CA2543818A1 - Method for the modification of polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres, using a cutinase enzyme - Google Patents
Method for the modification of polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres, using a cutinase enzyme Download PDFInfo
- Publication number
- CA2543818A1 CA2543818A1 CA002543818A CA2543818A CA2543818A1 CA 2543818 A1 CA2543818 A1 CA 2543818A1 CA 002543818 A CA002543818 A CA 002543818A CA 2543818 A CA2543818 A CA 2543818A CA 2543818 A1 CA2543818 A1 CA 2543818A1
- Authority
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- Canada
- Prior art keywords
- enzyme
- fibre
- fibres
- comonomer
- vinyl acetate
- 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.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 26
- 239000004952 Polyamide Substances 0.000 title claims abstract description 19
- XTXRWKRVRITETP-UHFFFAOYSA-N Vinyl acetate Chemical compound CC(=O)OC=C XTXRWKRVRITETP-UHFFFAOYSA-N 0.000 title claims abstract description 19
- 229920002647 polyamide Polymers 0.000 title claims abstract description 19
- 229920002239 polyacrylonitrile Polymers 0.000 title claims abstract description 16
- 108010005400 cutinase Proteins 0.000 title abstract description 17
- 230000004048 modification Effects 0.000 title abstract description 7
- 238000012986 modification Methods 0.000 title abstract description 7
- 239000000835 fiber Substances 0.000 claims description 28
- 238000011282 treatment Methods 0.000 claims description 21
- 108090000790 Enzymes Proteins 0.000 claims description 18
- 102000004190 Enzymes Human genes 0.000 claims description 18
- 108090000371 Esterases Proteins 0.000 claims description 9
- 239000000126 substance Substances 0.000 claims description 5
- 125000003277 amino group Chemical group 0.000 claims description 4
- 230000003197 catalytic effect Effects 0.000 claims description 4
- 108090000604 Hydrolases Proteins 0.000 claims description 3
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims description 3
- 102000004169 proteins and genes Human genes 0.000 claims description 3
- 108090000623 proteins and genes Proteins 0.000 claims description 3
- 230000002255 enzymatic effect Effects 0.000 abstract description 5
- 230000007062 hydrolysis Effects 0.000 abstract description 5
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 5
- 238000004043 dyeing Methods 0.000 abstract description 4
- 229920002994 synthetic fiber Polymers 0.000 abstract description 3
- 239000004744 fabric Substances 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 239000000985 reactive dye Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000004753 textile Substances 0.000 description 3
- 229920000742 Cotton Polymers 0.000 description 2
- 241000427940 Fusarium solani Species 0.000 description 2
- 239000013043 chemical agent Substances 0.000 description 2
- 230000009144 enzymatic modification Effects 0.000 description 2
- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 230000003595 spectral effect Effects 0.000 description 2
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
- NLHHRLWOUZZQLW-UHFFFAOYSA-N Acrylonitrile Chemical compound C=CC#N NLHHRLWOUZZQLW-UHFFFAOYSA-N 0.000 description 1
- 108090000531 Amidohydrolases Proteins 0.000 description 1
- 102000004092 Amidohydrolases Human genes 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- GKZCMEUEEFOXIJ-UHFFFAOYSA-N Lanosol Chemical compound OCC1=CC(O)=C(O)C(Br)=C1Br GKZCMEUEEFOXIJ-UHFFFAOYSA-N 0.000 description 1
- SJEYSFABYSGQBG-UHFFFAOYSA-M Patent blue Chemical compound [Na+].C1=CC(N(CC)CC)=CC=C1C(C=1C(=CC(=CC=1)S([O-])(=O)=O)S([O-])(=O)=O)=C1C=CC(=[N+](CC)CC)C=C1 SJEYSFABYSGQBG-UHFFFAOYSA-M 0.000 description 1
- 239000000980 acid dye Substances 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 125000003368 amide group Chemical group 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 125000004185 ester group Chemical group 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 238000001125 extrusion Methods 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 125000005245 nitryl group Chemical group [N+](=O)([O-])* 0.000 description 1
- 125000000636 p-nitrophenyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1*)[N+]([O-])=O 0.000 description 1
- 230000036314 physical performance Effects 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- GHMLBKRAJCXXBS-UHFFFAOYSA-N resorcinol Chemical compound OC1=CC=CC(O)=C1 GHMLBKRAJCXXBS-UHFFFAOYSA-N 0.000 description 1
- 235000011121 sodium hydroxide Nutrition 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 210000002268 wool Anatomy 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
- D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Textile Engineering (AREA)
- Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Abstract
This invention relates a new enzymatic process for the modification of the surface of synthetic fibres using a cutinase enzyme (3.1.1.74). The enzymatic action causes the hydrolysis of the polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres, improving their hydrophilic characteristics and dyeing properties.
Description
DESCRIPTION
"METHOD FOR THE MODIFICATION OF POLYACRYLONITRILE FIBRES
CONTAINING VINYL ACETATE AS A COMONOMER AND POLYAMIDE
FIBRES, USING A CUTINASE ENZYME"
Field of the invention The quality and the processing properties of filaments in the extrusion line, fibres, yarns and textile fabrics can be improved by modifying their surface. The traditional processes used for their modification require chemical agents with negative environmental effects. These negative effects can be prevented by using new processing techniques based on biotechnology.
Enzymatic processes can be used to modify the surface of fabrics constituted by synthetic fibres.
Hydrolysis of polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres results in the formation of hydrophilic groups. The increase in these groups at the surface of the fibres provides hydrophilic characteristics, therefore improving the comfort properties. This treatment also all ows these fibres to be dyed with specific reactive dyes.
"METHOD FOR THE MODIFICATION OF POLYACRYLONITRILE FIBRES
CONTAINING VINYL ACETATE AS A COMONOMER AND POLYAMIDE
FIBRES, USING A CUTINASE ENZYME"
Field of the invention The quality and the processing properties of filaments in the extrusion line, fibres, yarns and textile fabrics can be improved by modifying their surface. The traditional processes used for their modification require chemical agents with negative environmental effects. These negative effects can be prevented by using new processing techniques based on biotechnology.
Enzymatic processes can be used to modify the surface of fabrics constituted by synthetic fibres.
Hydrolysis of polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres results in the formation of hydrophilic groups. The increase in these groups at the surface of the fibres provides hydrophilic characteristics, therefore improving the comfort properties. This treatment also all ows these fibres to be dyed with specific reactive dyes.
Background of the invention Cutinase 3.1.1.74 is an esterase which degrades cutine, a structural polymeric component of plants composed.
of fatty acids (Carvalho et al., Biotech. Bioeng., 1999, 66, 17-34). This is an enzyme which is not very specific and which hydrolyses soluble and non-soluble p-nitrophenyl esters and triglycerides.
Several patents exist relating to the genetic enhancement of Fusarium solani cutinases and their application in the formulation of detergents for washing machines and dishwashers. These products have shown better lipolytiC action than other products previously used (IN183592, EP1290150, AU1503800, AU5488090, US5512203, W09414964, GB2296011, W08809367, EP0399681). In the textile field, the use of cutinases to reduce baCkstaining during stone-wash processes in cotton denim fabrics is also described (CA2413838, US2002066144). Cutinase is also described as being able to degrade aliphatic and aromatic polyesters (US6255451).
Cutinase is an esterase which shares the catalytic triad of serine-histidine-aspartic acid with other esterases and amidases, meaning that the degradation of amides besides ester groups is theoretically possible.
Recent research demonstrates that cutinase has activity in more hydrophobic media due to the external amino acids in the 3D structure (Vidinha et a1. (2003) "Effect of immobilization support, water activity and enzyme ionization state on cutinase activity and enantioselectivity in organic media", Biotechn. Bioeng., accepted).
The chemical agents of fibre modification described in general do not restrict their action to the fibre surface, rather they also penetrate inside and degrade the fibres with deterioration of their properties.
One of the treatments that was normally carried out to improve touch and increase the hydrophilicity of synthetic fibres was alkaline treatment with high concentrations of caustic soda. These treatments were damaging, not only to the physical performance of the fibres but also to the environment where the residues of this product were deposited (US20030119172).
Several chemical methods have been used in order to improve the structure of polyamide fibre. The modification of this fibre, according to the method described in the patent GB1072070, is carried out by acylation of the peptidic groups as well as of the terminal amino groups of the polyamide for greater polyamide reactivity. Another method already described in the patent US5599698 specifies the treatment of polyacrylonitrile fibre Containing vinyl acetate as a comonomer with a nitryl hydratase enzyme, in order to modify its hydrophilicity and consequently its comfort properties, also allowing the polyacrylonitrile fibres containing vinyl acetate as a comonomer to be dyed with acid dyes.
of fatty acids (Carvalho et al., Biotech. Bioeng., 1999, 66, 17-34). This is an enzyme which is not very specific and which hydrolyses soluble and non-soluble p-nitrophenyl esters and triglycerides.
Several patents exist relating to the genetic enhancement of Fusarium solani cutinases and their application in the formulation of detergents for washing machines and dishwashers. These products have shown better lipolytiC action than other products previously used (IN183592, EP1290150, AU1503800, AU5488090, US5512203, W09414964, GB2296011, W08809367, EP0399681). In the textile field, the use of cutinases to reduce baCkstaining during stone-wash processes in cotton denim fabrics is also described (CA2413838, US2002066144). Cutinase is also described as being able to degrade aliphatic and aromatic polyesters (US6255451).
Cutinase is an esterase which shares the catalytic triad of serine-histidine-aspartic acid with other esterases and amidases, meaning that the degradation of amides besides ester groups is theoretically possible.
Recent research demonstrates that cutinase has activity in more hydrophobic media due to the external amino acids in the 3D structure (Vidinha et a1. (2003) "Effect of immobilization support, water activity and enzyme ionization state on cutinase activity and enantioselectivity in organic media", Biotechn. Bioeng., accepted).
The chemical agents of fibre modification described in general do not restrict their action to the fibre surface, rather they also penetrate inside and degrade the fibres with deterioration of their properties.
One of the treatments that was normally carried out to improve touch and increase the hydrophilicity of synthetic fibres was alkaline treatment with high concentrations of caustic soda. These treatments were damaging, not only to the physical performance of the fibres but also to the environment where the residues of this product were deposited (US20030119172).
Several chemical methods have been used in order to improve the structure of polyamide fibre. The modification of this fibre, according to the method described in the patent GB1072070, is carried out by acylation of the peptidic groups as well as of the terminal amino groups of the polyamide for greater polyamide reactivity. Another method already described in the patent US5599698 specifies the treatment of polyacrylonitrile fibre Containing vinyl acetate as a comonomer with a nitryl hydratase enzyme, in order to modify its hydrophilicity and consequently its comfort properties, also allowing the polyacrylonitrile fibres containing vinyl acetate as a comonomer to be dyed with acid dyes.
Detailed Description of the Invention This invention describes the use of cutinase to modify the surface of synthetic polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres. Superficial hydrolysis of the ester and amide groups of the polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres, respectively, causes the formation of hydroxyl groups in the polyacrylonitrile fibres containing vinyl acetate as a comonomer and carboxylic and amino groups in the polyamide fibres. The increase in these groups at the surface of the fibres gives the fabric hydrophilic characteristics, therefore improving the comfort properties. This treatment also allows the polyacrylonitrile fibre containing vinyl acetate as a comonomer to be dyed with reactive dyes (used for cotton) and the polyamide fibre to be dyed with reactive dyes (used for wool). To date, no method for the modification of the vinyl acetate comonomer of acrylic or polyamide has been described in scientific literature or patents.
A first embodiment of the invention consists of a method for the treatment of polyacrylonitrile fibre containing vinyl acetate as a comonomer, which comprises the contact of the fibre with an enzyme solution in order to modify the chemical surface of the fibre, increasing the number of hydrophilic hydroxyl groups.
A second embodiment of the invention consists of a method for the treatment of polyamide fibre, which comprises the contact of the fibre with an enzyme solution in order to modify the chemical surface of the fibre, increasing the number of hydrophilic amino groups.
The treatment of the polyacrylonitrile fibre containing vinyl acetate as a comonomer or the polyamide fibre is preferably carried out using an enzyme with esterase action.
The enzyme preferably Contains the catalytic triad of serine-histidine-aspartic acid.
The abovementioned enzyme esterase is preferably a hydrolase that degrades cutine.
The amount of enzyme used is normally between 1 and 400 g of protein per kg of fibre.
In both of the embodiments described above, a treatment bath with a retrievable and reusable enzyme is used.
Examples The method consists of the chemical modification of the surface of polyacrylonitrile fibres containing vinyl acetate as a comonomer (constituted by about 93%
acrylonitrile and 7% vinyl acetate) and polyamide fibres through the action of a Cutinase solution obtained from the heterologous expression of Fusarium solani p.isi cutinase, by the Escherichia coli DHB4 transformed strain.
The treatment was carried out in a ROTAWASH
machine that simulates dyeings and other textile treatments. Each container had between 1 and 2U (~.mol/min as pNPP - paranitrophenolpalmitate) of cutinase activity.
Example 1:
Enzymatic modification of~lyacrylonitrile fibre containing vinyl acetate as a comonomer Samples of 0.7 g of polyacrylonitrile fabric containing vinyl acetate as a Comonomer were washed with water containing 1 g/L of Lutensol and dried at 50°C. The samples were then placed in a container with 1 U of cutinase, in a bath ratio of 1:35 (p/v). The treatment was carried out at pH 7.5 and at 30°C, for a period of 700 hours. The samples were removed from the solution, washed with water containing 2 g/L of Na2C03 and dried at room temperature.
Hydrolysis was confirmed by the formation of acetic acid arid the dyeing of the treated samples. No acetic acid was detected in the treatment baths. The samples were dyed with 2% reactive dye Remazol Brilliant _ 7 _ Blue, using a bath ratio of 1:50 (p/v), at 70°C. In the samples treated for 700 hours with the enzymatic solution of cutinase, the value of K/S (spectral coefficient) increased by an average of 30% in relation to the non treated sample.
Example 2:
Enzymatic modification of polyamide fibre Similar treatments were carried out to polyamide fabric using the following parameters: fabric samples of 1 g were washed with water containing 1 g/L of Lutensol and dried at 40°C. They were then placed in a specific container in the ROTAWASH machine with 2 U of cutinase, in a bath ratio of 1:200 (p/v). The treatment was carried out at pH 8.5 at 30°C, for a period of 97 hours. The samples were removed from the solution, washed with water containing 2 g/L of Na2C03 and dried at 40°C. The hydrolysis that occurred in the samples treated with the enzymatic solution was verified through dyeing with a reactive dye. The samples treated for 97 hours were dyed with 2% reactive dye (Lanasol Red 66), obtained from CIBA, using a bath ratio of 1:100, at 60 °C. In the samples treated, the value of K/S (spectral coefficient) increased in relation to the non-treated sample by 11.670 (60°C).
A first embodiment of the invention consists of a method for the treatment of polyacrylonitrile fibre containing vinyl acetate as a comonomer, which comprises the contact of the fibre with an enzyme solution in order to modify the chemical surface of the fibre, increasing the number of hydrophilic hydroxyl groups.
A second embodiment of the invention consists of a method for the treatment of polyamide fibre, which comprises the contact of the fibre with an enzyme solution in order to modify the chemical surface of the fibre, increasing the number of hydrophilic amino groups.
The treatment of the polyacrylonitrile fibre containing vinyl acetate as a comonomer or the polyamide fibre is preferably carried out using an enzyme with esterase action.
The enzyme preferably Contains the catalytic triad of serine-histidine-aspartic acid.
The abovementioned enzyme esterase is preferably a hydrolase that degrades cutine.
The amount of enzyme used is normally between 1 and 400 g of protein per kg of fibre.
In both of the embodiments described above, a treatment bath with a retrievable and reusable enzyme is used.
Examples The method consists of the chemical modification of the surface of polyacrylonitrile fibres containing vinyl acetate as a comonomer (constituted by about 93%
acrylonitrile and 7% vinyl acetate) and polyamide fibres through the action of a Cutinase solution obtained from the heterologous expression of Fusarium solani p.isi cutinase, by the Escherichia coli DHB4 transformed strain.
The treatment was carried out in a ROTAWASH
machine that simulates dyeings and other textile treatments. Each container had between 1 and 2U (~.mol/min as pNPP - paranitrophenolpalmitate) of cutinase activity.
Example 1:
Enzymatic modification of~lyacrylonitrile fibre containing vinyl acetate as a comonomer Samples of 0.7 g of polyacrylonitrile fabric containing vinyl acetate as a Comonomer were washed with water containing 1 g/L of Lutensol and dried at 50°C. The samples were then placed in a container with 1 U of cutinase, in a bath ratio of 1:35 (p/v). The treatment was carried out at pH 7.5 and at 30°C, for a period of 700 hours. The samples were removed from the solution, washed with water containing 2 g/L of Na2C03 and dried at room temperature.
Hydrolysis was confirmed by the formation of acetic acid arid the dyeing of the treated samples. No acetic acid was detected in the treatment baths. The samples were dyed with 2% reactive dye Remazol Brilliant _ 7 _ Blue, using a bath ratio of 1:50 (p/v), at 70°C. In the samples treated for 700 hours with the enzymatic solution of cutinase, the value of K/S (spectral coefficient) increased by an average of 30% in relation to the non treated sample.
Example 2:
Enzymatic modification of polyamide fibre Similar treatments were carried out to polyamide fabric using the following parameters: fabric samples of 1 g were washed with water containing 1 g/L of Lutensol and dried at 40°C. They were then placed in a specific container in the ROTAWASH machine with 2 U of cutinase, in a bath ratio of 1:200 (p/v). The treatment was carried out at pH 8.5 at 30°C, for a period of 97 hours. The samples were removed from the solution, washed with water containing 2 g/L of Na2C03 and dried at 40°C. The hydrolysis that occurred in the samples treated with the enzymatic solution was verified through dyeing with a reactive dye. The samples treated for 97 hours were dyed with 2% reactive dye (Lanasol Red 66), obtained from CIBA, using a bath ratio of 1:100, at 60 °C. In the samples treated, the value of K/S (spectral coefficient) increased in relation to the non-treated sample by 11.670 (60°C).
Claims (11)
1. Method for the treatment of polyacrylonitrile fibre containing vinyl acetate as a comonomer, characterised in that it comprises the contact of the fibre with an enzyme solution in order to modify the chemical surface of the fibre, increasing the number of hydrophilic hydroxyl groups.
2. Method according to claim 1, characterised in that it comprises the treatment of the polyacrylonitrile fibre containing vinyl acetate as comonomer with an enzyme with esterase action.
3. Method according to Claim 1, characterised in that the enzyme contains the catalytic triad of serine-histidine-aspartic acid.
4. Method according to claim 1, characterised in that the enzyme esterase is a hydrolase that degrades cutine.
5. Method according to claim 1, characterised by the use of an amount of enzyme between 1 and 400 g of protein per Kg of fibre.
6. Method for the treatment method of polyamide fibre, characterised in that it comprises the contact of the fibre with an enzyme solution in order to modify the chemical surface of the fibre, increasing the number of hydrophilic amino groups.
7. Method according to claim 6, characterised in that it comprises the treatment of the polyamide fibre with an enzyme with esterase action.
8. Method according to claim 6, characterised in that the enzyme contains the catalytic triad of serine-histidine-aspartic acid.
9. Method according to claim 6, characterised in that the enzyme esterase is a hydrolase that degrades cutine.
10. Method according to claim 6, characterised by the use of an amount of enzyme between 1 and 400 g of protein per Kg of fibre.
11. Method according to claims 1 and 6, characterised by the use of a treatment bath with a retrievable and reusable enzyme.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| PT103035A PT103035A (en) | 2003-10-29 | 2003-10-29 | METHOD FOR MODIFYING POLYACRYLONYRYL FIBERS WITH VINYL ACETATE AS A COMONOMER AND POLYAMIDE, USING A CUTINASE ENZYME |
| PTPT103035 | 2003-10-29 | ||
| PCT/PT2004/000025 WO2005040487A1 (en) | 2003-10-29 | 2004-10-28 | Method for the modification of polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres, using a cutinase enzyme |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2543818A1 true CA2543818A1 (en) | 2005-05-06 |
Family
ID=34511367
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002543818A Abandoned CA2543818A1 (en) | 2003-10-29 | 2004-10-28 | Method for the modification of polyacrylonitrile fibres containing vinyl acetate as a comonomer and polyamide fibres, using a cutinase enzyme |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US20070275453A1 (en) |
| EP (1) | EP1694903A1 (en) |
| CA (1) | CA2543818A1 (en) |
| PT (1) | PT103035A (en) |
| WO (1) | WO2005040487A1 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2145904A1 (en) * | 2008-07-18 | 2010-01-20 | Basf Se | Method for enzyme-catalysed hydrolysis of polyacrylic acid esters and esterases to be used |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5599698A (en) * | 1994-12-27 | 1997-02-04 | Montefibre S.P.A. | Modified materials based on polyacrylonitrile and process for their production |
| FR2736928B1 (en) * | 1995-07-18 | 1997-10-17 | Rhone Poulenc Fibres & Polymer | ENZYMES HAVING AMIDASE ACTIVITY MICRO-ORGANISMS LIKELY TO PRODUCE SUCH ENZYMES AND METHOD FOR HYDROLYSIS OF AMIDES USING THE SAME |
| CA2244694A1 (en) * | 1996-03-06 | 1997-09-12 | The Regents Of The University Of California | Enzyme treatment to enhance wettability and absorbency of textiles |
-
2003
- 2003-10-29 PT PT103035A patent/PT103035A/en active IP Right Grant
-
2004
- 2004-10-28 WO PCT/PT2004/000025 patent/WO2005040487A1/en active Application Filing
- 2004-10-28 CA CA002543818A patent/CA2543818A1/en not_active Abandoned
- 2004-10-28 US US10/577,012 patent/US20070275453A1/en not_active Abandoned
- 2004-10-28 EP EP04775191A patent/EP1694903A1/en not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| PT103035A (en) | 2005-04-29 |
| EP1694903A1 (en) | 2006-08-30 |
| US20070275453A1 (en) | 2007-11-29 |
| WO2005040487A1 (en) | 2005-05-06 |
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