 WO2005001056 A2 WO 2005001056A2 US 2004018861 W US2004018861 W US 2004018861W WO 2005001056 A2 WO2005001056 A2 WO 2005001056A2
Authority
WO
WIPO (PCT)
Prior art keywords
catalase
composition
protease
treatment
water
Prior art date
Application number
PCT/US2004/018861
Other languages
English (en)
Other versions
WO2005001056A3 (fr
Inventor
Jing Luo
Hui Xu
Kathryn Taylor
Original Assignee
Novozymes North America, Inc.
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 Novozymes North America, Inc. filed Critical Novozymes North America, Inc.
Publication of WO2005001056A2 publication Critical patent/WO2005001056A2/fr
Publication of WO2005001056A3 publication Critical patent/WO2005001056A3/fr

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F3/00—Biological treatment of water, waste water, or sewage
    • C02F3/34—Biological treatment of water, waste water, or sewage characterised by the microorganisms used
    • C02F3/342—Biological treatment of water, waste water, or sewage characterised by the microorganisms used characterised by the enzymes used
    • C—CHEMISTRY; METALLURGY
    • C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F1/00—Treatment of water, waste water, or sewage
    • C02F1/72—Treatment of water, waste water, or sewage by oxidation
    • C02F1/722—Oxidation by peroxides
    • C—CHEMISTRY; METALLURGY
    • C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F2103/00—Nature of the water, waste water, sewage or sludge to be treated
    • C02F2103/26—Nature of the water, waste water, sewage or sludge to be treated from the processing of plants or parts thereof
    • C02F2103/28—Nature of the water, waste water, sewage or sludge to be treated from the processing of plants or parts thereof from the paper or cellulose industry

Definitions

  • the present invention relates to enzymatic methods for controlling catalase activity.
  • Catalase is an enzyme that catalyzes the reaction of hydrogen peroxide to oxygen and water. Catalase is naturally produced by most cells, and primarily functions as a cellular defense mechanism to destroy both extracellular and intracellular peroxides.
  • Catalase activity is a problem in many industrial processes.
  • bacteria are present in the various sections of the white water system.
  • Catalase produced by micro- organisms in paper mills can significantly compromise the peroxide treatment used in various parts of the milling process, including, in pulping, deinking and bleaching processes.
  • High microbial catalase levels have been associated with both a lower brightness and greater variation in the brightness levels of the pulp and paper products.
  • Microbial catalase levels are becoming even more of a problem as paper mills and other industrial processes employ closed water loop systems.
  • U.S. Patent No. 6,124,111 is directed to a method for determining the amount of catalase before or in connection with bleaching of cellulose fibers in a pulp suspension so as to correct dosing of the actual bleaching substance for the purpose of providing a better and more uniform product quality.
  • the present invention relates to methods and composition for controlling catalase activity by contacting or treating a catalase contaminated system with a protease.
  • the protease treatment can be used to improve peroxide treatment processes, such as, peroxide bleaching processes, which are compromised by catalase activity resulting from microbial growth present in the system.
  • the present invention also relates to methods and composition for controlling catalase in pulp and paper mills.
  • the protease treatment may be applied in any suitable stage in the pulp and paper mill, such as, in pulping, deinking and/or bleaching or in any other process in which peroxide or other bleaching treatment is used.
  • the protease treatment may be applied to any composition, system or process in which catalase contamination is a problem.
  • the protease treatment is applied to systems or processes in which microbial catalase production reduces the effectiveness of a peroxide or bleaching treatment process, e.g., in paper mills and textile mills. More preferably, the protease treatment is applied to microbial catalase contamination in a closed loop system in an industrial process.
  • the protease treatment of the present invention is applied to a pulp and paper mill process. More preferably, the protease treatment of the present invention is applied in a paper recycling mill.
  • the protease treatment may be applied to any suitable stage in the paper mill, such as, in pulping, deinking (e.g., flotation deinking) and/or bleaching or in any other process in which peroxide or another bleaching chemical which is compromised by the catalase activity is used. More preferably, the protease is added in the water loop of the paper mill and is allowed to run throughout the system. For example, the protease may be added at a selected point in the water loop, and with each iteration, the concentration of the protease increases to the desired level to control the catalase contamination throughout the sys- tern.
  • the protease is added to a catalase contaminated system or process in an amount effective to control the catalase activity.
  • control means to reduce and/or prevent an increase in catalase concentration in the system, process or composition to be treated.
  • effective amounts of protease include 0.00001 g/L to 1 g/Lc of treatment water
  • Effective amounts of protease also include 0.0001% to 10% on oven dry equivalent fiber, more preferably, 0.001% to 1% on oven dry equivalent fiber
  • Suitable proteases include those of animal, vegetable or microbial origin, preferably of mi- crobial origin.
  • the protease may be a serine protease or a metalloprotease, preferably an alkaline microbial protease.
  • proteases include aminopeptidases, including pro- lyl aminopeptidase (3.4.11.5), X-pro aminopeptidase (3.4.11.9), bacterial leucyl aminopepti- dase (3.4.11.10), thermophilic aminopeptidase (3.4.11.12), lysyl aminopeptidase (3.4.11.15), tryptophanyl aminopeptidase (3.4.11.17), and methionyl aminopeptidase (3.4.11.18); serine endopeptidases, including chymotrypsin (3.4.21.1), trypsin (3.4.21.4), cucumisin (3.4.21.25), brachyurin (3.4.21.32), cerevisin (3.4.21.48)and subtilisin (3.4.21.62); cysteine endopeptidases, including papain (3.4.22.2), ficain (3.4.22.3), chymopapain (3.4.22.6), asclepain (3.4.22.7), actinidain (3.4.22.14),
  • subtilisins include subtilisin BPN', subtilisin amylosacchariticus, subtilisin 168, subtilisin mesentericopeptidase, subtilisin Carlsberg, subtilisin DY, subtilisin 309, subtilisin 147, thermitase, aqualysin, Bacillus PB92 protease, proteinase K, protease TW7, and protease TW3.
  • proteases include Alcalase TM, Savinase TM, Primase TM, Duralase TM., Esperase TM., Kannase TM., and Durazym TM (all available from No- vozymes A/S), Maxatase TM , Maxacal TM., Maxapem.TM., Properase TM, Purafect TM., Purafect OxP TM., FN2 TM., FN3 TM and FN4 TM. (all available from Genencor International Inc.).
  • a preferred commercial protease is AlcalaseTM (Novozymes A/S.)
  • protease treatment may be combined with other catalase control treatments known in the art, including, e.g., peracetic acid and biocides.
  • the protease treatment is applied to a recycling mill.
  • the protease treatment may be performed at any suitable time in the paper recycling process, e.g., the protease treatment may be applied before, during or following the ink separation proc- ess.
  • ink separation processes include mechanical deinking, flotation, chemi- mechanical deinking, agglomeration chemistry (see e.g. McBride, Pulp and Paper, April 1994, Miller Freeman Publishers, San Francisco, p. 44), washing, cycles of dilution and filtration, treatment in hydrolcyclones, or by a suitable combination of these.
  • the protease treatment is preferably performed prior to and/or simultaneously with a hydro- gen peroxide treatment step (e.g., bleaching).
  • a hydro- gen peroxide treatment step e.g., bleaching
  • the experiment determined the effect of catalase on residual peroxide concentration, with and without protease treatment.
  • Catalase (Terminox Ultra 50L, Novozymes A/S) and protease (Savinase TM, Novozymes A/S) were reacted in a Laundrometer for 1 hour at 45°C, followed by the addition of H 2 0 2 , and the reaction was then run for 20 min at 45°C. Analysis was done at 240 nm on a UV-Vis.
  • protease to control catalase activity was analyzed in the context of an ONP flotation deinking trial.
  • Catalase (Terminox Ultra 50L, Novozymes A/S) was added to mimic the catalase contamination seen in mills.
  • the protease treatment improved the brightness of the pulp after flotation.

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Microbiology (AREA)
  • Biodiversity & Conservation Biology (AREA)
  • Hydrology & Water Resources (AREA)
  • Engineering & Computer Science (AREA)
  • Environmental & Geological Engineering (AREA)
  • Water Supply & Treatment (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Paper (AREA)

Abstract

La présente invention concerne des procédés et une composition permettant de réguler la catalase par traitement ou par mise en contact d'un système contaminé par catalase avec une protéase. Ce traitement par protéase peut être utilisé pour améliorer des opérations de traitement au peroxyde, telles que des opérations de blanchiment au peroxyde, dont la réalisation est compromise par l'activité catalase résultant d'une croissance microbienne dans le système. La présente invention concerne également des procédés et une composition permettant de réguler la catalase dans la fabrication de la pâte et du papier.
PCT/US2004/018861 2003-06-10 2004-06-10 Procedes de regulation de catalase WO2005001056A2 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US47750603P 2003-06-10 2003-06-10
US60/477,506 2003-06-10

Publications (2)

Publication Number Publication Date
WO2005001056A2 true WO2005001056A2 (fr) 2005-01-06
WO2005001056A3 WO2005001056A3 (fr) 2005-06-30

Family

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Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2004/018861 WO2005001056A2 (fr) 2003-06-10 2004-06-10 Procedes de regulation de catalase

Country Status (1)

Country Link
WO (1) WO2005001056A2 (fr)

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8246778B2 (en) 2008-11-21 2012-08-21 Buckman Laboratories International, Inc. Method for controlling enzymatic decomposition of peroxide
US8389208B2 (en) 2004-03-22 2013-03-05 Health Protection Agency Biological indicator
CN107760619A (zh) * 2017-09-30 2018-03-06 河北天泓环保科技有限公司 水处理网载催化树脂酶机体及其使用方法

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5919698A (en) * 1995-09-25 1999-07-06 Novo Nordisk A/S Disinfection and cleaner of contact lenses

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5919698A (en) * 1995-09-25 1999-07-06 Novo Nordisk A/S Disinfection and cleaner of contact lenses

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8389208B2 (en) 2004-03-22 2013-03-05 Health Protection Agency Biological indicator
US8246778B2 (en) 2008-11-21 2012-08-21 Buckman Laboratories International, Inc. Method for controlling enzymatic decomposition of peroxide
CN107760619A (zh) * 2017-09-30 2018-03-06 河北天泓环保科技有限公司 水处理网载催化树脂酶机体及其使用方法

Also Published As

Publication number Publication date
WO2005001056A3 (fr) 2005-06-30

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