EP1386010A1 - Improvements in leather processing - Google Patents

Improvements in leather processing

Info

Publication number
EP1386010A1
EP1386010A1 EP02766642A EP02766642A EP1386010A1 EP 1386010 A1 EP1386010 A1 EP 1386010A1 EP 02766642 A EP02766642 A EP 02766642A EP 02766642 A EP02766642 A EP 02766642A EP 1386010 A1 EP1386010 A1 EP 1386010A1
Authority
EP
European Patent Office
Prior art keywords
leather
process according
range
enzyme
elastase
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.)
Granted
Application number
EP02766642A
Other languages
German (de)
French (fr)
Other versions
EP1386010B1 (en
Inventor
Tony Covington
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
BLC Leather Technology Centre Ltd
Original Assignee
BLC Leather Technology Centre Ltd
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
Priority claimed from GB0110695A external-priority patent/GB0110695D0/en
Application filed by BLC Leather Technology Centre Ltd filed Critical BLC Leather Technology Centre Ltd
Publication of EP1386010A1 publication Critical patent/EP1386010A1/en
Application granted granted Critical
Publication of EP1386010B1 publication Critical patent/EP1386010B1/en
Anticipated expiration legal-status Critical
Expired - Lifetime legal-status Critical Current

Links

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

  • the corium 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 av- erage 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 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.
  • 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 difunc- tional, 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 glutaral- dehyde produce leathers which are significantly coloured. Therefore, the preferred cross- linkers are the active-hydroxyl phosphonium salts, which are significantly less toxic than most of the other reagents and produce white leather.
  • Lohlein-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 HCI and non-degraded casein is precipitated with sodium sulphate.
  • the filtrate's content of HCI 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 resis- tance 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.

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)

Abstract

The invention relates to improvements in the processing of animal skins to create leather and results in improved leather quality, in terms of softness, and markedly increased area yield. According to the present invention there is provided 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. The invention applies particularly, although not exclusively, to clothing leather and upholstery leather production.

Description

IMPROVEMENTS IN LEATHER PROCESSING
FIELD OF THE INVENTION
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.
BACKBROUND OF THE INVENTION 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 col- lagen 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 corium 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 av- erage 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 elastic.
The area of the skin or leather is determined by the corium 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. In grain leather, the grain also limits the softness of the leather, since the presence of the elatin has a stiffening effect.
In order to increase area yield and softness of leather, it has been proposed to degrade the elastin. Applying elastolytic enzymes to raw, untanned hides or skins results in the desired area grain, but at the cost of (often unacceptable) looseness in the corium. The latter effect is due to the fact that elastolytic enzyme formulations or products have predominantly proteolytic activity and this causes considerable degradation to both the corium itself and to the non- structural proteins within the corium matrix, which contribute to the desired properties of the leather.
One solution to the problem would be to degrade the elastin by attacking it with elas- tase alone. However, there is no known source of elastase without accompanying protease. Furthermore, separating enzymes, to purify the elastase, is a high cost procedure, which makes the product prohibitively expensive for large scale industrial production.
SUMMARY OF THE INVENTION 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.
According to the present invention there is provided 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.
DETAILED DESCRIPTION OF THE INVENTION
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).
The process of this invention exploits the difference in chemistry of the collagen and the elastin. Those differences are set out in Table I, which contains some elements of their amino acid compositions: there is some dispute in the literature concerning the precise amino acid composition of these proteins, hence the figures quoted are indicative, based on published figures.
Table I. Indicative amino acid compositions of bovine type I collagen and elastin (residues per 1000 residues).
It can be seen that 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. Hence, it has long been known that it is very difficult to modify the properties of chrome tanned leather by applying proteolytic enzymes, such as those used in the processes leading up to tanning. On the other hand, the lack of acidic groups in elastin means that chrome tanning has little effect on elastin, so there is no conferring of enzymatic resistance. Therefore, the elastin in chrome tanned pelt remains vulnerable to degradation by elastase. Consequently, treating chrome leather (leather tanned with chromium (III) salts) with 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.
It is an important feature of the process of this invention that it is applied to chrome tanned leather, in which chromium (III) is covalently bound to the protein and hence is not displaced in solution; if it were displaced, the enzymes would be deactivated by the resulting tanning effect applied to themselves. This would occur if, for example, aluminium (III) or zirconium (IV) were to be included in the tannage. Typical chromium (III) tanning procedures are disclosed in Chem. Soc. Rev. 26(2), III, 1997 (Modern Tanning Chemistry - A.D. Covington).
The role of 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 difunc- tional, 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 glutaral- dehyde produce leathers which are significantly coloured. Therefore, the preferred cross- linkers are the active-hydroxyl phosphonium salts, which are significantly less toxic than most of the other reagents and produce white leather.
Other 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 polyphe- nols, 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 Lohlein 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. One Lohlein-Volhard unit (LVU) 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 HCI and non-degraded casein is precipitated with sodium sulphate. The filtrate's content of HCI 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.
It is a noteworthy feature of the invention, that 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 resis- tance 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.
The effectiveness of the invention is highlighted by treatment of 'double face' leather, e.g. English domestic wool sheepskins, following drying after chrome tanning. This is the worst case situation, because the flesh layer is still in place and the presence of the wool in the grain limits the ability of the grain to relax. Nevertheless, surprisingly it was found that the leather became significantly softer and measurably gained in area; see Example 1 below. In the case of chrome tanned upholstery leather the area gain can be considerable, up to 10%; see Example 2 below. The more powerful effect in the upholstery leather is because the pelt is split prior to tanning, so the tannage is applied only to the grain split and the restricting effect of the flesh layer on the ability of the grain and corium layers to relax is removed.
A major impact of the new technology lies in the increased profitability of the product. This is exemplified by a tannery processing about 50 tonnes of hide per day: the annual added profit from applying this invention would be about £3M.
The following three recipes give examples on the proposed use of the enzyme in the neutralization step.
Recipe 1 :
UPHOLSTERY LEATHER WITH NOVOCOR AX German bovine wetblue, 1.1-1.2 mm
All % refer to shaved weight
* Trade name of BASF,
Recipe 2:
DOUBLE FACE LAMBSKIN GARMENT WITH NOVOCOR AX English domestic lambskin
Float ratio: 15L/skin
* Trade name of TFL Recipe 3:
UPHOLSTRY RETANNING WITH NOVOCOR AX Raw material: Wet blue, Danish cows, 1.1-1.2 mm
All % refer to shaved weight:
The invention is further illustrated by the following non-limitative Examples.
Example 1
Wool sheepskins (50 pieces) in the dyed, crust state were wetted back, adjusted to pH 8.0 with sodium hydrogen carbonate, then treated with 1.0 wt-%? Pyrase® 250MP (Trade Name for a proteolytic/elastolytic enzyme formulation supplied by Novozymes A/S) at 40°C for 60 minutes. Pyrase® is a protease produced by surmerged fermentation of a genetically modified Bacillus.
After dyeing in the normal way, it was found that the softness had increased, markedly improving the handle. Area Measurement revealed that the average area gain of the experimental leathers was 3% greater than normal production. In this production, although the area gain is commercially important, the more significant result is the improvement in quality with regard to softness.
Example 2
In two separate processes conducted in a tannery, single bovine upholstery hides, pre- viously split in the limed state and chrome tanned all as usual, were neutralised to pH 7.0, when they were treated with 1.0 wt-% Pyrase® 250MP for 2 hours at 40°C.
Table II. Mean results for trials on upholstery hides.
From Table II, after drying in the normal way, the experimental hides were on average 9.0% bigger in area than untreated control hides, comparing the crust area with the wet blue area. In addition, the Pyrase treated hides were almost twice as strong, as measured by both tear and tensile strength.

Claims

1. A process for improving softness and/or area yield of leather which comprises providing animal skins tanned with chromium (III) salts or an aldehydic tanning agent, and treating the tanned skins with an enzyme mixture comprising a protease and an elastase.
2. The process according to claim 1 , wherein the enzyme mixture is a microbial protease with an elastase component.
3. The process according to claim 1 or 2, wherein the enzyme mixture is added to the neutralisation bath preceding a post-tanning treatment.
4. The process according to any of the preceding claims, wherein the enzymatic treatment is carried out at a temperature in the range of 35-45°C, more preferably around 40°C
5. The process according to any of the preceding claims, wherein the enzymatic treatment is carried out at a pH in the range of pH 5-8, preferably pH 6-7.
6. The process according to any of the preceding claims, wherein the enzymatic treatment is carried out at a reaction time in the range of 30-180 minutes, preferably in the range of 60-120 minutes.
7. The process according to any of the preceding claims, wherein the enzyme dosage is in the range of 2-10 kg enzyme product per ton of pelt, preferably in the range of 3-5 kg enzyme product per ton of pelt.
8. The process according to claim 1 , substantially as described herein in Example 1 or 2.
EP02766642A 2001-05-01 2002-04-26 Improvements in leather processing Expired - Lifetime EP1386010B1 (en)

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 true EP1386010A1 (en) 2004-02-04
EP1386010B1 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 (en)
KR (1) KR100871597B1 (en)
CN (1) CN1273619C (en)
AR (1) AR049240A1 (en)
AT (1) ATE497024T1 (en)
AU (1) AU2002308063B2 (en)
BR (1) BR0209303B1 (en)
DE (1) DE60239055D1 (en)
MX (1) MXPA03009853A (en)
NZ (1) NZ529172A (en)
TR (1) TR200301830T2 (en)
WO (1) WO2002088397A1 (en)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101307368B (en) * 2008-07-01 2012-03-21 中国科学院昆明动物研究所 Method for processing elephant skin for making attitude specimen of elephas maximus
CN102002541B (en) * 2010-05-24 2013-04-24 孟凡标 Integrated process of tanning leather from quebracho extracts
CN102827967A (en) * 2012-09-14 2012-12-19 兴业皮革科技股份有限公司 Method for increasing leather area yield
CN107619892A (en) * 2016-07-15 2018-01-23 北京市纺织纤维检验所 A kind of processing method of stable Chrome-free leather area
US12421563B2 (en) 2019-10-30 2025-09-23 Kao Corporation Leather improving agent

Family Cites Families (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE4035839A1 (en) * 1990-11-10 1992-05-14 Roehm Gmbh PROTEASE AS A ACTIVE ENZYME, TENSIDE-FREE, FIXED ENZYMERS
DE4439990A1 (en) 1994-11-09 1996-05-15 Bayer Ag Leather tanning agents and agents for dyes
RU2096466C1 (en) * 1996-06-25 1997-11-20 Центральный научно-исследовательский институт кожевенно-обувной промышленности Method of leather raw treatment
RU2114917C1 (en) * 1996-07-16 1998-07-10 Татьяна Флавиановна Миронова Method of processing rabbit skins
US6340458B1 (en) * 1999-11-19 2002-01-22 Reva Amir Use of enzymes for skin expansion
JP4114046B2 (en) * 2002-07-12 2008-07-09 川村通商株式会社 Enzymatic hair removal treatment and enzymatic hair removal method

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO02088397A1 *

Also Published As

Publication number Publication date
AR049240A1 (en) 2006-07-12
EP1386010B1 (en) 2011-01-26
NZ529172A (en) 2005-09-30
TR200301830T2 (en) 2004-12-21
KR100871597B1 (en) 2008-12-02
AU2002308063B2 (en) 2007-10-25
WO2002088397A1 (en) 2002-11-07
ATE497024T1 (en) 2011-02-15
DE60239055D1 (en) 2011-03-10
BR0209303A (en) 2004-06-15
MXPA03009853A (en) 2004-12-06
KR20040015233A (en) 2004-02-18
CN1273619C (en) 2006-09-06
CN1505686A (en) 2004-06-16
BR0209303B1 (en) 2011-10-04

Similar Documents

Publication Publication Date Title
CA1167608A (en) Polymer products in the form of solutions or aqueous dispersions for treating pelts and leather
US4875900A (en) Method of treating leather
AU2008327902B2 (en) Agent and method for tanning skins and pelts
Zhang et al. An integrated pickling-bating technology for reducing ammonia-nitrogen and chloride pollution in leather manufacturing
WO2008093353A1 (en) An improved process for dehairing and fibre opening of hide/skin
AU2002308063B2 (en) Improvements in leather processing
GB2054642A (en) Manufacturing leather
Li et al. A novel approach to clean tanning technology
Zhang et al. Ammonium-free and grain-protection deliming technology with the combination of aromatic sulfonic acid and sodium dihydrogen phosphate in leather manufacture
AU2002308063A1 (en) Improvements in leather processing
US20100263134A1 (en) Leather processing
EP3425069B1 (en) A deliming process
US7063728B2 (en) Process for making chrome tanned leathers
EP1304389B1 (en) Enzymatic unhairing agent for use in tanning for producing leather and method for enzymatic unhairing treatment
AU656448B2 (en) Use of silica sols for obtaining a hide which is called a stabilized pickled white or stabilized white
CN1245523C (en) Process for producing leather using protease and process for treating waste from leather processing using it
US5580355A (en) Leather tanning agent and standardizing agents for dyestuffs
KR100441377B1 (en) Method for preparation of leather using protease and method for treatment of wastes derived from leather production process using the same
US5340737A (en) Process of preparing pepsin for bating hides
US7651531B2 (en) Bio-tanning process for leather making
Durga et al. Rapid fiber opening process for skins: an approach for fail-safe chemical-free process
Kopp et al. Application of Cellulose in Leather
ALI Chemical studies to improve chrome absorption in leather tanning
EP1460137A1 (en) Fatliquors and use thereof

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20031201

AK Designated contracting states

Kind code of ref document: A1

Designated state(s): AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU MC NL PT SE TR

AX Request for extension of the european patent

Extension state: AL LT LV MK RO SI

17Q First examination report despatched

Effective date: 20091209

GRAP Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOSNIGR1

GRAS Grant fee paid

Free format text: ORIGINAL CODE: EPIDOSNIGR3

GRAA (expected) grant

Free format text: ORIGINAL CODE: 0009210

AK Designated contracting states

Kind code of ref document: B1

Designated state(s): AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU MC NL PT SE TR

REG Reference to a national code

Ref country code: GB

Ref legal event code: FG4D

REG Reference to a national code

Ref country code: CH

Ref legal event code: EP

REG Reference to a national code

Ref country code: IE

Ref legal event code: FG4D

REF Corresponds to:

Ref document number: 60239055

Country of ref document: DE

Date of ref document: 20110310

Kind code of ref document: P

REG Reference to a national code

Ref country code: DE

Ref legal event code: R096

Ref document number: 60239055

Country of ref document: DE

Effective date: 20110310

REG Reference to a national code

Ref country code: NL

Ref legal event code: VDEP

Effective date: 20110126

Ref country code: ES

Ref legal event code: FG2A

Ref document number: 2360181

Country of ref document: ES

Kind code of ref document: T3

Effective date: 20110601

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: GR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110427

Ref country code: PT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110526

Ref country code: SE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: AT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

Ref country code: BE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

Ref country code: NL

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

Ref country code: FI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

Ref country code: CY

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: DK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20110126

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MC

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110430

REG Reference to a national code

Ref country code: CH

Ref legal event code: PL

PLBE No opposition filed within time limit

Free format text: ORIGINAL CODE: 0009261

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: NO OPPOSITION FILED WITHIN TIME LIMIT

26N No opposition filed

Effective date: 20111027

REG Reference to a national code

Ref country code: FR

Ref legal event code: ST

Effective date: 20111230

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: FR

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110502

Ref country code: CH

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110430

Ref country code: LI

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110430

REG Reference to a national code

Ref country code: IE

Ref legal event code: MM4A

REG Reference to a national code

Ref country code: DE

Ref legal event code: R097

Ref document number: 60239055

Country of ref document: DE

Effective date: 20111027

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: IE

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110426

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LU

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110426

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: GB

Payment date: 20180621

Year of fee payment: 17

GBPC Gb: european patent ceased through non-payment of renewal fee

Effective date: 20190426

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: GB

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190426

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: DE

Payment date: 20210428

Year of fee payment: 20

Ref country code: IT

Payment date: 20210421

Year of fee payment: 20

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: TR

Payment date: 20210407

Year of fee payment: 20

Ref country code: ES

Payment date: 20210504

Year of fee payment: 20

REG Reference to a national code

Ref country code: DE

Ref legal event code: R071

Ref document number: 60239055

Country of ref document: DE

REG Reference to a national code

Ref country code: ES

Ref legal event code: FD2A

Effective date: 20220902

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: ES

Free format text: LAPSE BECAUSE OF EXPIRATION OF PROTECTION

Effective date: 20220427