CN1321180C - Method for raising stability for preserving catalase prepared by microbiological method - Google Patents
Method for raising stability for preserving catalase prepared by microbiological method Download PDFInfo
- Publication number
- CN1321180C CN1321180C CNB2004100146315A CN200410014631A CN1321180C CN 1321180 C CN1321180 C CN 1321180C CN B2004100146315 A CNB2004100146315 A CN B2004100146315A CN 200410014631 A CN200410014631 A CN 200410014631A CN 1321180 C CN1321180 C CN 1321180C
- Authority
- CN
- China
- Prior art keywords
- catalase
- enzyme
- liquid
- prepared
- present
- 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.)
- Expired - Fee Related
Links
Landscapes
- Enzymes And Modification Thereof (AREA)
Abstract
The present invention relates to a method for improving the storage stability of catalase prepared by a microbiological method, which relates to a biologic enzyme used for the cleaning production of textile industry. In the present invention, thermosacus aurantiancus IFO9862 which is purchased from Japanese NBRC (an original Japanese ' NITE biological resource center ') is used as an original strain; a certain amount of sodium chloride or gelatin or glycerol as a stabilizing agent is added in catalase prepared by the submerged fermentation of liquid after the catalase prepared by the submerged fermentation of liquid is processed by ultrafiltration and concentration. The mixture liquid is stored for 60d at the temperature of 40 DEG C, and the retention rate of enzyme activity reaches more than 90%. The stabilizing agent of the present invention has low price, the problem that the catalase of liquid is easy to lose activity can be solved, and the stability of the enzyme is obviously improved.
Description
Technical field
The present invention is a kind of method that improves the catalase storage stability of microbial method preparation.Relate to the used a kind of biological enzyme of textile industry cleaner production.
Background technology
Hydrogen peroxide is that its technology can be accepted on ecology, and is feasible economically to all are from the most general SYNTHETIC OPTICAL WHITNER of natural fibers use of plant or animal now.Therefore hydrogen peroxide bleaching or concise " chlorine-free bleaching " technology are just obtaining application more and more widely.But in dye bath,, can cause reactive dyestuffs to fade to oxidation-sensitive if there is hydrogen peroxide.Verified, even the less change of dye molecule all can cause the disappearance of color and luster.Because strict specification of quality even small color change is arranged on the DYED FABRICS, all can not be accepted commercial.Therefore bleaching process is in case end is to guarantee the back painted security in road, and hydrogen peroxide removal residual after oxygen must being floated is clean, to avoid the dyeing course generation problem thereafter.Traditional technology has unsatisfactory part: repeatedly heat up, wash as need, and may bring into poisonous and material difficult degradation.Catalase reaction speed is very fast: under optimum condition, every mole of catalase can decompose 500 ten thousand moles of hydrogen peroxide in one minute.Therefore, in dyeing and finishing technology, use catalase to substitute residual H in repeatedly cleaning and the chemical reducing agent removal sodium hypochlorite solution
2O
2, have very big economic advantages and environment-friendly advantage.Yet because the easy inactivation of liquid hydrogen peroxide enzyme has limited its widespread use to a certain extent.
Summary of the invention
The purpose of this invention is to provide for catalase preservation effect stablizer preferably.Use stablizer of the present invention can solve the problem of the easy inactivation of liquid hydrogen peroxide enzyme, significantly improved the stability of enzyme.
Technical scheme of the present invention, employing available from golden yellow thermophilic ascomycete (Thermoascus aurantiacus) IFO9862 of the strain of Japanese NBRC (former Japan " slope fermentation research institute ") as starting strain, catalase through the liquid submerged fermentation preparation, enzyme is lived and is 2000U/mL, the fermented liquid suction filtration removed thalline after 10 times of ultrafiltration and concentration, enzyme is lived and is 20000U/mL, add stablizer sodium-chlor 15-25mmol/L or gelatin 0.4-0.6g/L or glycerine 80-100g/L respectively, preserve 60d at 40 ℃, its enzyme is lived retention rate more than 90%.
Beneficial effect of the present invention:
Aspect cost: related stablizer is cheap, and consumption is moderate.
Aspect product quality: owing to added the stablizer that suitable liquid hydrogen peroxide enzyme is preserved, improved the stability of this enzyme largely, preserved 60d at 40 ℃, its enzyme is lived retention rate still more than 90%.
Embodiment
Embodiment 1
Through the catalase that liquid submerged fermentation prepares, suction filtration is removed thalline, and enzyme is lived and is 2000U/mL, is placed on 40 ℃ and preserves 30d and 60d, and its enzyme retention rate alive is respectively 21.3% and 2.4%.After it was carried out 10 times of ultrafiltration and concentration, enzyme was lived and is 20000U/mL, places 40 ℃ to preserve 30d and 60d, and its enzyme retention rate of living is respectively 74.7% and 9.6%.
Embodiment 2
Enzyme liquid after ultrafiltration adds stablizer sodium-chlor 20mmol/L, preserves 60d at 40 ℃, and its enzyme retention rate alive is 94.0%.
Embodiment 3
Enzyme liquid after ultrafiltration adds stablizer gelatin 0.5g/L, preserves 60d at 40 ℃, and its enzyme retention rate alive is 93.9%.
Embodiment 4
Enzyme liquid after ultrafiltration adds stablizer glycerine 90g/L, preserves 60d at 40 ℃, and its enzyme retention rate alive is 90.8%.
Claims (1)
1. method that improves the catalase storage stability of microbial method preparation, it is characterized in that adopting available from golden yellow thermophilic ascomycete (Thermoascus aurantiacus) IFO9862 of the strain of Japanese NBRC as starting strain, catalase through the liquid submerged fermentation preparation, the fermented liquid suction filtration removed thalline after 10 times of ultrafiltration and concentration, add stablizer sodium-chlor 15-25mmol/L or glycerine 80-100g/L respectively, preserve 60d at 40 ℃, its enzyme is lived retention rate more than 90%.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNB2004100146315A CN1321180C (en) | 2004-04-09 | 2004-04-09 | Method for raising stability for preserving catalase prepared by microbiological method |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNB2004100146315A CN1321180C (en) | 2004-04-09 | 2004-04-09 | Method for raising stability for preserving catalase prepared by microbiological method |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1563373A CN1563373A (en) | 2005-01-12 |
| CN1321180C true CN1321180C (en) | 2007-06-13 |
Family
ID=34478493
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNB2004100146315A Expired - Fee Related CN1321180C (en) | 2004-04-09 | 2004-04-09 | Method for raising stability for preserving catalase prepared by microbiological method |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN1321180C (en) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN100434515C (en) * | 2005-12-23 | 2008-11-19 | 上海复星长征医学科学有限公司 | Enzyme combining stabilizer |
| SG148934A1 (en) | 2007-06-11 | 2009-01-29 | Novozymes As | A process for combined biopolishing and bleach clean-up |
| CN102239264B (en) * | 2008-10-03 | 2013-11-20 | 纳幕尔杜邦公司 | Stabilization of perhydrolases in a formulation with a carboxylic acid ester |
| CN101955923B (en) * | 2010-09-30 | 2012-05-23 | 江南大学 | Method for improving storage stability of catalase |
| TR201909592T4 (en) | 2012-08-16 | 2019-07-22 | Novozymes As | The method for treating textile with endoglucanase. |
| WO2014086659A2 (en) | 2012-12-06 | 2014-06-12 | Ahmedabad Textile Industry's Research Association | Method for enzymatical preparation of textiles |
| EP2970542B1 (en) | 2013-03-15 | 2019-07-24 | Lubrizol Advanced Materials, Inc. | Itaconic acid copolymers |
| CN103243566B (en) * | 2013-05-25 | 2015-03-25 | 上海秋橙新材料科技有限公司 | Bio-enzyme pretreatment method of vinylon-cotton blend fabric |
| CN103266495B (en) * | 2013-05-25 | 2015-08-05 | 上海秋橙新材料科技有限公司 | Cotton-polyester blend biological fabric enzyme pre-treating method |
| CN106574018A (en) | 2014-03-14 | 2017-04-19 | 路博润先进材料公司 | Itaconic acid polymers and copolymers |
| CN105624140A (en) * | 2016-03-29 | 2016-06-01 | 常州大学 | Method for improving storage stability of hydrogen peroxide |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4543326A (en) * | 1981-11-12 | 1985-09-24 | Wako Pure Chemical Industries, Ltd. | Stabilization of oxidase |
| US4596757A (en) * | 1985-04-05 | 1986-06-24 | American Hoechst Corporation | Photopolymerizable dual transfer negative working color proofing system |
-
2004
- 2004-04-09 CN CNB2004100146315A patent/CN1321180C/en not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4543326A (en) * | 1981-11-12 | 1985-09-24 | Wako Pure Chemical Industries, Ltd. | Stabilization of oxidase |
| US4596757A (en) * | 1985-04-05 | 1986-06-24 | American Hoechst Corporation | Photopolymerizable dual transfer negative working color proofing system |
Non-Patent Citations (1)
| Title |
|---|
| 明胶对过氧化氢酶活性保护的研究 刘欣如，吉林师范学院学报，第16卷第11期 1995 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN1563373A (en) | 2005-01-12 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| FI100109B (en) | A microperoxidase preparation containing a hemopeptide as an active component | |
| Moldes et al. | Grape seeds: the best lignocellulosic waste to produce laccase by solid state cultures of Trametes hirsuta | |
| Pazarlıoǧlu et al. | Laccase: production by Trametes versicolor and application to denim washing | |
| CN1321180C (en) | Method for raising stability for preserving catalase prepared by microbiological method | |
| Nyanhongo et al. | Production of laccase by a newly isolated strain of Trametes modesta | |
| Chavan | Indigo dye and reduction techniques | |
| JP3789933B2 (en) | Multi-component bleaching system | |
| ES2267200T3 (en) | CELLULOSE PRODUCED BY ACTINOMYCETES AND METHOD TO PRODUCE IT. | |
| Hess et al. | Enhanced formation of extracellular laccase activity by the white-rot fungus Trametes multicolor | |
| Couto et al. | Lacasses in the textile industry | |
| Domı́nguez et al. | Design of a new rotating drum bioreactor for ligninolytic enzyme production by Phanerochaete chrysosporium grown on an inert support | |
| JPH11502701A (en) | Novel endoglucanase | |
| Liu et al. | Ecofriendly pretreatment of grey cotton fabric with enzymes in supercritical carbon dioxide fluid | |
| Fruhwirth et al. | An immobilised catalase peroxidase from the alkalothermophilic Bacillus SF for the treatment of textile-bleaching effluents | |
| Mojsov | Trends in bio-processing of textiles | |
| Roy Choudhury | Sustainable textile wet processing: Applications of enzymes | |
| Rodríguez Couto et al. | Ligninolytic enzyme production and the ability of decolourisation of Poly R-478 in packed-bed bioreactors by Phanerochaete chrysosporium | |
| Halim et al. | Chemistry of sustainable coloration of textile materials | |
| Tochetto et al. | Can enzymatic processes transform textile processes? A critical analysis of the industrial application | |
| Jajpura | Enzyme: a bio catalyst for cleaning up textile and apparel sector | |
| Ratnapandian | Natural colorants and its recent developments | |
| JP5888906B2 (en) | Novel microorganism and colored wastewater treatment method using the same | |
| Liu et al. | Laccase production by Trameteshirsuta, characterization, and its capability of decoloring chlorophyll | |
| Saravanan et al. | Bleaching of cotton fabrics using hydrogen peroxide produced by glucose oxidase | |
| Singh et al. | Decolourisation of chemically different dyes by enzymes from spent compost of Pleurotus sajor-caju and their kinetics |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C14 | Grant of patent or utility model | ||
| GR01 | Patent grant | ||
| C19 | Lapse of patent right due to non-payment of the annual fee | ||
| CF01 | Termination of patent right due to non-payment of annual fee |