WO2006032450A1 - Method for the inactivation of enzymes - Google Patents
Method for the inactivation of enzymes Download PDFInfo
- Publication number
- WO2006032450A1 WO2006032450A1 PCT/EP2005/010123 EP2005010123W WO2006032450A1 WO 2006032450 A1 WO2006032450 A1 WO 2006032450A1 EP 2005010123 W EP2005010123 W EP 2005010123W WO 2006032450 A1 WO2006032450 A1 WO 2006032450A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- hcho
- releasing
- use according
- enzymes
- catalase
- Prior art date
Links
- HUHGPYXAVBJSJV-UHFFFAOYSA-N OCCN1CN(CCO)CN(CCO)C1 Chemical compound OCCN1CN(CCO)CN(CCO)C1 HUHGPYXAVBJSJV-UHFFFAOYSA-N 0.000 description 1
- UUGLSEIATNSHRI-UHFFFAOYSA-N OCN(C(C(N1CO)N2CO)N(CO)C2=O)C1=O Chemical compound OCN(C(C(N1CO)N2CO)N(CO)C2=O)C1=O UUGLSEIATNSHRI-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- 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
- C12N9/99—Enzyme inactivation by chemical treatment
Definitions
- the invention relates to use of HCHO-releasing chemicals for the inactivation of en ⁇ zymes, preferably the inactivation of catalase.
- Hydrogen peroxide is used in the production of pulp, especially in the production of recycled pulp, in order to enhance its brightness by bleaching.
- the perform- ance of hydrogen peroxide in the process is reduced by decomposition. Consequently, more peroxide is required which reduces the cost effectiveness of the process and may also cause additional problems such as corrosion problems.
- Hydrogen peroxide decomposition may be caused by certain metal ions. Such problem can be overcome by the use of certain chelating agents.
- Another way of decomposition is decomposition caused by peroxide-decomposing enzymes, such as catalase. These enzymes are produced by microbial action in the pulp.
- WO 95/00439 discloses a process for inhibiting enzymatic decomposition of peroxide using dialdehydes, such as glutaraldehyde, and acetals thereof.
- HCHO-releasing chemicals for the inactivation of enzymes.
- the enzyme to be inhibited is catalase and in another preferred embodiment HCHO-releasing chemicals are used in order to inactivate enzymes in a process production and/or treatment of pulp.
- the HCHO-releasing chemicals exhibit a better performance in inactivating enzymes as compared to other compounds such as the dialdehydes mentioned above.
- Suitable HCHO-releasing chemicals for use according to the invention are all chemi ⁇ cals which release HCHO under the conditions of use.
- the compounds should release HCHO at temperatures below 80 0 C, preferably below 5O 0 C, more pref ⁇ erably below 4O 0 C and most preferably already at 2O°C.
- the HCHO-releasing com ⁇ pounds are preferably soluble in water or in aqueous formulations comprising at least 50 % by weight of water together with other solvents miscible with water.
- HCHO-releasing chemicals comprise 1,3,5-Tris-(2-hy- droxyethyl)-1,3,5-hexahydrotriazine (HT) and lmidazo[4,5-d]imidazol-2,5-(1H, 3H)- dione-tetrahydro-1 ,3,4,6-tetrakis-(hydroxymethyl) (TD).
- Both compounds are commercially available under the trade name Protector HT and Protectol ® TD, respectively.
- the components are known as biocides each. It is of course possible to use mixtures of different HCHO-releasing compounds.
- a preferred HCHO-releasing compound is lmidazo[4,5-d]imidazol-2,5-(1H, 3H)-dione- tetrahydro-1 ,3,4,6-tetrakis-(hydroxymethyl) (TD).
- the HCHO-releasing chemicals are used for the inactivation of enzymes.
- enzymes which may be inhibited comprise protease, amy ⁇ lase, cellulase or catalase.
- the enzyme to be inhibited is catalase.
- the HCHO-releasing chemicals are added to the enzyme containing medium to be protected, which may be a solution, formulation, dispersion, technical material, process medium or the like comprising the enzyme.
- the medium to be protected is the process medium used in a production process and/or treatment of pulp, preferably recycled pulp, and especially using hydrogen peroxide or other peroxides as bleaching agent.
- Such media typically comprise fibres, water, hydrogen peroxide, and other additives.
- Catalase may be generated in such media by microbial action which in turn catalyses the decomposition of hydrogen peroxide.
- catalase it may also be possible to control catalase in industrial waste systems whereby excess catalase can be inhibited once it has broken down the hydrogen peroxide or primarily where an excess of hydrogen peroxide is employed which then requires catalase to be used in controlled amounts.
- the amount of HCHO-releasing chemicals added to the medium may be selected by the skilled artisan according to the desired effect and of course depends on the con ⁇ centration of the enzyme to be inhibited.
- the HCHO-releasing chemicals are used at concentrations below their Minimum Inhibitory Concentration (M. I. C), i.e. the aim of the invention is not to combat the microbes which produce enzymes thereby causing ad ⁇ verse effects but to inhibit the enzymes themselves in order to avoid said adverse ef ⁇ fects. It's the advantage of said strategy that much lower amounts of active ingredients are sufficient in order to obtain the same effect.
- M. I. C Minimum Inhibitory Concentration
- the M. I. C. of component (HT) mentioned above with regard to bacteria such as Staphylococcus aureas, Bacillus subtilis, Klebsiella pneumoniae, Enterobacter aero- genes, yeasts such as Candida albicans, or moulds such as penicillium funiculosum is 500 ppm
- the M. I. C. of (TD) mentioned above with regard to several organisms is 1000 ppm.
- the HCHO-releasing chemicals are preferably used at concentrations well below 500 ppm, more preferably below 250 ppm, and most preferably below 125 ppm.
- concentrations well below 500 ppm more preferably below 250 ppm, and most preferably below 125 ppm.
- a concentration of 1 to 100 ppm is sufficient for inhibition, preferably 2 to 80 more preferably 5 to 60 ppm, most preferred 10 to 50 ppm, and for example 20 to 40 ppm.
- the pH-value for using the HCHO-releasing chemicals may be selected by the skilled artisan according to the desired effect. Usually, the pH-value should be above 4, though the invention is not restricted to said range. Preferably, the range of pH-values is from 6 to 14, more preferably 7 to 13, most preferably 8 to 12, and for example 9 to 12.
- the temperature usually is around ambient temperature, however the temperature range may be typically from O 0 C to 7O 0 C, preferably 10 to 5O 0 C.
- biocides which combat microbes themselves.
- biocides comprise one or more components selected from the group of alcohols, isothiazolones, activated halogen compounds, formaldehyde release compounds, phenolic compounds, aldehydes, acids and esters, biphenyls, urea derivatives, O-acetals, O-formals, N-acetals, N-formals, benzamidines, phthalimides, pyridine derivatives, quaternary ammonium and phospho- nium compounds, amines, amphoteric compounds, dithiocarbamates, compounds con ⁇ taining active oxygen and mixtures of any of these.
- the active component is selected from at least one of 2-bromo-2-nitropropane-1 ,3-diol, 1 ,2-benzisothiazol- 3(2H)-one, 5-chloro-2-methyl-2H-isothiazol-3-one, 2-methyl-2H-isothiazol-3-one, tetra- hydro-1 ,3 I 4 I 6-tetrakis(hydroxymethyl)-imidazo[4,5-d]imida2ole-2,5(2H,3H)-dione I 1 ,3- dimethyl-5,5-dimethylhydantoin and a polyvinylamine, 3-Bromo-1-chloro-5,5-dimethyl- 2,4-imidazoIinedione), 2,2-Dibromo-3-Nitrilopropionamide, hydrogen peroxide, perace- tic acid.
- 2-bromo-2-nitropropane-1 ,3-diol 1 ,2-benzisothiazol-
- Test solution - Aqueous solution of NaOH ( 0,6 g/l)
- the pH of the solution was 11 ,0. No bacteria were used in the test solution.
- HCHO-releasing chemicals and other compounds to be tested were added in the concentrations given below. The tests were performed at ambient temperatures and the concentration of H 2 O 2 monitored as a function of time.
- test data are summarized in table 1 :
- HCHO-releasing chemicals significantly enhanced the time for complete decomposition of H 2 O 2 .
- Table 1 also contains the theoretical HCHO-concentration in solution resulting from complete hydrolysis. Although the theoretical amounts of free HCHO generated via the HCHO-releasing chemicals is less than 50 ppm HCHO as in the comparative example, surprisingly, the HCHO-releasing compounds exhibit an even better performance than free HCHO.
Abstract
Use of HCHO-releasing chemicals for the inactivation of enzymes.
Description
Method for the Inactivation of Enzymes
Description
The invention relates to use of HCHO-releasing chemicals for the inactivation of en¬ zymes, preferably the inactivation of catalase.
Hydrogen peroxide is used in the production of pulp, especially in the production of recycled pulp, in order to enhance its brightness by bleaching. However, the perform- ance of hydrogen peroxide in the process is reduced by decomposition. Consequently, more peroxide is required which reduces the cost effectiveness of the process and may also cause additional problems such as corrosion problems.
Hydrogen peroxide decomposition may be caused by certain metal ions. Such problem can be overcome by the use of certain chelating agents. Another way of decomposition is decomposition caused by peroxide-decomposing enzymes, such as catalase. These enzymes are produced by microbial action in the pulp.
WO 95/00439 discloses a process for inhibiting enzymatic decomposition of peroxide using dialdehydes, such as glutaraldehyde, and acetals thereof.
It is an object of the present invention to provide an improved process for the inactiva¬ tion of enzymes in which less amounts of enzyme inhibitor may be used.
Accordingly, we have found the use of HCHO-releasing chemicals for the inactivation of enzymes. In a preferred embodiment of the invention the enzyme to be inhibited is catalase and in another preferred embodiment HCHO-releasing chemicals are used in order to inactivate enzymes in a process production and/or treatment of pulp.
Surprisingly, the HCHO-releasing chemicals exhibit a better performance in inactivating enzymes as compared to other compounds such as the dialdehydes mentioned above.
Regarding the invention, the following may be stated specifically.
Suitable HCHO-releasing chemicals for use according to the invention are all chemi¬ cals which release HCHO under the conditions of use. Preferably, the compounds should release HCHO at temperatures below 800C, preferably below 5O0C, more pref¬ erably below 4O0C and most preferably already at 2O°C. The HCHO-releasing com¬ pounds are preferably soluble in water or in aqueous formulations comprising at least 50 % by weight of water together with other solvents miscible with water.
Preferred examples of such HCHO-releasing chemicals comprise 1,3,5-Tris-(2-hy- droxyethyl)-1,3,5-hexahydrotriazine (HT) and lmidazo[4,5-d]imidazol-2,5-(1H, 3H)- dione-tetrahydro-1 ,3,4,6-tetrakis-(hydroxymethyl) (TD).
Both compounds are commercially available under the trade name Protector HT and Protectol® TD, respectively. The components are known as biocides each. It is of course possible to use mixtures of different HCHO-releasing compounds.
A preferred HCHO-releasing compound is lmidazo[4,5-d]imidazol-2,5-(1H, 3H)-dione- tetrahydro-1 ,3,4,6-tetrakis-(hydroxymethyl) (TD).
According to the invention the HCHO-releasing chemicals are used for the inactivation of enzymes. Examples of enzymes which may be inhibited comprise protease, amy¬ lase, cellulase or catalase. Preferably, the enzyme to be inhibited is catalase.
For using the HCHO-releasing chemicals according to the invention they are added to the enzyme containing medium to be protected, which may be a solution, formulation, dispersion, technical material, process medium or the like comprising the enzyme.
In a preferred embodiment of the invention the medium to be protected is the process medium used in a production process and/or treatment of pulp, preferably recycled pulp, and especially using hydrogen peroxide or other peroxides as bleaching agent. Such media typically comprise fibres, water, hydrogen peroxide, and other additives. Catalase may be generated in such media by microbial action which in turn catalyses the decomposition of hydrogen peroxide.
Other examples of technical media comprise adhesive and starch based formulations, formulations for leather soaking or formulations for the treatment of textiles.
It may also be possible to control catalase in industrial waste systems whereby excess catalase can be inhibited once it has broken down the hydrogen peroxide or primarily where an excess of hydrogen peroxide is employed which then requires catalase to be used in controlled amounts.
The amount of HCHO-releasing chemicals added to the medium may be selected by the skilled artisan according to the desired effect and of course depends on the con¬ centration of the enzyme to be inhibited.
In a preferred embodiment of the invention the HCHO-releasing chemicals are used at concentrations below their Minimum Inhibitory Concentration (M. I. C), i.e. the aim of the invention is not to combat the microbes which produce enzymes thereby causing ad¬ verse effects but to inhibit the enzymes themselves in order to avoid said adverse ef¬ fects. It's the advantage of said strategy that much lower amounts of active ingredients are sufficient in order to obtain the same effect.
The M. I. C. of component (HT) mentioned above with regard to bacteria such as Staphylococcus aureas, Bacillus subtilis, Klebsiella pneumoniae, Enterobacter aero- genes, yeasts such as Candida albicans, or moulds such as penicillium funiculosum is 500 ppm, and the M. I. C. of (TD) mentioned above with regard to several organisms is 1000 ppm.
Therefore, the HCHO-releasing chemicals are preferably used at concentrations well below 500 ppm, more preferably below 250 ppm, and most preferably below 125 ppm. Typically, a concentration of 1 to 100 ppm is sufficient for inhibition, preferably 2 to 80 more preferably 5 to 60 ppm, most preferred 10 to 50 ppm, and for example 20 to 40 ppm.
The pH-value for using the HCHO-releasing chemicals may be selected by the skilled artisan according to the desired effect. Usually, the pH-value should be above 4, though the invention is not restricted to said range. Preferably, the range of pH-values is from 6 to 14, more preferably 7 to 13, most preferably 8 to 12, and for example 9 to 12.
The temperature usually is around ambient temperature, however the temperature range may be typically from O0C to 7O0C, preferably 10 to 5O0C.
In order to provide better protection for processes and materials it is of course possible to combine the HCHO-releasing chemicals inhibiting enzymes with typical biocides which combat microbes themselves. Examples of such biocides comprise one or more components selected from the group of alcohols, isothiazolones, activated halogen compounds, formaldehyde release compounds, phenolic compounds, aldehydes, acids and esters, biphenyls, urea derivatives, O-acetals, O-formals, N-acetals, N-formals, benzamidines, phthalimides, pyridine derivatives, quaternary ammonium and phospho- nium compounds, amines, amphoteric compounds, dithiocarbamates, compounds con¬ taining active oxygen and mixtures of any of these. Preferably, the active component is selected from at least one of 2-bromo-2-nitropropane-1 ,3-diol, 1 ,2-benzisothiazol-
3(2H)-one, 5-chloro-2-methyl-2H-isothiazol-3-one, 2-methyl-2H-isothiazol-3-one, tetra- hydro-1 ,3I4I6-tetrakis(hydroxymethyl)-imidazo[4,5-d]imida2ole-2,5(2H,3H)-dioneI 1 ,3- dimethyl-5,5-dimethylhydantoin and a polyvinylamine, 3-Bromo-1-chloro-5,5-dimethyl- 2,4-imidazoIinedione), 2,2-Dibromo-3-Nitrilopropionamide, hydrogen peroxide, perace- tic acid.
Such combinations provide an improved protection.
Examples which follow illustrate the invention:
The performance of the HCHO-releasing chemicals as compared to other components was evaluated using the following test procedure:
Test solution: - Aqueous solution of NaOH ( 0,6 g/l)
- 25 ppm H2O2
115 IU/ml of catalase
The pH of the solution was 11 ,0. No bacteria were used in the test solution.
To the test solution HCHO-releasing chemicals and other compounds to be tested were added in the concentrations given below. The tests were performed at ambient temperatures and the concentration of H2O2 monitored as a function of time.
The test data are summarized in table 1 :
The examples and comparative examples demonstrate that the HCHO-releasing chemicals exhibit a better performance than the dialdehydes disclosed in WO 95/00439.
In the control solution after 10 min nearly all H2O2 decomposed, and after 15 min no H202was present in the test solution.
The use of HCHO-releasing chemicals significantly enhanced the time for complete decomposition of H2O2.
Table 1 also contains the theoretical HCHO-concentration in solution resulting from complete hydrolysis. Although the theoretical amounts of free HCHO generated via the HCHO-releasing chemicals is less than 50 ppm HCHO as in the comparative example, surprisingly, the HCHO-releasing compounds exhibit an even better performance than free HCHO.
Table 1 : Concentration of H2O2 in the test solutions as a function of time. OI theoretical HCHO-concentration in solution resulting from complete hydrolysis.
Claims
1. Use of HCHO-releasing chemicals for the inactivation of enzymes.
2. Use according to claim 1 , wherein the enzyme is at least one selected from the group of catalase, amylase, protease, and cellulase.
3. Use according to claim 2, wherein the enzyme is catalase
4. Use according to any one of claims 1 to 3, wherein the HCHO-releasing chemi¬ cals are used at a concentration of less than 500 ppm.
5. Use according to any one of claims 1 to 4, wherein the HCHO-releasing chemi¬ cals are used at pH > 4.
6. Use according to any one of claims 1 to 5, wherein the HCHO-releasing chemi¬ cals are selected from the group of 1 ,3,5-Tris-(2-hydroxyethyl)-1 ,3,5- hexahydrotriazine and lmidazo[4,5-d]imidazol-2,5-(1H, 3H)-dione-tetrahydro- 1,3,4,6-tetrakis-(hydroxymethyl).
7. Use according to any one of claims 1 to 6, wherein the enzyme to be inhibited is present in a production process or recirculating circuit for the production and/or treatment of pulp using peroxides as bleaching agent.
8. Use according to claims 1 to 7, wherein the pulp is recycled pulp.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB0421359A GB0421359D0 (en) | 2004-09-24 | 2004-09-24 | Method for the inactivation of enzymes |
| GB0421359.1 | 2004-09-24 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO2006032450A1 true WO2006032450A1 (en) | 2006-03-30 |
Family
ID=33397261
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/EP2005/010123 WO2006032450A1 (en) | 2004-09-24 | 2005-09-20 | Method for the inactivation of enzymes |
Country Status (2)
| Country | Link |
|---|---|
| GB (1) | GB0421359D0 (en) |
| WO (1) | WO2006032450A1 (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2390408A1 (en) * | 2010-05-31 | 2011-11-30 | Kemira Oyj | Control of enzymes in the production of pulp |
| US8246778B2 (en) | 2008-11-21 | 2012-08-21 | Buckman Laboratories International, Inc. | Method for controlling enzymatic decomposition of peroxide |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2269191A (en) * | 1992-07-29 | 1994-02-02 | Solvay Interox Ltd | Method of treating aqueous process liquors |
| US5728263A (en) * | 1919-06-17 | 1998-03-17 | Cellkem Oy | Method for inhibiting enzymatic decomposition of peroxide in the treating of fiber pulp using dialdehydes and acetals |
| US5885412A (en) * | 1993-12-23 | 1999-03-23 | Bim Kemi Ab | Inhibition of hydrogen peroxide decomposing enzymes during bleaching of cellulose fibers |
| WO2001094692A2 (en) * | 2000-06-08 | 2001-12-13 | Lonza Inc. | Aldehyde donors for stabilizing peroxides in papermaking applications |
-
2004
- 2004-09-24 GB GB0421359A patent/GB0421359D0/en not_active Ceased
-
2005
- 2005-09-20 WO PCT/EP2005/010123 patent/WO2006032450A1/en active Application Filing
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5728263A (en) * | 1919-06-17 | 1998-03-17 | Cellkem Oy | Method for inhibiting enzymatic decomposition of peroxide in the treating of fiber pulp using dialdehydes and acetals |
| GB2269191A (en) * | 1992-07-29 | 1994-02-02 | Solvay Interox Ltd | Method of treating aqueous process liquors |
| US5885412A (en) * | 1993-12-23 | 1999-03-23 | Bim Kemi Ab | Inhibition of hydrogen peroxide decomposing enzymes during bleaching of cellulose fibers |
| WO2001094692A2 (en) * | 2000-06-08 | 2001-12-13 | Lonza Inc. | Aldehyde donors for stabilizing peroxides in papermaking applications |
Non-Patent Citations (4)
| Title |
|---|
| HARMAT N J S ET AL: "1,2-disubstituted cyclohexane derived tripeptide aldehydes as novel selective thrombin inhibitors", BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, OXFORD, GB, vol. 8, no. 10, 19 May 1998 (1998-05-19), pages 1249 - 1254, XP004137056, ISSN: 0960-894X * |
| SASAKI T ET AL: "INHIBITORY EFFECT OF DI- AND TRIPEPTIDYL ALDEHYDES ON CALPAINS AND CATHEPSINS", JOURNAL OF ENZYME INHIBITION, NEW YORK, NY, US, vol. 3, no. 3, January 1990 (1990-01-01), pages 195 - 201, XP000386338 * |
| SHEPHERD T A ET AL: "Small peptidic aldehyde inhibitors of human rhinovirus 3C protease", BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, OXFORD, GB, vol. 6, no. 23, 3 December 1996 (1996-12-03), pages 2893 - 2896, XP004136100, ISSN: 0960-894X * |
| WOO J-T ET AL: "Peptidyl aldehyde derivatives as potent and selective inhibitors of cathepsin L", BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, OXFORD, GB, vol. 5, no. 14, 20 July 1995 (1995-07-20), pages 1501 - 1504, XP004135433, ISSN: 0960-894X * |
Cited By (4)
| 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 |
| EP2390408A1 (en) * | 2010-05-31 | 2011-11-30 | Kemira Oyj | Control of enzymes in the production of pulp |
| WO2011151260A1 (en) * | 2010-05-31 | 2011-12-08 | Kemira Oyj | Control of enzymes in the production of pulp |
| CN102971460A (en) * | 2010-05-31 | 2013-03-13 | 凯米拉公司 | Control of enzymes in the production of pulp |
Also Published As
| Publication number | Publication date |
|---|---|
| GB0421359D0 (en) | 2004-10-27 |
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