EP0575927B1 - Procédé de pelage de cuirs et de peaux - Google Patents
Procédé de pelage de cuirs et de peaux Download PDFInfo
- Publication number
- EP0575927B1 EP0575927B1 EP93109846A EP93109846A EP0575927B1 EP 0575927 B1 EP0575927 B1 EP 0575927B1 EP 93109846 A EP93109846 A EP 93109846A EP 93109846 A EP93109846 A EP 93109846A EP 0575927 B1 EP0575927 B1 EP 0575927B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- liming
- alkaline
- elastase
- skins
- proteases
- 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
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
- C14C1/00—Chemical treatment prior to tanning
- C14C1/06—Facilitating unhairing, e.g. by painting, by liming
-
- 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
- C14C1/00—Chemical treatment prior to tanning
- C14C1/06—Facilitating unhairing, e.g. by painting, by liming
- C14C1/065—Enzymatic unhairing
Definitions
- the invention relates to a method for liming skins and furs, the aqueous liming liquor containing alkaline proteases simultaneously with thiourea dioxide.
- THDO thiourea dioxide
- formamidine sulfinic acid was proposed as a sulfide substitute (AT-PS 381 952, EP 197 918).
- This compound has a very high reduction potential compared to cysteine, so that in doses of 0.1-1% by weight, perfect depilation can be achieved together with calcium oxide or calcium carbonate.
- the compound is largely odorless and the degree of preservation of the hair is significantly better than that of a pure sulphide ash.
- the compound has a low toxicity to wastewater, since it is readily biodegradable.
- the present invention thus relates to a process for the liming of hides and skins, the aqueous liming liquors having a pH in the range 10-14, preferably 12-14, containing thiourea dioxide and alkaline proteases AP with elastase activity.
- the liming liquors preferably contain 0.3 to 2% by weight, in particular 0.5 to 1% by weight, of thiourea dioxide together with an effective amount of one or more alkaline proteases AP.
- the liming process in the sense of the present invention summarizes the hair loosening, the actual liming, the skin disruption and, if necessary, the post-liming.
- THDO and alkaline proteases according to the invention is therefore excellently suitable for sulfide-free liming and / or post-liming as well as for low-sulfide liming / post-liming.
- alkaline proteases AP with elastase activity The alkaline proteases AP with elastase activity
- Elastase preparations even in crystallized form, must be regarded as inconsistent from the start; Even the purest preparations still contain a part of proteolytic, non-elastolytic activity. In structure and specific activity, the elastases seem to resemble trypsin and chymotrypsin. The quantitative determinations are based on the (both proteolytic and mucolytic) degradation of the elastin. The main method of determination is the degradation of elastin, which is loaded with dyes such as orcin (or Congo red, dimethylaminonaphthalene sulfonic acid) or fluorescein.
- dyes such as orcin (or Congo red, dimethylaminonaphthalene sulfonic acid) or fluorescein.
- alkaline proteases AP to be used according to the invention with elastase activity are characterized by an optimum activity in the alkaline pH range, generally in the range pH 12 ⁇ 2.
- microorganisms in particular of the bacterial type, especially the bacilli, are currently the preferred starting materials.
- Other examples include Flavobacterium elastolyticum, Chlortridium histolyticum, Staph. epidermis.
- alkaline proteases In the case of preparations of alkaline proteases from Bacillus types, portions of 30-60% by weight of alkaline protease, 0.002-2% by weight of elastase in addition to neutral proteinase and collagenase (see USSR-PS 802 909, Chem. Abstr 94 , 148 340x). Alkaline elastases have recently also been produced as products of genetic manipulation, for example by cloning the alkaline elastase gene from alkalophilic Bacillus and expression in Bacillus subtilis (cf. JP-OS 90 76 586, Chem. Abstr. 115 , 249 561c; Y.Ch. Tsai et al. Biochim.
- EUgly elastase units The units of elastase activity determined in the manner specified there are hereinafter referred to as EUgly elastase units.
- the definition is: One elastase unit (EUgly) corresponds to the extinction of a ⁇ Mol glycine by trinitrobenzenesulfonic acid determination; Analysis conditions: substrate is elastin, in buffer pH 8 and at 37 degrees C whereby the increase in extinction per minute is evaluated.
- the activities of the active enzymes in the enzyme preparations AP are preferably in a certain ratio in the process according to the invention.
- the protease activity of the alkaline protease [in Löhlein-Volhard units (LVE)] divided by a thousand times one Factor F gives the number of elastase activity in the units EUgly chosen for the purposes of the present invention (cf. experimental part). According to the invention, the factor F is between 0.6 and 20, preferably 1 to 5.
- alkaline proteases present in the enzyme preparations AP that can be used according to the invention are characterized in the usual way. (See Kirk-Othmer 3rd. Ed. Vol. 9, pp. 199-202, J. Wiley 1980; Ullmann's Encyclopedia of Industrial Chemistry Vol. A9, pp. 409-414, VCH 1987; L. Keay in "Process Biochemistry 17-21 (1971) These proteases, which mostly belong to the serine type, usually develop their optimum activity in a pH range of about 8-13.
- Bacterial proteases in particular from Bacillus strains, are particularly mentioned, advantageously those which contain the elastase Bring activities from their origin, however, alkaline proteases of different origins can also be combined with one another, the elastase activity having to be introduced by appropriate addition.
- alkaline proteases are, above all, those obtained from Bacillus strains, especially B.subtilis, but also B.formus, B.licheniformis, B.alcalophilus, B.polymixa, B.mesentericus, and also from Streptomyces strains such as S.alcalophilus called.
- the cheapest working temperature with alkaline bacterial proteases is generally 40 - 60 degrees C, with fungal proteases rather at 20 - 40 degrees C.
- Alkaline fungal proteases include those from Aspergillus strains such as A.oryzae, from Penicillinum strains such as P.cyanofulvum or Paecilumyces persicinus.
- the activity of the alkaline fungal proteases is predominantly in the pH range 8.0 - 11.0.
- the proteolytic activity of the alkaline proteases is customarily determined by the Anson hemoglobin method (cf. ML Anson J. Gen. Physiol. 22 , 79 (1939) or by the Löhlein-Volhard method (modified according to TEGEWA, cf. Leder, 22 , 121 - 126 1971).
- One Löhlein-Volhard unit corresponds to the amount of enzyme that causes an increase in hydrolysis product in 20 ml casein filtrate, corresponding to an equivalent of 5.75 ⁇ 10 -3 ml 0.1 N NaOH.
- the protease activity to be used is generally between 1,000 and 60,000 LVU per kg skin, preferably between 2,000 and 14,000 LVU per kg skin.
- the process according to the invention usually comes with amounts of proteases between 0.05 to 0.8% by weight, preferably about 0.1 to 0.3% by weight, as a rule of thumb when using an alkaline bacterial protease (Bacillus alcalophilus) ) with 4,000 LVE based on the weight of the hides and skins used.
- 0.3-2% by weight, preferably 0.5-1% by weight, of thiourea dioxide are used together with the proteolytic enzymes AP.
- the fleet length is usually 100 to 120 wt .-% based on the weight of the hides and skins used.
- the pH range of the liquor is advantageously adjusted using hydrated lime, but sodium hydroxide solution and / or soda can also be used proportionally.
- agents known per se such as, for example, organic amines, for example diethanolamine and / or hydrotropic substances such as, for example, urea, can also be used.
- a dirt switch and a main switch are carried out for the pretreatment (US Pat. No. 4,344,762).
- the main switch as is customary in the business, is carried out using suitable proteases and / or surfactants at a pH of 9-10 over a period of 4-6 hours.
- the main switch fleet is typically drained and a new bath is continued.
- the enzymatic reaction is carried out in the temperature range 20-28 degrees C., preferably at 26 degrees C.
- the liquor containing the enzymes and the thiourea dioxide which is adjusted to an alkaline pH, especially in the range 10-13, is left in a conventional reaction vessel, for example a mixer, tanning drum, etc., with agitation, for example, for a sufficient period of time, as a rule of thumb there are approximately 90 Called minutes, act on the hides and skins until they are largely hair-free. Then it can be post-alkalized with a little alkali, for example 0.2% by weight of a 50% sodium hydroxide solution, preferably with agitation for about 30 minutes.
- a conventional reaction vessel for example a mixer, tanning drum, etc.
- the process according to the invention permits the production of remarkably soft leather, it being particularly emphasized that despite the use of degrading enzymes there is generally a completely intact scar pattern. Overall, the result can be regarded as very surprising, since the nubucking to be expected when using the enzyme in the liming occurs less than the expected loose grain in the flames.
- the required amount can be used Significantly reduce thiourea dioxide.
- the combination of thiourea dioxide and alkaline protease in the liming thus enables an ecologically extremely favorable liming process, which combines high leather quality with sufficient application safety.
- the ecological advantage lies primarily in the good hair preservation and thus the lower COD pollution in the wastewater as well as in the avoidance of any use of sulfide.
- Dirt diverter main diverter is normally used by using tensides at pH 9-10 for 4-6 hours.
- the main switch fleets are drained and all examples continue to work in a new bath.
- 1 unit of elastase corresponds to the amount of enzyme that causes staining with TNBS equivalent to 1 ⁇ mol of glycine per minute in an elastin suspension under the specified standard conditions.
- 250 mg of elastin are weighed into a 50 ml narrow-neck Erlenmeyer flask with a ground glass stopper and mixed with 10 ml of 0.1 m borate buffer.
- the flask is preheated in the shaking thermostat for 10 min. After adding 1 ml of enzyme solution, the mixture is mixed well and the flask is returned to the shaking thermostat. Temperature: 37 degrees C.
- the reaction is stopped by filtering the reaction mixture through a pleated filter after exactly 2 hours.
- the fragments are immediately stained using the TNBS method .
- TNBS Response:
- test tube 100 ⁇ l of the sample are added to 8 ml of TNBS reagent and the test tube is left for 25 min. stand in a water bath at 50 degrees C. After exactly 25 min. the test tube is 5 min. placed in ice water and immediately afterwards the absorbance measured at 420 nm.
- the enzyme solution is only added after the second hour of the reaction time.
- the further treatment is the same as for the main value, i.e. begins with the stopping.
- the staining of glycine with TNBS is measured and in addition ⁇ mol of glycine against O.D. applied.
- the blank value (O.D. of TNBS reagent + 10 l distilled water) was previously subtracted from all glycine values.
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)
- Cosmetics (AREA)
- Glass Compositions (AREA)
- Chemical And Physical Treatments For Wood And The Like (AREA)
- Adornments (AREA)
- Gloves (AREA)
- Laminated Bodies (AREA)
- Coloring (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Claims (6)
- Procédé de pelanage de peaux et de cuirs en poils avec utilisation d'enzymes protéolytiques en bain hydroalcalin, caractérisé en ce que le bain de pelanage contient en même temps, avec un pH dans la gamme de 10 à 14, du dioxyde de thio-urée et des protéases alcalines AP ayant une activité d'élastase.
- Procédé selon la revendication 1, caractérisé en ce que le bain de pelanage contient de 0,3 à 2% en poids de dioxyde de thio-urée.
- Procédé selon la revendication 1 ou 2, caractérisé en ce que le bain de pelanage contient, en plus d'une protéase alcaline [E.C.3.4.21], une proportion efficace d'élastase alcaline [E.C.3.4.21.11].
- Procédé selon l'une quelconque des revendications 1 à 3, caractérisé en ce que le bain de pelanage ne contient pas d'addition de sulfure.
- Procédé selon l'une quelconque des revendications 1 à 4, caractérisé en ce que la protéase alcaline est une protéase bactérienne.
- Procédé selon la revendication 5, caractérisé en ce que la protéase alcaline bactérienne a été obtenue à partir de Bacillus alcalophilus.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE4220838A DE4220838A1 (de) | 1992-06-25 | 1992-06-25 | Verfahren zum Äschern von Häuten und Fellen |
DE4220838 | 1992-06-25 |
Publications (3)
Publication Number | Publication Date |
---|---|
EP0575927A2 EP0575927A2 (fr) | 1993-12-29 |
EP0575927A3 EP0575927A3 (fr) | 1994-02-09 |
EP0575927B1 true EP0575927B1 (fr) | 1996-08-28 |
Family
ID=6461801
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP93109846A Expired - Lifetime EP0575927B1 (fr) | 1992-06-25 | 1993-06-21 | Procédé de pelage de cuirs et de peaux |
Country Status (10)
Country | Link |
---|---|
US (1) | US5508195A (fr) |
EP (1) | EP0575927B1 (fr) |
JP (1) | JP3211914B2 (fr) |
KR (1) | KR100256152B1 (fr) |
AT (1) | ATE141959T1 (fr) |
BR (1) | BR9302644A (fr) |
DE (2) | DE4220838A1 (fr) |
DK (1) | DK0575927T3 (fr) |
ES (1) | ES2091523T3 (fr) |
MX (1) | MX9303809A (fr) |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE4332785A1 (de) * | 1993-09-27 | 1995-03-30 | Roehm Gmbh | Verbessertes enzymunterstütztes Äscherverfahren |
US6340458B1 (en) * | 1999-11-19 | 2002-01-22 | Reva Amir | Use of enzymes for skin expansion |
JP2001164300A (ja) * | 1999-12-06 | 2001-06-19 | Daiwa Kasei Kk | 皮革鞣製における酵素脱毛剤及び酵素脱毛法 |
US20030061666A1 (en) * | 2001-05-01 | 2003-04-03 | Blc Leather Technology Centre Limited Leather Trade House | Leather processing |
US6777219B2 (en) * | 2002-03-13 | 2004-08-17 | Council Of Scientific And Industrial Research | Process for the preparation of alkaline protease |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IT1011668B (it) * | 1973-04-28 | 1977-02-10 | Roehm Gmbh | Procedimento di purga delle pelli |
DE2917376C2 (de) * | 1979-04-28 | 1987-03-26 | Röhm GmbH, 6100 Darmstadt | Enzymatisches Verfahren zur Haargewinnung und zum gleichzeitigen Hautaufschluß |
AT381952B (de) * | 1985-04-03 | 1986-12-29 | Oesterr Chem Werke | Verfahren zum aeschern von haeuten und fellen |
AT388387B (de) * | 1987-09-02 | 1989-06-12 | Oesterr Chem Werke | Verfahren zum nachaeschern von bloesen und spalten |
DE3802640A1 (de) * | 1988-01-29 | 1989-08-03 | Roehm Gmbh | Haarerhaltendes aescherverfahren |
DE3922748B4 (de) * | 1989-07-11 | 2006-01-05 | Röhm GmbH & Co. KG | Enzymatisches Weichverfahren |
-
1992
- 1992-06-25 DE DE4220838A patent/DE4220838A1/de not_active Withdrawn
-
1993
- 1993-06-21 AT AT93109846T patent/ATE141959T1/de not_active IP Right Cessation
- 1993-06-21 DK DK93109846.1T patent/DK0575927T3/da active
- 1993-06-21 DE DE59303551T patent/DE59303551D1/de not_active Expired - Lifetime
- 1993-06-21 EP EP93109846A patent/EP0575927B1/fr not_active Expired - Lifetime
- 1993-06-21 ES ES93109846T patent/ES2091523T3/es not_active Expired - Lifetime
- 1993-06-24 BR BR9302644A patent/BR9302644A/pt not_active IP Right Cessation
- 1993-06-24 MX MX9303809A patent/MX9303809A/es not_active IP Right Cessation
- 1993-06-24 JP JP15340893A patent/JP3211914B2/ja not_active Expired - Fee Related
- 1993-06-25 KR KR1019930011654A patent/KR100256152B1/ko not_active IP Right Cessation
-
1995
- 1995-09-26 US US08/533,674 patent/US5508195A/en not_active Expired - Lifetime
Also Published As
Publication number | Publication date |
---|---|
KR940005808A (ko) | 1994-03-22 |
EP0575927A2 (fr) | 1993-12-29 |
US5508195A (en) | 1996-04-16 |
MX9303809A (es) | 1994-01-31 |
DE4220838A1 (de) | 1994-01-05 |
BR9302644A (pt) | 1994-01-11 |
JP3211914B2 (ja) | 2001-09-25 |
EP0575927A3 (fr) | 1994-02-09 |
ES2091523T3 (es) | 1996-11-01 |
JPH0657300A (ja) | 1994-03-01 |
KR100256152B1 (en) | 2000-06-01 |
DE59303551D1 (de) | 1996-10-02 |
DK0575927T3 (da) | 1996-09-30 |
ATE141959T1 (de) | 1996-09-15 |
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