EP0464531B1 - Compositions enzymatiques de mordançage - Google Patents

Compositions enzymatiques de mordançage Download PDF

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Publication number
EP0464531B1
EP0464531B1 EP91110302A EP91110302A EP0464531B1 EP 0464531 B1 EP0464531 B1 EP 0464531B1 EP 91110302 A EP91110302 A EP 91110302A EP 91110302 A EP91110302 A EP 91110302A EP 0464531 B1 EP0464531 B1 EP 0464531B1
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EP
European Patent Office
Prior art keywords
proteases
activity
protease
preparations
optimum
Prior art date
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Expired - Lifetime
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EP91110302A
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German (de)
English (en)
Other versions
EP0464531A2 (fr
EP0464531A3 (en
Inventor
Jürgen Dr. Christner
Ernst Pfleiderer
Tilman Dr. Taeger
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.)
Roehm GmbH Darmstadt
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Roehm GmbH Darmstadt
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Publication date
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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
    • C14C1/08—Deliming; Bating; Pickling; Degreasing

Definitions

  • the invention relates to new enzymatic pickling preparations for CO2 decalcification.
  • Conventional leather technology consists of a sequence of individual steps, the first section of which represents the so-called water workshop, followed by the actual tanning and finishing of the leather (cf. F. Stather, tanning chemistry and tanning technology, Akademie-Verlag, Berlin 1967).
  • the hides and skins are usually subjected to a liming process, which is usually followed by so-called descaling and pickling.
  • the liming is usually a treatment in the alkaline range (pH 12-14), carried out either as a purely alkaline "hydroxyl ash” using calcium hydroxide and sodium hydroxide or in the majority of cases as a reducing "sulphide ash".
  • Sulfide ash usually contain inorganic sulfide in the form of S2 ⁇ or SH ⁇ ion.
  • the present object can be achieved by using an enzymatic pickling preparation for carrying out the pickling which has a balanced activity spectrum in the entire pH range of the CO2 decalcification with simultaneous optimum activity at pH 6-8, especially at pH 6.5-7. 5.
  • proteolytically active enzymes can take place from different points of view, for example according to the origin (plant / animal / microbiological), according to the point of attack (exo-versus-endo-enzymes), using the "Active Site "of the proteases (" serine proteases ”) and according to the pH optimum of the proteolytic activity.
  • the alkaline bacterial proteases to be used according to the invention [EC3.4.21.14; see. L. Keay in Process Biochemistry 17-21 (1971) also mostly belongs to the serine type. They are preferably the so-called subtilisins, which are derived from various Bacillus sp. are produced, in particular by B.subtilis, B.licheniformis, B.pumilis, B.alkalophilus, B.firmus, B.megaterium, B.cereus, B.amylosacchariticus.
  • the alkaline proteases, the structure of which has been partially analyzed generally have molar masses in the range from 26,000 to 34,000.
  • subtilisins are predominantly quite stable in the pH range from 5 to 10, as long as work is carried out in the temperature range below 35 ° C. At temperatures of around 65 degrees C and above, however, activity is quickly lost.
  • the subtilisins are more active against casein than against hemoglobin or bovine serum albumin.
  • Technical preparations often show activities between 1 and 6 ANSON units per g (while the activity of crystalline subtilisin is between 25 and 30 ANSON units / g).
  • pancreatic proteases as they are used industrially, are mixtures of trypsin, chymotrypsin and various peptidases. They can contain amylase and lipase as accompanying enzymes. They are usually obtained by salt precipitation from fresh pancreatic press juice or from residues from insulin production. Compared to the substrates casein, hemoglobin and gelatin, the optimal pH value of the effect is 9.0 (30 - 40 degrees C), whereby it should be noted that the proteases are inactivated in the optimal range with increasing temperature.
  • the proteolytic activity of enzymes is customarily determined using the Anson-Hemoglobin method (ML Anson J. Gen. Physiol. 22, 79 (1939) or the Löhlein-Volhard method (Löhlein-Volhard's method for determining the proteolytic method Activity. Area. Paperback, Dresden-Leipzig, 1955) determined as "LVE” (Löhlein-Volhard unit).
  • Löhlein-Volhard unit is the amount of enzyme that digests 1.725 mg casein under the specific conditions of the method.
  • units which are derived from the Anson method are used for the activity determination of the enzymes active in the acidic range. These are referred to as "proteinase units (hemoglobin)" U Hb .
  • the enzymatic pickling preparations to be used according to the invention can be in the form of solid mixtures or preferably as preparations in a liquid medium (DE-A 39 04 465; unpublished German patent application P 39 27 286.9).
  • the pickling preparations advantageously also contain known additives such as stabilizers, adjusting agents and the like.
  • Calcium salts for example, are suitable as stabilizers.
  • Alkali chlorides, sulfates or bicarbonates are recommended as adjusting agents.
  • Ammonium salts such as ammonium sulfate or chloride can be used in small amounts ( ⁇ 0.5% by weight, based on the skin material) to accelerate the decalcification.
  • the proportion of salts in the pickling agents is generally ⁇ 90% by weight, based on the agents as a whole.
  • the mordant especially in liquid form, can also contain emulsifiers and solvents, for example of the type described in DE-A 33 12 840 or DE-A 33 22 840.
  • the proportion of emulsifiers is in the range from 0.01 up to 5% by weight, preferably 0.1 to 0.5% by weight, based on the weight of the skin.
  • nonionic emulsifiers if appropriate in combination with anionic emulsifiers, is particularly preferred.
  • Suitable solvents which are generally used in amounts of 0.1 to 5% by weight, based on the weight of the decalcifying liquor, are conventional, for example from the group of mineral oils or mineral oil fractions, the lower alcohols and glycols and their etherified derivatives in question. For example, mineral oils with between 10 and 60, in particular 15 and 30,% by weight of aromatics may be mentioned.
  • the implementation of the invention can closely follow the known procedures for CO2 decalcification. It is preferable to work in the tanning drum or in the tanning machine, a recirculation or pumping device for the fleet being advantageous.
  • the liquors used are generally in the range up to 150% based on the weight of the skin.
  • CO2 gas is fed directly into the pumping system.
  • the dosage is advantageously 7-11 l / min.
  • the pickling agent for example product A according to the exemplary embodiments, is metered in right at the start.
  • the pH of the liquor then drops from close to 12 to a value around 8 in the first period, after about 20 minutes, after one a further period of about 10 minutes to a value of approx. 6.5 - 7.
  • the pelts with a thickness of 1.8 - 2.5 mm are completely decalcified after a descaling period of approx. 120 minutes.
  • the skins are to be rated better than when using a purely pancreatic mordant with the same activity (with optimum activity at pH 8) if the procedure is otherwise identical.
  • the process according to the invention does not require a fundamental change in the CO2 decalcification and pickling process.
  • Enzyme preparations consisting of:
  • pancreatic enzyme suspension 100 kg of squeezed juice obtained after grinding, activating and extracting pancreatic glands is mixed with 50 kg of ammonium sulfate and the pancreatic enzymes are precipitated.
  • the pancreatic enzyme suspension has an activity of 8 400 U HB at pH 8 and a density of approx. 1.22 to 1.23 g / cm3. This suspension is then treated with as much thickened isotonic ammonium sulfate solution (480 mPa s) diluted to achieve an activity of 250 U HB at pH 8.
  • 1,000 kg of ashed beef skin with 800 kg of water are placed in a tanning drum with a recirculation or pumping unit for the fleet.
  • CO2 gas is fed directly into the pumping system.
  • the dosage of CO2 is 8 to 9 l / min.
  • 0.5% (based on the pelt weight) of the mordant (product A) is added.
  • the initial pH in the liquor drops from pH 11.8 to pH 8.2-8 during the first 10 minutes and to pH 6.5 -7 after a further 10 minutes.
  • the bare cross-sections are completely descaled.
  • the skins are to be rated better in terms of basic purity, smoothness and skin disruption than in identical applications of a pure pancreatic stain with the same activity and optimum activity at pH 8.
  • Product B was used with the same dosage and application. Since product B is liquid, it can be added automatically via a dosing device. In this case an additional opening of the tanning drum is not necessary. This avoids exposure to toxic hydrogen sulfide, which is released to a greater extent during CO2 decalcification.
  • product C is used in the same application and dosage.
  • Product C contains emulsifiers which further improve the basic purity of the skins.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Medicines Containing Material From Animals Or Micro-Organisms (AREA)
  • Treatment And Processing Of Natural Fur Or Leather (AREA)
  • Medicinal Preparation (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Claims (4)

  1. Compositions de traitement enzymatique pour le déchaulage au dioxyde de carbone par utilisation de protéases, caractérisées en ce que les compositions de traitement contiennent, en tant que protéases P
    A) des protéases alcalines de bactéries ayant un pH optimal compris entre 9 et 11, dans des proportions de 10 à 20% en poids par rapport à la totalité des protéases P
    B) des protéases de pancréas ayant un pH optimal compris entre 7 et 9, dans des proportions de 40 à 70% en poids par rapport à la totalité des protéases P et
    C) des protéases de champignons ou des protéases de bactéries ayant un pH optimal compris dans le domaine de pH de 5 à 7, en proportions de 20 à 40% en poids par rapport à la totalité des protéases P,
    à condition que l'activité protéolytique
    A') des protéases alcalines de bactéries à pH 10,
    B') des enzymes pancréatiques à pH 8 et
    C') des protéases acides de champignons ou de bactéries à pH 6,5
    soit ajustée à un niveau identique.
  2. Compositions de traitement enzymatique selon la revendication 1, caractérisées en ce qu'elles contiennent encore, en dehors des protéases, des agents auxiliaires connus en soi, choisis dans le groupe des stabilisants d'enzymes, des agents de fixation.
  3. Compositions de traitement enzymatique selon la revendication 1 ou 2, caractérisées en ce qu'elles contiennent des solvants connus en soi.
  4. Compositions liquides ou solides de traitement enzymatique selon l'une quelconque des revendications 1 à 3, caractérisées en ce qu'elles sont déjà introduites au début du déchaulage par CO₂ ou pendant celui-ci.
EP91110302A 1990-06-23 1991-06-22 Compositions enzymatiques de mordançage Expired - Lifetime EP0464531B1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE4020110 1990-06-23
DE4020110A DE4020110A1 (de) 1990-06-23 1990-06-23 Neue enzymatische beizpraeparate

Publications (3)

Publication Number Publication Date
EP0464531A2 EP0464531A2 (fr) 1992-01-08
EP0464531A3 EP0464531A3 (en) 1992-09-09
EP0464531B1 true EP0464531B1 (fr) 1994-09-28

Family

ID=6408983

Family Applications (1)

Application Number Title Priority Date Filing Date
EP91110302A Expired - Lifetime EP0464531B1 (fr) 1990-06-23 1991-06-22 Compositions enzymatiques de mordançage

Country Status (5)

Country Link
EP (1) EP0464531B1 (fr)
AT (1) ATE112323T1 (fr)
DE (2) DE4020110A1 (fr)
DK (1) DK0464531T3 (fr)
ES (1) ES2062621T3 (fr)

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US2147542A (en) * 1937-01-27 1939-02-14 Ruby Kid Co Treating skins, hides, and pelts
DE974813C (de) * 1954-12-24 1961-05-04 Roehm & Haas G M B H Verfahren zum Beizen tierischer Hautbloessen

Also Published As

Publication number Publication date
ES2062621T3 (es) 1994-12-16
DE59103082D1 (de) 1994-11-03
DE4020110A1 (de) 1992-01-02
DK0464531T3 (da) 1994-11-14
EP0464531A2 (fr) 1992-01-08
EP0464531A3 (en) 1992-09-09
ATE112323T1 (de) 1994-10-15

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