EP1386010B1 - Improvements in leather processing - Google Patents
Improvements in leather processing Download PDFInfo
- Publication number
- EP1386010B1 EP1386010B1 EP02766642A EP02766642A EP1386010B1 EP 1386010 B1 EP1386010 B1 EP 1386010B1 EP 02766642 A EP02766642 A EP 02766642A EP 02766642 A EP02766642 A EP 02766642A EP 1386010 B1 EP1386010 B1 EP 1386010B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- leather
- process according
- enzyme
- range
- carried out
- 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 - Lifetime
Links
- 239000010985 leather Substances 0.000 title claims abstract description 44
- 230000006872 improvement Effects 0.000 title abstract description 4
- 238000000034 method Methods 0.000 claims abstract description 29
- 102000004190 Enzymes Human genes 0.000 claims abstract description 28
- 108090000790 Enzymes Proteins 0.000 claims abstract description 28
- 230000008569 process Effects 0.000 claims abstract description 25
- 239000000203 mixture Substances 0.000 claims abstract description 20
- 102000016387 Pancreatic elastase Human genes 0.000 claims abstract description 15
- 108010067372 Pancreatic elastase Proteins 0.000 claims abstract description 15
- 108091005804 Peptidases Proteins 0.000 claims abstract description 15
- 239000004365 Protease Substances 0.000 claims abstract description 13
- BFGKITSFLPAWGI-UHFFFAOYSA-N chromium(3+) Chemical compound [Cr+3] BFGKITSFLPAWGI-UHFFFAOYSA-N 0.000 claims abstract description 9
- 241001465754 Metazoa Species 0.000 claims abstract description 4
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 3
- 230000002797 proteolythic effect Effects 0.000 claims description 7
- 230000003246 elastolytic effect Effects 0.000 claims description 6
- 230000002255 enzymatic effect Effects 0.000 claims description 6
- 238000006386 neutralization reaction Methods 0.000 claims description 6
- 241000283690 Bos taurus Species 0.000 claims description 5
- 238000009472 formulation Methods 0.000 claims description 5
- 210000002268 wool Anatomy 0.000 claims description 4
- 239000003795 chemical substances by application Substances 0.000 claims description 3
- 230000000813 microbial effect Effects 0.000 claims description 3
- 230000035484 reaction time Effects 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 abstract description 4
- 125000002485 formyl group Chemical class [H]C(*)=O 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 19
- 102000016942 Elastin Human genes 0.000 description 13
- 108010014258 Elastin Proteins 0.000 description 13
- 229920002549 elastin Polymers 0.000 description 13
- 102000035195 Peptidases Human genes 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- 239000000047 product Substances 0.000 description 9
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 8
- 102000008186 Collagen Human genes 0.000 description 8
- 108010035532 Collagen Proteins 0.000 description 8
- 229920001436 collagen Polymers 0.000 description 8
- 101710185622 Pyrrolidone-carboxylate peptidase Proteins 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 239000005018 casein Substances 0.000 description 6
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 6
- 235000021240 caseins Nutrition 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 235000018102 proteins Nutrition 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 230000015556 catabolic process Effects 0.000 description 5
- 238000006731 degradation reaction Methods 0.000 description 5
- 230000002378 acidificating effect Effects 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 4
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 description 3
- 101710172711 Structural protein Proteins 0.000 description 3
- 150000001299 aldehydes Chemical class 0.000 description 3
- 239000002994 raw material Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- BVKZGUZCCUSVTD-UHFFFAOYSA-M Bicarbonate Chemical compound OC([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-M 0.000 description 2
- 102000012422 Collagen Type I Human genes 0.000 description 2
- 108010022452 Collagen Type I Proteins 0.000 description 2
- 239000004971 Cross linker Substances 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 239000000835 fiber Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 229910052684 Cerium Inorganic materials 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 229910052685 Curium Inorganic materials 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical class O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- REDXJYDRNCIFBQ-UHFFFAOYSA-N aluminium(3+) Chemical compound [Al+3] REDXJYDRNCIFBQ-UHFFFAOYSA-N 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- GWXLDORMOJMVQZ-UHFFFAOYSA-N cerium Chemical compound [Ce] GWXLDORMOJMVQZ-UHFFFAOYSA-N 0.000 description 1
- -1 chromium (III) salts Chemical class 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 238000004043 dyeing Methods 0.000 description 1
- KOWWOODYPWDWOJ-LVBPXUMQSA-N elatine Chemical compound C([C@]12CN(C3[C@@]45OCO[C@]44[C@H]6[C@@H](OC)[C@@H]([C@H](C4)OC)C[C@H]6[C@@]3([C@@H]1[C@@H]5OC)[C@@H](OC)CC2)CC)OC(=O)C1=CC=CC=C1N1C(=O)CC(C)C1=O KOWWOODYPWDWOJ-LVBPXUMQSA-N 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 231100001231 less toxic Toxicity 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 150000002917 oxazolidines Chemical class 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- RDBMUARQWLPMNW-UHFFFAOYSA-N phosphanylmethanol Chemical class OCP RDBMUARQWLPMNW-UHFFFAOYSA-N 0.000 description 1
- 150000008442 polyphenolic compounds Chemical class 0.000 description 1
- 235000013824 polyphenols Nutrition 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- GBNDTYKAOXLLID-UHFFFAOYSA-N zirconium(4+) ion Chemical compound [Zr+4] GBNDTYKAOXLLID-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C14—SKINS; HIDES; PELTS; LEATHER
- C14C—CHEMICAL TREATMENT OF HIDES, SKINS OR LEATHER, e.g. TANNING, IMPREGNATING, FINISHING; APPARATUS THEREFOR; COMPOSITIONS FOR TANNING
- C14C3/00—Tanning; Compositions for tanning
- C14C3/02—Chemical tanning
Definitions
- This invention concerns improvements in the processing of animal skins to create leather.
- the invention results in improved leather quality, in terms of softness, and markedly increased area yield.
- the invention applies particularly, although not exclusively, to clothing leather and upholstery leather production.
- the area of a piece of leather and, to a lesser extent, its softness are primarily controlled by structural features of the material from which the leather is made, that is hide or skin.
- This raw material comprises three main layers which each contribute to the properties of the piece.
- the flesh layer is the part that was closest to the animal's body. It is composed of collagen fibres that have a distinctly low angle of weave, lying almost parallel to the surfaces of the hide or skin. This means that the layer has limited ability to stretch by distorting the weave horizontally and hence limits the area of the skin or leather.
- the curium is the middle section and is the thickest part of the original skin. It is composed of a matrix of Interconnecting collagen fibres: in the raw material the fibres have an average angle of weave close to 45°.
- the weave allows the skin or leather to adopt a larger area, if the angle is lowered by relaxation or straining, or to adopt a smaller area, if the angle of weave is raised during the leather making processes, for example by swelling the pelt.
- the grain layer is the outermost part of the skin. It has a larger area than the corium and, because it is composed of very fine fibres, it is weaker than the corium, so it adopts a convoluted arrangement, which allows it to stretch without rupturing.
- the reversibility of the stretching mechanism is made possible by the presence of elastin, a fibrous protein which behaves very much like plastic.
- the area of the skin or leather is determined by the cerium angle of weave, which in turn is controlled by the area of the flesh layer, if it is present in the leather, and the area of the grain layer, which is usually present in the leather: of the two controlling mechanisms, the more important is the grain.
- grain leather the grain also limits the softness of the leather, since the presence of the elatin has a stiffening effect.
- the present invention is based on the finding that mixtures of proteolytic and elastolytic enzymes can be successfully used to improve softness and area yield of leather by treating skins tanned with chromium (III) salts, or aldehydic tanning agents.
- a process for improving area yield and/or softness of leather which comprises treating chromium (III) or aldehyde tanned skins with an enzyme composition which is a mixture of at least one protease and at least one elastase.
- Enzyme mixtures containing protease(s) and elastase(s) are commercially available. They are typically derived from bacterial sources in the form of a so-called microbial protease, which in the absence of an expensive purification procedure also contains elastase.
- the present invention advantageously uses the relatively inexpensive unpurified "protease".
- An example of en enzyme mixture commercially available is NovoCor® AX (available from Novozymes A/S).
- elastin possesses an order of magnitude fewer acidic and basic groups on sidechains than collagen and almost double the amount of apolar sidechains.
- the basis of the invention is that by tanning using chromium (III) salts, chromium (III) is fixed to protein at the acidic side-chains, so the availability of such groups in collagen allows the tannage to work.
- Part of the definition of the tanning effect is that the protein acquires resistance to microbial attack i.e. putrefaction by the action of proteolytic enzymes.
- proteolytic enzymes such as those used in the processes leading up to tanning.
- the lack of acidic groups in elastin means that chrome tanning has little effect on elastin, so there is no conferring of enzymatic resistance.
- chrome leather leather tanned with chromium (III) salts
- an enzyme mixture containing an elastase and a protease will result in elastin degradation, but no damage to the collagen and other tanned non-structural proteins.
- chromium (III) tannage also applies to covalent reaction at the amino groups i.e. by aldehydic tanning reactions, assuming the bound reagent is not released from a polymeric state by hydrolysis.
- Suitable aldehydic tanning agents include aldehydes themselves, mono- and difunctional, aldehyde derivatives and compounds which have at least partial aldehydic function or reactive hydroxyl function, such as hydroxymethyl phosphonium salts, typically the sulphate or chloride, and especially oxazolidines. It is recognised that not all the potential crosslinkers are acceptable in the workplace because of toxicity hazards. In addition, all derivatives of glutaraldehyde produce leathers which are significantly coloured. Therefore, the preferred crosslinkers are the active-hydroxyl phosphonium salts, which are significantly less toxic than most of the other reagents and produce white leather.
- tanning reactions that might be used prior to the treatment are likely to result in failure to gain a positive result; such tannages include vegetable tanning with plant polyphenols, syntan and resin tanning. The reason is that these reactions are labile, i.e. reversible, and they rely in some considerable part on forming hydrophobic interactions with the protein.
- the process of the invention is particularly simple, merely requiring the enzymes to be added to the leather during the normal process of neutralisation prior to conventional post-tanning. Therefore, there is no extra process step involved in the overall treatment of skins to produce leather. This means that the process timing remains unaffected and, importantly, there is no capital cost associated with its introduction. This means that the new process can be applied in all tanneries.
- the process is remarkably safe, with regard to damaging the leather.
- the pH of the leather does not have to be high, because the enzyme mixture can be used at a concentration high enough to produce the effect, without the necessity to operate at the pH optimum for the elastase.
- the resistance of the collagen is high, although it can be damaged, but not until extremely high concentration of protease is used at significantly elevated temperature, e.g. 50°C.
- Additional aspects of the safety of the process are: the reaction does not have to be prolonged for penetration by the enzyme, because access to the elastin is only a short distance through the grain surface and the elastin does not have to be completely dissolved, it is sufficient to cause significant degradation, so that its function is eliminated.
- the new technology has the advantage of not being restricted to specific relative activities of elastase and protease in the formulation.
- the enzymatic reaction may preferably be carried out at a temperature in the range of 35-45°C, more preferably around 40°C, a pH preferably in the range of pH 5-8, more preferably pH 6-7, and a reaction time preferably in the range of 30-180 minutes, more preferably in the range of 60-120 minutes.
- the enzyme dosage may preferably be in the range of 2-10 kg enzyme product per ton of pelt, more preferably in the range of 3-5 kg enzyme product per ton of pelt.
- the enzyme product may have an activity measured in Löhlein Volhard Units (LVU) per gram in the range of 50,000 LVU/g to 250,000 LVU/g, preferably 100,000 LVU/g to 150,000 LVU/g.
- Löhlein Volhard Units Löhlein Volhard Units
- Löhlein-Volhard unit is the amount of enzyme, which degrades 1.725 mg casein under the conditions set out here.
- Proteases degrade casein from an alkaline casein solution under the following standard conditions: Temperature 37°C, pH 8.2 and reaction time 60 minutes.
- the reaction is stopped by adding HCl and non-degraded casein is precipitated with sodium sulphate.
- the filtrate's content of HCl which is not bound to degraded casein or its degradation products is determined by titration with NaOH. The more casein which is degraded and so non-precipitable, the more acid there will be in the filtrate.
- the consumption of NaOH in back titration therefore serves as a direct measure of the level of proteolytic activity.
- the softness and area gains can be achieved without loosening the leather. This is due to two complementary factors. First, the relaxation of the corium is limited by the effects of the tannage, essentially fixing the fibre structure in place, so retaining much of the handle characteristics of the leather. Second, the resistance of the protein to proteolytic attack means that the non-structural protein is not removed nor is the collagen dissolved, so the filling of the fibre structure is maintained. Importantly, that resistance to degradation includes the grain-corium junction, where damage is seen as a loosening of the layers, resulting in poor break, i.e. coarse rippling of the grain surface when the leather is bent. The maintaining of the 'tight' structure is a vital quality determining factor in the finished leather.
- German bovine wetblue 1.1-1.2 mm
Landscapes
- Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Treatment And Processing Of Natural Fur Or Leather (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB0110695 | 2001-05-01 | ||
| GB0110695A GB0110695D0 (en) | 2001-05-01 | 2001-05-01 | Improvements in leather processing |
| DKPA200101798 | 2001-12-04 | ||
| DK200101798 | 2001-12-04 | ||
| PCT/EP2002/004635 WO2002088397A1 (en) | 2001-05-01 | 2002-04-26 | Improvements in leather processing |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EP1386010A1 EP1386010A1 (en) | 2004-02-04 |
| EP1386010B1 true EP1386010B1 (en) | 2011-01-26 |
Family
ID=26069106
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP02766642A Expired - Lifetime EP1386010B1 (en) | 2001-05-01 | 2002-04-26 | Improvements in leather processing |
Country Status (12)
| Country | Link |
|---|---|
| EP (1) | EP1386010B1 (tr) |
| KR (1) | KR100871597B1 (tr) |
| CN (1) | CN1273619C (tr) |
| AR (1) | AR049240A1 (tr) |
| AT (1) | ATE497024T1 (tr) |
| AU (1) | AU2002308063B2 (tr) |
| BR (1) | BR0209303B1 (tr) |
| DE (1) | DE60239055D1 (tr) |
| MX (1) | MXPA03009853A (tr) |
| NZ (1) | NZ529172A (tr) |
| TR (1) | TR200301830T2 (tr) |
| WO (1) | WO2002088397A1 (tr) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101307368B (zh) * | 2008-07-01 | 2012-03-21 | 中国科学院昆明动物研究所 | 用于制作亚洲象姿态标本的象皮处理方法 |
| CN102002541B (zh) * | 2010-05-24 | 2013-04-24 | 孟凡标 | 一种栲胶鞣毛革一体工艺 |
| CN102827967A (zh) * | 2012-09-14 | 2012-12-19 | 兴业皮革科技股份有限公司 | 一种增大皮革面积得率的方法 |
| CN107619892A (zh) * | 2016-07-15 | 2018-01-23 | 北京市纺织纤维检验所 | 一种稳定无铬皮革面积的处理方法 |
| US12421563B2 (en) | 2019-10-30 | 2025-09-23 | Kao Corporation | Leather improving agent |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE4035839A1 (de) * | 1990-11-10 | 1992-05-14 | Roehm Gmbh | Protease als wirkenzym enthaltende, tensidfreie feste enzympraeparate |
| DE4439990A1 (de) | 1994-11-09 | 1996-05-15 | Bayer Ag | Ledergerbstoffe und Stellmittel für Farstoffe |
| RU2096466C1 (ru) * | 1996-06-25 | 1997-11-20 | Центральный научно-исследовательский институт кожевенно-обувной промышленности | Способ обработки кожевенного сырья |
| RU2114917C1 (ru) * | 1996-07-16 | 1998-07-10 | Татьяна Флавиановна Миронова | Способ обработки шкурок кролика |
| US6340458B1 (en) * | 1999-11-19 | 2002-01-22 | Reva Amir | Use of enzymes for skin expansion |
| JP4114046B2 (ja) * | 2002-07-12 | 2008-07-09 | 川村通商株式会社 | 酵素脱毛処理剤および酵素脱毛法 |
-
2002
- 2002-04-26 CN CNB02809137XA patent/CN1273619C/zh not_active Expired - Lifetime
- 2002-04-26 KR KR1020037014268A patent/KR100871597B1/ko not_active Expired - Fee Related
- 2002-04-26 TR TR2003/01830T patent/TR200301830T2/tr unknown
- 2002-04-26 EP EP02766642A patent/EP1386010B1/en not_active Expired - Lifetime
- 2002-04-26 AT AT02766642T patent/ATE497024T1/de not_active IP Right Cessation
- 2002-04-26 MX MXPA03009853A patent/MXPA03009853A/es active IP Right Grant
- 2002-04-26 BR BRPI0209303-0A patent/BR0209303B1/pt not_active IP Right Cessation
- 2002-04-26 WO PCT/EP2002/004635 patent/WO2002088397A1/en not_active Ceased
- 2002-04-26 DE DE60239055T patent/DE60239055D1/de not_active Expired - Lifetime
- 2002-04-26 AU AU2002308063A patent/AU2002308063B2/en not_active Ceased
- 2002-04-26 NZ NZ529172A patent/NZ529172A/en not_active IP Right Cessation
- 2002-04-30 AR ARP020101588A patent/AR049240A1/es unknown
Also Published As
| Publication number | Publication date |
|---|---|
| AR049240A1 (es) | 2006-07-12 |
| NZ529172A (en) | 2005-09-30 |
| TR200301830T2 (tr) | 2004-12-21 |
| EP1386010A1 (en) | 2004-02-04 |
| KR100871597B1 (ko) | 2008-12-02 |
| AU2002308063B2 (en) | 2007-10-25 |
| WO2002088397A1 (en) | 2002-11-07 |
| ATE497024T1 (de) | 2011-02-15 |
| DE60239055D1 (de) | 2011-03-10 |
| BR0209303A (pt) | 2004-06-15 |
| MXPA03009853A (es) | 2004-12-06 |
| KR20040015233A (ko) | 2004-02-18 |
| CN1273619C (zh) | 2006-09-06 |
| CN1505686A (zh) | 2004-06-16 |
| BR0209303B1 (pt) | 2011-10-04 |
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