EP1556522A1 - Procede permettant d'eliminer les substances de corne de la peau des animaux - Google Patents

Procede permettant d'eliminer les substances de corne de la peau des animaux

Info

Publication number
EP1556522A1
EP1556522A1 EP03757967A EP03757967A EP1556522A1 EP 1556522 A1 EP1556522 A1 EP 1556522A1 EP 03757967 A EP03757967 A EP 03757967A EP 03757967 A EP03757967 A EP 03757967A EP 1556522 A1 EP1556522 A1 EP 1556522A1
Authority
EP
European Patent Office
Prior art keywords
weight
compound
hydrolysis
alkyl
peptide bonds
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.)
Withdrawn
Application number
EP03757967A
Other languages
German (de)
English (en)
Inventor
Hans-Georg Lemaire
Tilman Lüdecke TAEGER
Gunther Pabst
Philippe Lamalle
Michael Breuer
Burkhard Kröger
Thomas Subkowski
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.)
BASF SE
Original Assignee
BASF SE
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 DE10249077A external-priority patent/DE10249077A1/de
Priority claimed from DE2003119240 external-priority patent/DE10319240A1/de
Application filed by BASF SE filed Critical BASF SE
Publication of EP1556522A1 publication Critical patent/EP1556522A1/fr
Withdrawn legal-status Critical Current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
    • C14C1/00—Chemical treatment prior to tanning
    • C14C1/06—Facilitating unhairing, e.g. by painting, by liming
    • C14C1/065—Enzymatic unhairing

Definitions

  • the present invention relates to a process for removing home substances from animal skins, characterized in that animal skins in aqueous liquor with 0.05 to 5 wt .-%, based on the salt weight, of one or more compounds of the general formula I
  • R 1 is selected from hydrogen or -CC 12 alkyl, unsubstituted or substituted with one or more SH or OH groups;
  • X 1 to X 4 are the same or different and selected from hydrogen, CC alkyl, OH, SH or N-HR 2 ,
  • At least one further X 1 to X 4 is selected from SH, OH or NH-R 2 ,
  • FR 1,126,252 describes the depilation of animal skins by the action of thioglycolamide (example 1) or thioglycerol (example 2) in the presence of ammonium sulfate at a pH of 7-8.
  • DE 21 31 630 shows that agents consisting of at least 0.25% by weight dimer-captobutanediol and about 0.01 to 40% by weight of a water-soluble guanidine compound and a pH of less than 12 on guinea pigs can be applied to depilate them, or to human cornea to remove calluses without causing skin irritation in guinea pigs or even erythremia (malignant growths in the education system of the red blood cells). The epidermis remains intact in the treatment described in DE 21 31 630.
  • EP-A 0 095 916 discloses the use of formulations containing aminoethanethiol and 1,4-dimercaptobutanediol and an aminoguanidine or diguanide compound in order to eliminate unwanted human body and facial hair.
  • page 2, line 1 it is taught that small thiol molecules are preferably suitable for achieving rapid depilation because they penetrate the skin more quickly. The epidermis is retained in the treatment described in EP-A 0 095 916.
  • EP-A 0 096 521 discloses the use of formulations containing, for example, 1,4-dimercaptobutanediol and an aminoguanidine or diguanidine compound, in order to eliminate unwanted human body and facial hair. The epidermis is retained in the treatment described in EP-A 0 096 521.
  • collagen can be modified by opening S-S bridges in the collagen by reaction with dithioerythrol and subsequent chlorination with chloroacetamide or chloroacetic acid, see. for example E. Heidemann, "Fundamentals of Leather Manufacturing", E. Roether KG Druckerei und Verlag, Darmstadt 1993, page 253. Protein solutions can also be preserved by adding dithioerythrol or dithiothreitol. The preservation is based on a kind of protection against oxidation, because dithioerythrol is usually the first to be oxidized instead of the proteinic SH groups.
  • R ' are selected from hydrogen, an amino group and alkyl radicals with 1 to 6 carbon atoms
  • n is a number from 0 to 6
  • the animal skins are first treated in acid pH range with thioglycolic acid (example 1), mercaptoacetic acid (example 2) or mercaptoethanol and thioglycolic acid (example 3) or a combination with thioglycolic acid and thiourea, but the pretreatment agents have a very unpleasant odor.
  • the task was to provide a method for removing hom substances from animal skins and removing the epidermis as far as possible in the same work step, in which as little unpleasant odors as possible are emitted.
  • the task was to provide a method for removing home substances in such a way that they are destroyed as far as possible.
  • home substances are understood to be calluses, feathers, parts of nails and claws, and in particular hair of animals.
  • the animal skins may contain remains of meat from the animals in question. It is essential to the invention that they contain hom substances.
  • the amount of horny substance, based on the total weight of the animal skin, is not critical.
  • the method according to the invention is suitable both for removing large amounts of horny substance and for removing small hair residues.
  • animal skins are understood not only to mean skins of animals slaughtered or intentionally killed in some other way, but also of those animals which have been caused by accidents, for example traffic accidents or fights with conspecifics or other animals, or by natural causes such as age or Disease have died.
  • the animal skins within the meaning of the present invention are usually vertebrate animal skins such as e.g. Cattle, calves, pigs, goats, sheep, lambs, moose, game such as deer or deer, and also birds such as ostriches, fish or reptiles such as snakes.
  • vertebrate animal skins such as e.g. Cattle, calves, pigs, goats, sheep, lambs, moose, game such as deer or deer, and also birds such as ostriches, fish or reptiles such as snakes.
  • Animal skins are treated with 0.05 to 5% by weight, based on the salt weight, of one or more compounds of the general formula I.
  • R 1 selected from
  • CC 12 alkyl such as methyl, ethyl, n-propyl, iso-propyl, n-butyl, iso-butyl, sec-butyl, tert-butyl, n-pentyl, iso-pentyl, sec.-pentyl, neo-pentyl , 1,2-dimethylpropyl, iso-amyl, n-hexyl, iso-hexyl, sec.-hexyl or n-decyl, particularly preferably CC-alkyl such as methyl, ethyl, n-propyl, iso-propyl, n-butyl, isobutyl, sec-butyl and tert-butyl;
  • C C 2 alkyl substituted with one or more hydroxy or thiol groups such as hydroxymethyl, 2-hydroxyethyl, 1,2-dihydroxyethyl, 3-hydroxy-n-propyl, 2-
  • X 1 to X 4 are the same or different and selected from hydrogen
  • C r C alkyl such as methyl, ethyl, n-propyl, iso-propyl, n-butyl, iso-butyl, sec-butyl and tert-butyl
  • R 2 is hydrogen or
  • CrC 1 alkyl such as methyl, ethyl, n-propyl, iso-propyl, n-butyl, iso-butyl, sec.-
  • At least one X 1 to X 4 means SH, and in the event that R 1 contains neither OH nor SH, at least one further X 1 to X 4 is selected from SH, OH or NH-R 2 .
  • X 2 and X 3 are each very particularly preferably hydroxyl groups.
  • X 1 and X 4 are very particularly preferably each SH groups, and very particularly preferably R 1 is hydrogen.
  • the corresponding alkali and alkaline earth metal salts in particular the mono- and disodium salts, mono- and dipotassium salts and potassium sodium salts of the compounds of the general formula I are also to be mentioned, as are the corresponding calcium and magnesium salts.
  • the ammonium salts or primary, secondary, tertiary and in particular quaternary mono- and diammonium salts and phosphonium salts should also be mentioned. Mixtures of compounds of the general formula I and their corresponding alkali metal or alkaline earth metal salts or ammonium or phosphonium salts can of course also be used.
  • Preferred mono- and diammonium salts have cations of the formula N (R 3 ) (R) (R 5 ) (R 6 ) + , where R 3 to R 6 are each the same or different and selected from hydrogen, CrC ⁇ 2 alkyl, Phenyl or CH 2 -CH 2 -OH. Examples include tetramethylammonium, tetraethylammonium, methyldiethanolammonium and n-butyldiethanolammonium.
  • Preferred mono- and diphosphonium salts have cations of the formula P (R 3 ) (R 4 ) (R 5 ) (R 6 ) + , where R 3 to R 6 are as defined above.
  • I a and I a ' are also referred to as dithiothreitol
  • I b is also referred to as dithioerythrol.
  • the use of racemic dithiothreitol is very particularly preferred.
  • I a, I a 'and I b are practically odorless, easily metered and readily water-soluble compounds.
  • the compounds I a or I a 'and I b are known and commercially available, for example, from Aldrich or AGROS Chemicals. The synthesis of other representatives succeeds as in US 4,472,569 or J. Chem. Soc. 1949, 248 or by analogous implementations.
  • At least one process according to the invention is carried out in the presence of at least one compound which catalyzes the hydrolysis of peptide bonds.
  • At least one of these compounds is preferably an organic compound.
  • organic compounds which catalyze the hydrolysis of peptide bonds are to be understood in particular as enzymes.
  • Exo- and endopeptidases are preferred. It can be representative of the Main classes of proteases, for example serine proteases, cysteine proteases, metalloproteases and acid proteases.
  • Mixtures of 2 enzymes can be used.
  • serine proteases examples include trypsin, chymotrypsin, elastase, thrombin, plasmin, subtilisin and acrosine.
  • cysteine proteases are papain, bromelain and cathepsin B.
  • metalloproteases are carboxypeptidase and ACE (angiotensin conversion enzyme).
  • acidic proteases are pepsin and HIV protease.
  • Serine proteases such as trypsin, chymotrypsin, subtilisin and proteinase K and variants of the above-mentioned enzymes are particularly suitable in the context of the present invention.
  • Variants include, inter alia, mutants which have arisen as a result of insertion (s), deletion (s) and point mutation (s) and which have modified, in particular advantageous properties, in comparison with the protease which was in each case started. Examples of changed properties are thermostability, higher affinity for the substrate to be converted enzymatically, (higher) substrate specificity and shifting the pH optimum into the desired pH range. Fragments of the aforementioned proteases are also referred to as variants in the sense of the present invention.
  • variants are produced recombinantly using the customary methods described, for example, in "Molecular Cloning - A Laboratory Manual” by Sambrook, Fritsch and Maniatis (1989) in a suitable bacterial or fungal host system.
  • Proteases of the four main classes serine, cysteine, metallo- and acid proteases
  • specific keratinolytic activity and mixtures of these enzymes are very particularly preferred.
  • enzymes which hydrolyze peptide bonds are also to be understood as commercially available enzyme formulations. Examples of such products are Alcalase 3.0T, Pyrase 250 MP, conc.
  • PTN 3.0 type p from Novozymes, Prozym 6 from TFL, pancreatin from Nordmark A, Pancreatina enzyme conc. from Scientific Protein Laboratory, Alprolase 3m, Basozym® L10 and Basozym® S20 from BASF-Aktiengesellschaft, Batinase (manufacturer: Genencor), Proleather (manufacturer: Amano), Protease L 660 (manufacturer: Genencor), Esperase (manufacturer: Novo Nordisk), Alcalase 2.4L (manufacturer: Novo Nordisk), Savinase (manufacturer: Novo Nordisk) and Pruafect 4000 L (manufacturer: Genencor).
  • LVEs Löhlein-Volhard units
  • the LVEs are determined by titrimetric methods known per se, which are based on the breakdown of casein by an enzyme formulation to be investigated or an enzyme to be investigated and the subsequent titration of the released carboxyl groups with 0.1 N NaOH.
  • One LVE corresponds to 0.00575 ml 0.1 N NaOH.
  • Salt weight of the animal skin to be treated Salt weight of the animal skin to be treated.
  • Compounds or compounds which catalyze the hydrolysis of peptide bonds are generally used in amounts which are at least a factor of 10, preferably 100, particularly preferably 1000, smaller than the amount of compound I, based on pure compounds.
  • one or more enzymes are used as the compound, it is usually not the pure enzyme that is metered in, but rather one or more solid or liquid formulations containing the compound which catalyzes the hydrolysis of peptide bonds.
  • solid formulations also contain inorganic or organic solids or mixtures thereof.
  • inorganic solids are NaCl, Na 2 SO 4, diatomaceous earth, NaHCO 3 , Na 2 CO 3 or kaolin, concrete, clay minerals;
  • Suitable organic solids are, for example, polysaccharides such as starch and modified starch or urea.
  • Fixed formulations can further reducing substances such as NaHSO 3 contain.
  • Liquid formulations contain at least one liquid solvent or dispersant, for example water or mixtures of water and organic solvent.
  • the animal skins are preferably treated in accordance with the invention with one or more compounds of the general formula I and at least one compound which catalyzes the hydrolysis of peptide bonds, in the liming or the Schwöde, either under hair-destroying or under hair-preserving conditions.
  • the liming or painting instead of the usual concentration of about 2 to 4 wt .-% Na 2 S or NaHS, with a concentration of less than 0.1 wt .-% Na 2 S or NaHS in the same great effect with regard to the removal of home substances.
  • the animal skins are treated according to the invention in an aqueous liquor.
  • the liquor ratio is from 1:10 to 10: 1, preferably 1: 2 to 4: 1, particularly preferably up to 3: 1, based on the skin weight or salt weight of the animal skins.
  • the process according to the invention is carried out at pH values from 6 to 14, preferably from 7 to 12.3, particularly preferably from 7.5 to 10.5 and very particularly preferably from 8.1 to 10.
  • lime also hydrated lime
  • the amount of lime can also be reduced to a maximum of 0.3% by weight.
  • lime is not used.
  • 0.1 to 4% by weight of one or more inorganic basic alkali metal compounds for example one or more hydroxides or carbonates of alkali metals, preferably of Sodium or potassium and most preferably sodium.
  • suitable inorganic basic alkali metal compounds are alkali metal silicates.
  • magnesium oxide, magnesium hydroxide, amines such as, for example, ammonia, methylamine, dimethylamine, ethylamine or triethylamine or combinations of alkali metal compound and one or more amines can be added.
  • the method according to the invention can be carried out in vessels in which cremation is usually carried out.
  • the method according to the invention is preferably carried out in rotatable drums with internals.
  • the speed is usually 0.5 to 100 / min, preferably 1.5 to 15 / min and particularly preferably up to 5 / min. If cremation is to take place over a period of more than 8 hours, the speed is usually 0.5 to 10 / min, preferably 1.5 to 5 / min and particularly preferably up to 3 / min for 5 minutes within each hour, ie 5 Minutes and 55 minutes rest per hour.
  • the pressure and temperature conditions for carrying out the method according to the invention are generally not critical. Carrying out at atmospheric pressure has proven to be suitable; a pressure increased up to 10 bar is also conceivable. Suitable temperatures are 10 to 45 C C, preferably 15 to 35 ° C and particularly preferably 25 to 30 ° C.
  • the compound or compounds of the general formula I can be metered in at the beginning of the liming process, but the animal skins can first be soaked under basic conditions and only after a while one or more compounds of the general formula I and at least one compound which hydrolyses peptide bonds catalyzed, metered. Dosing can be done in one step, i.e. the total amount of the compound or compounds I used is metered in one step; compound I can also be metered in portions or continuously. The same procedure can be followed with at least one compound which catalyzes the hydrolysis of peptide bonds. Compound I and compound which catalyzes the hydrolysis of peptide bonds can be dosed together or separately.
  • the process according to the invention can be carried out in a period of 5 minutes to 48 hours, preferably 10 minutes to 36 hours and particularly preferably 20 minutes to 15 hours.
  • organic polyelectrolytes can be added.
  • Organic polyelectrolytes are generally understood to mean organic polymers with a large number of ionically dissociable groups which can be an integral part of the polymer chains or can be attached to them laterally.
  • each of the statistical repetition units carries at least one group that is ionically dissociable in aqueous solution.
  • so-called ionomers are also counted among the organic polyelectrolytes, which are those organic polymers in which many, but not every repeating unit carries an ionically dissociable group.
  • Polybases polyacids, polyampholytes or their polysalts or mixtures thereof can be used in the process according to the invention.
  • Polyacids are organic polyelectrolytes which dissociate in an aqueous medium with the elimination of protons, for example with polyvinylsulfonic acid, polyvinylsulfuric acid, polyvinylphosphonic acid, polymethacrylic acid or polyacrylic acid as a statistical repeating unit.
  • Polybases are understood to mean those organic polyelectrolytes which contain groups or radicals which can be protonated by reaction with Bronsted acids, for example polyethyleneimines, polyvinylamines or polyvinylpyridines.
  • Polyampholytes are usually understood to mean those polymers which both.
  • Polysalts are usually understood to mean single or in particular multiple deprotonated polyacids.
  • Synthetic polyelectrolytes are preferably used in the process according to the invention.
  • tanning agents that are customary in tanning, for example phosphines, such as, for example, B. triphenylphosphine or tris (2-carboxyethyl) phosphine hydrochloride, further hydroxylamine, urea, guanidine or guanidinium hydrochloride, hydrazine, biocides, surfactants and emulsifiers.
  • phosphines such as, for example, B. triphenylphosphine or tris (2-carboxyethyl) phosphine hydrochloride, further hydroxylamine, urea, guanidine or guanidinium hydrochloride, hydrazine, biocides, surfactants and emulsifiers.
  • the method according to the invention makes it possible to produce excellently hairless pelts. It is found that the epidermis is completely or at least largely detached after a short treatment period. Furthermore, it is found that, in particular in the treatment of animal skins of completely or partially black animals such as, for example, black-colored cattle, a substantial proportion or even all of the melanin is destroyed or removed from the nakedness, so that particularly bright nakedness is obtained.
  • the present invention therefore relates to particularly light pelts produced by the process according to the invention.
  • the pelts produced according to the invention are extremely suitable for the production of leather.
  • the pelts produced according to the invention can be processed further into leather with an improved area yield and less swelling damage, compared with leather which is produced from pelts which are produced with the aid of, for example, Na 2 S, NaHS, Thi - oglycolic acid or aminethanol have been depilated.
  • the pelts produced according to the invention can be dyed in a particularly unimportant manner. If the use of lime is dispensed with in the process according to the invention, then bare lumps according to the invention with particularly flat and smooth scars are obtained.
  • the pickling step can be omitted in the further processing.
  • Another object of the present invention are leather, made from the pelts of the invention. They are characterized by overall advantageous application properties.
  • the wastewater produced in the process according to the invention in particular wastewater from processes according to the invention in which work is carried out without Na 2 S, NaSH or mercaptans such as aminoethanol or thioglycolic acid, can be worked up particularly well.
  • the pelts obtained are separated from the liquor, for example by simply removing the pelts or by draining the liquor.
  • the separated liquor is also referred to below as the residual liquor according to the invention or as the residual liquor.
  • the remaining liquor contains, among other things, reacted and possibly unused compound of the general formula I, basic alkali metal compound or basic amines or lime, and in particular residues of the horny materials separated from the nakedness and the epidermis and optionally melanin and / or degradation products of melanin.
  • the residual liquor according to the invention contains no noticeable proportions from the compound of the general formula I.
  • the present invention furthermore relates to residual liquors which contain only small amounts of Na 2 S and preferably neither Na 2 S nor NaHS and, as organic sulfur compounds, those of the general formula I and their reaction and secondary products from the removal of home substances from animal skins, and see organic sulfur compounds that come from animal skins.
  • the residual liquors according to the invention can now contain melanin and / or breakdown products of melanin as well as melamine and / or breakdown products from melanin.
  • the salt load is considerably reduced by using the method at pH values below 12.4, in particular at pH values from 7 to 10. This is particularly possible if you have not used lime.
  • the liquors according to the invention are obtainable by the process according to the invention. They are almost odorless and particularly easy to work up compared to the residual tannery liquors known from the prior art.
  • the remaining liquors contain reaction and secondary products of compounds of the general formula I which result from the removal of home substances from the animal skins, mainly to name hydrolysis and oxidation products of compounds of the general formula I and proteins hydrolysed with the aid of organic compounds.
  • Another object of the present invention is a method for working up residual liquors according to the invention.
  • the refurbishment process according to the invention comprises several steps.
  • the pelts according to the invention are separated from the lime. This step is naturally only necessary if lime has been used in the treatment of the animal skins, otherwise it is not necessary.
  • the separation is carried out by settling, flotation, decanting, filtering or centrifuging, the separation of the lime by decanting, settling or filtering being preferred in the case of large amounts of residual liquors according to the invention.
  • the first step described above makes lime-free residual liquors accessible.
  • the lime-free residual liquors are then neutralized with acid until a pH of 2 to 8, preferably 3 to 7, particularly preferably 4 to 5 is reached.
  • Organic or inorganic acids are suitable as acids. Examples include hydrochloric acid, phosphoric acid, CO 2 , formic acid, sulfuric acid, acetic acid, citric acid, adipic acid and dicarboxylic acid mixtures of adipic acid, glutaric acid and succinic acid. Acidification can be carried out without any special measures relating to the development of hydrogen sulfide.
  • the present invention furthermore relates to a process for working up residual liquors according to the invention by neutralization and separation of proteins.
  • Casein Hammarsten (commercially available from E. Merck, Art. 2242) was used as a 4% by weight solution.
  • casein A 4% by weight solution of casein was prepared by diluting 40 g of casein at temperatures up to 60 ° C with 800 ml of distilled water and 32 ml of 1N NaOH, mixing until no precipitation or undissolved solids were present. The solution was cooled to 25 ° C. and adjusted to a pH of 8.2 with 0.1 N NaOH or 0.1 N HCl. The mixture was then diluted to 1000 ml with distilled water.
  • a blank was made by mixing the above reagents without adding the formulation of the compound (s) to be examined which catalyzes the hydrolysis of peptide bonds. The work was continued as described above. The difference in NaOH consumption multiplied by 17.39 and divided by the enzyme mass used in g corresponds to the LVE / g.
  • the salted skin of a South German cattle was first at 120 ° C. with 150% by weight of water and 0.2% by weight of C 15 H 3 ⁇ -O- (CH 2 -CH 2 -O) 7 -H for 120 minutes pre-soaked a barrel with slight movement.
  • the liquor was drained (X1-1 "liquor pre-soak", 200% by weight) and then with 100% by weight water, 0.2% by weight C 15 H 31 -O- (CH 2 -CH 2 - O) 7 -H and 0.5% by weight of Na 2 CO 3 soaked for 19 hours with occasional agitation.
  • the liquor was then drained off (X1-2 "liquor main switch", 100% by weight).
  • the data in% by weight relate to the pelt weight, grain gap, 2.8 mm (corresponds to 75% salt weight), unless stated otherwise.
  • the mixture was left to act for 90 minutes with occasional rotation and blunted with 0.2% by weight of sodium formate a pH value of 3.9 after a contact time of 15 hours, a further 0.2% by weight of sodium formate and 0.2% by weight of NaHCO 3 were added, and the pH was now 4.0
  • 0.2% by weight of a dispersion of fungicide Cortymol® Fun diluted with water in a volume ratio of 1: 3 was added.
  • the barrel was rotated at 5 rpm for 5 minutes and left motionless for 55 minutes, after which the movement cycle was repeated. After an exposure time of 10 hours, 50% by weight of water was added, the liquor was drained, 150% by weight of water was added, the mixture was agitated for 10 minutes and the washing liquor was discharged again.
  • Example E6 was carried out analogously, except that NaOH solution was replaced by solid MgO and base was not added.
  • Example E7 was carried out analogously, but the addition of base was dispensed with.
  • Table 2 Experimental parameters of the liming of the examples according to the invention
  • the data in% by weight relate to the pelt weight, grain gap, 2.8 mm (corresponds to 75% salt weight), unless stated otherwise.
  • the mixture was left to act for 90 minutes with occasional rotation and was blunted then with 0.2% by weight of sodium formate to a pH of 3.9 After 15 hours of exposure, a further 0.2% by weight of sodium formate and 0.2% by weight of NaHCO 3 were added The value was now 4.0 After a further 90 minutes, 0.2% by weight of a dispersion of fungicide Cortymol® Fun diluted with water in a volume ratio of 1: 3 was added.
  • the leather produced according to the invention was distinguished from the leather according to the comparative example by a smoother and flatter scars without visible nubucking.
  • the epidermis and the hair with the hair root were completely removed or destroyed from the nakedness according to the examples according to the invention.
  • the very bright appearance of the pelts according to the invention was particularly striking and advantageous.
  • the bluish shadows (reaction of sulfide with iron ions) and lime shadows, which are common for lime / sodium sulphate liming, as well as lime shadows, which can lead to uneven coloring, especially in light shades, were completely absent.
  • the properties of the pelts produced according to the invention with regard to swelling were also excellent.
  • Polymer 1 alternating copolymer of (C 20 -C 24 - olefin) maleic anhydride; molar comonomer fraction of (sum of ⁇ -olefins): maleic anhydride 1: 1, M w 8900 g, preparation described in EP 0412389 B1 as dispersion I. Form of use: 30.2% by weight of dispersion.
  • Polymer 2 30% by weight aqueous, partially neutralized with NaOH polymer solution; Homopolymer of methacrylic acid, M "approx. 10,000 g / mol; K-value according to Fikentscher: 12, viscosity of the 30% by weight solution: 65 mPa-s (DIN EN ISO 3219, 23 ° C), pH 5.1.
  • the leathers obtained after 3 were wilted and folded using conventional methods.
  • the fold thickness of the leather was 2.0-2.2 mm (fold weight corresponds to 25% salt weight).
  • the retanning was carried out as follows:
  • the pretanned leather L V1 or L E1 to L E6 was treated with a liquor length of 100 wt.% Water at 30 ° C. with 15 wt.% Polymer 1 as 30.2 wt.% Aqueous dispersion and 15 wt. % of a 30% by weight aqueous dispersion of polymer 2 (treatment step (a), see Table 4).
  • the commercially available Luganil® Black AS fl. Dye was then added to the leather. Then another 10% by weight of polymer 1 in the form of the 30.2% by weight aqueous dispersion and 2% by weight of polymer 2 as 20% by weight of dispersion were added.
  • the leather remained in the resulting liquor for the time given in Table 4 (exposure step (b)).
  • reaction temperature was then increased by adding 100% water at 45 ° C.
  • the pH was adjusted to 3.5 with formic acid.
  • the leather remained in the resulting liquor for the time given in Table 4 (exposure step (c)).
  • the leather was dyed with a solution of 1.5% by weight of Luganil® Black AS fl. In 100% by weight of water and 0.7% by weight of formic acid over a period of 45 minutes, then washed as usual, fixed and completed.
  • the finished crust leather C V1 (comparative example) and C E1 to C E6 (according to the invention) were obtained.
  • the crust leathers produced from the examples according to the invention differed in their haptic and optical properties by the smoother and finer scars from the comparative example.
  • the liquor limber E1-3 and wash liquor limber E1-4 were combined and adjusted to a pH of 4.5 with concentrated sulfuric acid (98% by weight).
  • the precipitated protein was separated off with a chamber filter press.
  • the data for the combined and cleaned fleets E1-3 and E1-4 are listed under 8.1 (Fleet E1-A).
  • the cleaned liming liquors were ideal as soft liquors. This can significantly reduce water consumption.
  • the remaining liquors of the examples according to the invention could be acidified to a pH of 4.5 with sulfuric acid without the development of hydrogen sulfide, and the precipitated proteins could be removed without problems by filtration.
  • the remaining fleets were also almost clear.
  • the fleet according to comparative experiment V1 could not be acidified without precautionary measures and developed malodorous hydrogen sulfide. Even after processing, it could not be used to soften cattle hides.
  • the softened skin was then processed further in the same way as E1.
  • a crust leather with the same properties as C E1 was obtained.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Detergent Compositions (AREA)
  • Peptides Or Proteins (AREA)
  • Cosmetics (AREA)

Abstract

L'invention concerne un procédé permettant d'éliminer les substances de corne de la peau des animaux. L'invention est caractérisée en ce que l'on traite les peaux d'animaux dans un bain aqueux contenant 0,05 à 5 % en poids, par rapport au poids de sel, d'au moins un composé de la formule générale (I) ou leurs sels métalliques alcalins ou alcalinoterreux correspondants ou des sels d'ammonium ou de phosphonium, les variables ayant la définition suivante: R1 est sélectionné parmi l'hydrogène ou alkyle C1-C12, non substitué ou substitué par au moins un groupe S-H ou un groupe O-H; X1 à X4, identiques ou différents, sont sélectionnés parmi l'oxygène, alkyle C1-C4, O-H, S-H ou N-HR2, R2 représente hydrogène ou alkyle C1-C12 ou un groupe alkyle C1-C4-C=O, au moins un X1 à X4 représentant S-H. Si R1 ne contient ni O-H ni S-H, au moins un autre X1 à X4 est sélectionné parmi S-H, OH ou NH-R2. Ce bain contient également au moins un composé qui catalyse l'hydrolyse de liaisons peptidiques.
EP03757967A 2002-10-21 2003-10-14 Procede permettant d'eliminer les substances de corne de la peau des animaux Withdrawn EP1556522A1 (fr)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
DE10249077 2002-10-21
DE10249077A DE10249077A1 (de) 2002-10-21 2002-10-21 Verfahren zur Herstellung von Leder
DE10319240 2003-04-28
DE2003119240 DE10319240A1 (de) 2003-04-28 2003-04-28 Verfahren zur Entfernung von Hornsubstanzen aus Tierhäuten
PCT/EP2003/011326 WO2004038046A1 (fr) 2002-10-21 2003-10-14 Procede permettant d'eliminer les substances de corne de la peau des animaux

Publications (1)

Publication Number Publication Date
EP1556522A1 true EP1556522A1 (fr) 2005-07-27

Family

ID=32178268

Family Applications (1)

Application Number Title Priority Date Filing Date
EP03757967A Withdrawn EP1556522A1 (fr) 2002-10-21 2003-10-14 Procede permettant d'eliminer les substances de corne de la peau des animaux

Country Status (5)

Country Link
US (2) US7250062B2 (fr)
EP (1) EP1556522A1 (fr)
AR (1) AR041659A1 (fr)
AU (1) AU2003273997A1 (fr)
WO (1) WO2004038046A1 (fr)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
AR039980A1 (es) 2002-05-22 2005-03-09 Basf Ag Procedimiento para eliminar sustancias corneas de pieles o pellejos
US7250062B2 (en) 2002-10-21 2007-07-31 Basf Aktienegesellschaft Method for removing horn substances from animal skin
IT1404926B1 (it) * 2010-06-14 2013-12-09 Cogolo Metodo per il trattamento delle pelli
CN102898240B (zh) * 2012-10-29 2014-03-05 罗星 利用铬革固体废弃物制备氨基酸螯合肥的方法
US10344914B2 (en) 2015-12-16 2019-07-09 William Cardozo Adjustable mount for a mountable device
RU2643713C2 (ru) * 2016-05-23 2018-02-05 Федеральное государственное бюджетное учреждение высшего профессионального образования "Астраханский государственный технический университет" Способ обработки кожевенного сырья

Family Cites Families (15)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1973130A (en) * 1933-07-21 1934-09-11 Rohm & Haas Process of unhairing hides or skins
AT187223B (de) 1954-06-24 1956-10-25 Chemie Linz Ag Verfahren zum Vorbereiten von tierischen Häuten für die Gerbung
DE2131630A1 (de) 1970-06-29 1972-01-05 Avon Prod Inc Mittel zur Entfernung von Hornsubstanzen,insbesondere Haaren
US3865546A (en) * 1970-10-22 1975-02-11 Collaborative Res Inc Depilatory composition and method of use
DE2917376A1 (de) * 1979-04-28 1980-11-13 Roehm Gmbh Enzymatisches verfahren zur haargewinnung und zum gleichzeitigen hautaufschluss
DE2929844A1 (de) * 1979-07-23 1981-02-26 Roehm Gmbh Weichverfahren
EP0096521A3 (fr) 1982-06-01 1985-01-23 THE PROCTER & GAMBLE COMPANY Compositions dépilatoires
EP0095916A3 (fr) 1982-06-01 1984-08-08 THE PROCTER & GAMBLE COMPANY Compositions dépilatoires
DE3224881A1 (de) * 1982-07-03 1984-03-01 Röhm GmbH, 6100 Darmstadt Verfahren zur herstellung von enthaartem, lagerfaehigem hautmaterial
US4472569A (en) * 1983-06-13 1984-09-18 Phillips Petroleum Company Mercaptohydroxy alkanes
GB9425876D0 (en) 1994-12-21 1995-02-22 Procter & Gamble Perfumed bleaching compositions
US5834299A (en) * 1994-12-21 1998-11-10 Novo Nordisk A/S Method for dehairing of hides or skins by means of enzymes
AR039980A1 (es) * 2002-05-22 2005-03-09 Basf Ag Procedimiento para eliminar sustancias corneas de pieles o pellejos
US7198647B2 (en) * 2002-07-15 2007-04-03 Council Of Scientific And Industrial Research Process for lime and sulfide free unhairing of skins or hides using animal and/or plant enzymes
US7250062B2 (en) 2002-10-21 2007-07-31 Basf Aktienegesellschaft Method for removing horn substances from animal skin

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO2004038046A1 *

Also Published As

Publication number Publication date
AR041659A1 (es) 2005-05-26
US20070143930A1 (en) 2007-06-28
US20060037148A1 (en) 2006-02-23
US7250062B2 (en) 2007-07-31
WO2004038046A1 (fr) 2004-05-06
AU2003273997A1 (en) 2004-05-13

Similar Documents

Publication Publication Date Title
DD210078A5 (de) Verfahren zum umweltfreundlichen aeschern von rohhaeuten
DE2404789C3 (de) Verfahren zur Herstellung gerbfertiger Blößen aus tierischen Häuten und Fellen
DE2917376A1 (de) Enzymatisches verfahren zur haargewinnung und zum gleichzeitigen hautaufschluss
DE3429047C2 (fr)
DE3224881A1 (de) Verfahren zur herstellung von enthaartem, lagerfaehigem hautmaterial
US20070143930A1 (en) Method for removing horn substances from animal skin
DE10249077A1 (de) Verfahren zur Herstellung von Leder
EP1511865B1 (fr) Procédé pour enlever des matières cornes de peaux ou de fourrures
DE2263133C3 (de) Verfahren zur enzymatischen Enthaarung von Tierhäuten
DE1230169B (de) Verfahren zur Herstellung gerbfertiger Bloessen
DE10319240A1 (de) Verfahren zur Entfernung von Hornsubstanzen aus Tierhäuten
EP0216271B1 (fr) Utilisation de dérivés de l'acide phosphonique comme adjuvants dans la fabrication du cuir
WO2005049870A1 (fr) Procede pour enlever de la corne sur des peaux d'animaux morts
DE767061C (de) Verfahren zum Beizen von geaescherten Hautbloessen
DE2307603C3 (fr)
DE2301591C3 (de) Verfahren zur Herstellung gerbfertiger Blößen aus tierischen Häuten und Fellen
DE10106541B4 (de) Enzympräparat und dessen Verwendung in der Gerberei
DE1288728B (de) Verfahren zur Herstellung gerbfertiger Bloessen
DE1203416B (de) Verfahren zur Herstellung tierischer Bloessen
DD254595A1 (de) Verfahren zur herstellung weicher, weisser leder
EP0464531B1 (fr) Compositions enzymatiques de mordançage
AT73691B (de) Verfahren, um Blößen und Rohfelle zum Abstoßen des Narbens vorzubereiten.
DE4332785A1 (de) Verbessertes enzymunterstütztes Äscherverfahren
AT132392B (de) Verfahren zur Herstellung gerbfertiger Blößen aus tierischen Häuten und Fellen.
EP0025933A1 (fr) Mélange adjuvant et procédé de trempage des peaux et des fourrures

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: 20050523

AK Designated contracting states

Kind code of ref document: A1

Designated state(s): AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HU IE IT LI LU MC NL PT RO SE SI SK TR

AX Request for extension of the european patent

Extension state: AL LT LV MK

DAX Request for extension of the european patent (deleted)
RAP1 Party data changed (applicant data changed or rights of an application transferred)

Owner name: BASF SE

17Q First examination report despatched

Effective date: 20110408

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

Free format text: STATUS: THE APPLICATION IS DEEMED TO BE WITHDRAWN

18D Application deemed to be withdrawn

Effective date: 20110819