CA1122550A - Process for the treatment of collagen-containing materials - Google Patents
Process for the treatment of collagen-containing materialsInfo
- Publication number
- CA1122550A CA1122550A CA324,147A CA324147A CA1122550A CA 1122550 A CA1122550 A CA 1122550A CA 324147 A CA324147 A CA 324147A CA 1122550 A CA1122550 A CA 1122550A
- Authority
- CA
- Canada
- Prior art keywords
- collagen
- containing material
- treatment
- protease
- urea
- 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
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
- C09H—PREPARATION OF GLUE OR GELATINE
- C09H1/00—Pretreatment of collagen-containing raw materials for the manufacture of glue
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08H—DERIVATIVES OF NATURAL MACROMOLECULAR COMPOUNDS
- C08H1/00—Macromolecular products derived from proteins
- C08H1/06—Macromolecular products derived from proteins derived from horn, hoofs, hair, skin or leather
Abstract
ABSTRACT OF THE DISCLOSURE
A process for the treatment of collagen-containing materinl which comprises treating a collagen-containing ma-terial with a neutral and/or alkaline protease in a treatment medium having 8 pH of from 6.5 to 13 and containing urea and/or guanidine and/or a salt of urea or guanidine, whereby the solubility in hot water of the collagen contained in the said material is increased. The resulting product can then be processed to produce gelatine and similar collagen-containing products. The collagen-containing starting material employed in the above process can be for example bones, skins and hides.
A process for the treatment of collagen-containing materinl which comprises treating a collagen-containing ma-terial with a neutral and/or alkaline protease in a treatment medium having 8 pH of from 6.5 to 13 and containing urea and/or guanidine and/or a salt of urea or guanidine, whereby the solubility in hot water of the collagen contained in the said material is increased. The resulting product can then be processed to produce gelatine and similar collagen-containing products. The collagen-containing starting material employed in the above process can be for example bones, skins and hides.
Description
~12ZS5~
The present invention relates to a new process ~or the treatment of collagen-containing materials.
Collagen-containing raw materials are used in industry for the manufacture of various products wherein the collagen is not decomposed substantially below a molecular weight of 1 x 104. Examples of such products include gelatine, glue, collagen ~hreads and collagen films ~see G. Reich in the monograph "Collagen", pages 256 to 2~2 J Verlag Steinkopff~ Dresden, 1966).
Methods of obtaining such products froD~ collagen may be illustrated by reference to the manufacture of gelatine.
The starting material for the manufacture of gelatine is, as is known, collagen which is a fibrous protein contained in bones and in the connective tissue of animals and forming the reticular tissue of the corium, numeTous internal membranes, tendons, cartilages and fish scales.
The structure of collagen is largely known.
~elatine is manufactured industTially predominantly fTom bones and skin (bone and skin gelatine).
The raw materials for the manufacture of gelatine are mainly waste products and by-products of tanneries, the leather-processing industry slaughterhouses and butcher's shops. Skin gelatine is manufactured from, for e~ample, calf and ox heads, flank and leg sectinns which may be fresh, limed or salted, split leather ~in the limed, dried or salted state) for making glue, and the skins of slaughtered piglets etc. Bone gelatine is manufactured from for example crushed bones, skin bone, waste from leg material, various head bones, shoulder blades~ etc.
.- ~
:. :
. :
- - llZZSSO
The structure of the collagen is par-tly retained upon conversion into the desired Einal produc-ts such as gelatine, glue, collagen threads and collagen films!
and industrial processes for obtaining these said products need to take this requirement into accound.
From the point of view of the decomposition or pretreatment of the raw material, there are two types of gelatine: alkaline-limed gelàtines, and acid-limed gelatines.
The acid-limed gelatines which are manufactured mainly from the skins of piglets are not concerned in the present invention Treatment with alkali (liming)causes a chemical transformation o the collagen ("ripening'l~, so that it subsequently dissolves upon boiling in hot water.
Gelatine manufacture thus comprises a series of working steps. Whèn bones are used as raw materials, cleaning, defatting and crushing steps are initially carried out.
Tricalcium phosphate in the bony tissue is then dissolv~d out by treatment or 8 to 14 days with dilute acid ("maceration"~,-the bone material is then washed and is subsequently limed with a 5% to 15% calcium hydroYide solution for approximately 3 to 16 weeks. After liming is completed the bones are freed from adherent lime in mechanica`l washing machines and are neutralised. This . . .
.;: : , : : :
' ~ss~
washing and cleaning of the raw material obtained from the liming operation requires large quantities of water.
The gelatine is then extracted with water from the neutrally washed bone collagen as a colloidal solution at temperatures between 40C and 90~C in several "offtakes".
~ hen skin is used as raw material, the procedure is analogous to that fox bones. Untreated skin material is firstly freed from preserving salts by the addition of milk of lime (to initiate the swelling process). It is then treated for approximately 3 weeks with milk of lime of 6 to 7 ~e to effect complete loosening of the hair.
The hairs are subsequently removed and the skin material is crushad and again limed fox approximately 12 to 15 weeks with milk of lime. The skin collagen is then further processed, as described for bone gelatine.
The extraction of gelatine from split skins follows the procedure for untreated skin material The skins are crushed and subsequently limed for approximately 8 to 14 weeks. Furthex treatment is effected as for bone gelatine.
The colla~en content of the treated raw material is generally known.
It is clear that the degree of decomposition of the collagen and, consequently, the quality of the decomposition product depends on the decomposition process and the thermal 25 ` hydrolysis~ In aqueous solution, for example, the gelatine ; molecules are present with relative molecular weights of approximately 4000 to approximately 4 x 106. In practice, molecular weights of approximately ll,Q00 to 100/000 are expected for gelatine.
The various measures, especially liming of the ~ ~!
collagen-containing material, require disproportionately long times and there;have been numerous attempts to shorten the liming process and, if possible, to impro~e the quality of products such as gelatinec US-PS 2,741,575 and 1,741,576 teach the use of micro-organisms such as Saccharomyces, Mycoderma or Torulopis for treating raw materials for use in the manufacture of glue ~from skins~ and gelatine.
USSR-PA 151,745 proposed the use of an enzyme extract of Asper~illus ~lavus and also pancreatine to acce-lerate the liming of leather waste. Japanese patent speci-fication 7006274 recommends the treatment of collagen-con~ain-ing material with acid proteases at an acid pH value for the manufacture of gelatine. The treatment of calfskin at pH 2.9 with proctase from A. ni~er var. macrosporus for 48 hours is given as an example.
According to Bull. Soc. Sci., PhotogrO Jap. No. 16, 30 (1966), a urther possibility for manufacturing gelatine involves the conversion of collagen fibres into soluble monomeric collagen molecules by means of proteolytic enz~mes, An enzyme is recommended which has a wide specificity, for example, pronase in ~e presence of calcium chl~ride. Accor-ding to German Offenlegungsschrift 2,629,594, a solution o a neutral or alkaline proteolytic en~yme at a pH value be~ween 7 and 13 for a period of 4 to 72 hours at 20C to 400C is advantageously used for the "alkaline or neutral conditioning"
of collagen in the extraction of gelatine. Trypsine, Baclllus proteases and the alkalases as described in British patent 1,234,784, are specifically mentioned.
We have now surprisingly found that the treatment .
~Z55~
time for decomposition of collagen, e.g. as present in bone material after maceration and in the raw materials based on skin tissue or connective tissue, optionally after removal of preserving salt, hairs, etc., can be reduced by the presence in the treatment medium of urea and/or guanidine and/or an acid addition`salt thereof.
According to the present invention there is provided a process for the treatment of collagen-containing material which comprises treating a collagen-containing material with a neutral and/or alkaline protease in a treatment medium having a pH of from 6.5 to 13 and containing urea and/or guanidine and/or a salt, e.g. derived from a strong mineral acid such as hydrochloric or sulphuric acid of urea or guanidine, whereby the solubility of the collagen contained in the said material is increased such that the collagen can be extracted with hot water.
Collagen-containing materials for use in the treat-ment process according to the invention include the a~oresaid materials based on bones, skins and hides, especially bone material, fresh limed or salted skins and split hides which are limed dried or salted.
The neutral and alkaline proteases which may be employed in the process according to the invention may be obtained fLom micro-organisms or from higher organisms, e.g. neutral and/or alkaline proteases of bacterial origin, for example the proteases isolated from Bacillus strains.
Examples of such protease~s include neutral and/or alkaline proteases from B. licheniformis, B. firmus, B. pumilis, ~lZ~550 B. cereus, B. mycoides, B. alcal'o-phi`lus, B. subtilis and B. parasiticus, as well as the neutral bacterial protease from Streptomyces griseus. Neutral and/or alkaline fungal proteases may also be employed, for example -those from Aspergillus species (such as ~ arasiticus, A oryzae, A. sojae or A. flavus) PaeciIomyces varioti, Rhizopus chinensis and Mucor pu_illus, as well as vegetable proteases such as papain, bromelain and ficin. The pancreatic proteases can also be employed as well as combination of any of the above enzymes. The designation "neutral" or "alkaline" proteases relates to the relative pH range (Ullmann's Encyclopaedia of Industrial Chemistry, edited by E. Bartholome et al., volume 10, pages 517 to 522, Verlag Chemie Weinheim, 1975). By neutral proteases are meant those active in a pH range between 5.5. and 7.5 and by alkaline proteases are meant those active in a pH range between 7 and 12.
In the process of the present invention, it is desirable to adjust the pH value to a value approximating to that for the opeimum activity of the enzyme or enzymes used. The temperature must also, if required, be adjusted according to the temperature at which the selected enzymes display satisfactory activity. In general, temperatures of 18C to 4QC ar~ preerred. Concentrations of from 1 to 10, especially 2 to 5, Lohlein-Volhard units (L.V.E., as defined hereinafter~ per gram of collagen contained in the ra~ material are the preferred concentrat-ions for the enzymes used in the process according to the , ..
~;
, ~ ~
25Sg~
invention.
The enzymes may be employed in conventional manner having regard to the known optimal temperatures r stability conditions etc for the enzymes providing that such - 5 parameters are suitable for use on an industrial scale.
It is extremely surprising that in the process according to the invention, the necessary transformation of the col~agen in the starting materials can be carried out satisfactorilyon an industrial scale by the use of neutral or alkaline proteases with the addition of urea, guanidine or an acid addition salt thereof. The urea, guanidine or acid addition salt is preferably added to the enzymatic mixture in an amount of from 0.004 g to 0.04 g, preferably 0.01 g to 0.03 g, per g of collagen in the dry collagen-containing raw material.
- Otherwise the process can be carried out using conventional techniques in the art.
The process of the present invention enables the ripeni~ times to be reduced to approximately 4 to 24 hours.
This reduction is an important one.
The enzymatic decomposition process to obtain gelatin according to the present invention may be discontinued when a condition of "ripeness" is reached.
For deinition of "ripeness" see G. Reich, loc. cit., p.
244; see also Example 1. The enzyme or enzymes are subsequently appropriately inactivated, for example, by acidification of the material.
Further treatment to product gelatine, glue, 112Z55~
- 7a -collagen threads and collagen fibre may be effected in conventional manner.
In the process accordiny to the present invention, conventional additives such as activators, stabilisers and 5 the like, may be used ln the enzymatic reaction. The proteolytic activity of enzymes is determined conventionally by the Anson haeoglobin method (M.L. Anson, J. Gen.
Physiol., 22, 79 (1939)) or by the Lohlein-Volhard method to determine proteolytic activity (Gerbereichem. Teschenbuch, 10 Dresden-Leipzig 1955) as "LVE" (Lohlein-Volhard unit~.
By one Lohlein-Volhard unit is meant that quantity of enzyme in grams which digests 1.725 mg of casèin under the speciic conditions of the method.
As indicated earlier, the collagen product obtained 15 by the treatment of the collagen containing material according to the process of the invention may be further processed, in particular to produce shaped articles, eg in the form of films, or may be spun to produce a thread.
1~a22550 The following Examples illustrate the process according to the invention.
Example 1 Starting material ~or treatment is bull hide softened with water and limed with lime and sodium sulphide 1 kg of bull hide is mixed with 1.5 litres of water at 400C. The temperature is kept at 40OC in a water bath and treated without stirring with 1 g of alkaline bacterial proteinase from Bacillus licheniformis 9000 LVE~
- 4 g of urea 20 g of calcium hydroxide for 4 hours at pH 10Ø After this time, "readiness for boiling"
is reached, that is, the bull hide can be torn with the finger and the fibres isolated by rubbing between the fingers. The weight of the hide is reduced to 635 g. The hide material is thereafter first washed several times with deionised water. To inhibit the enzyme activity, it is brought into solution with 200 % desalted ~ater at 20C, 4 g of sulphuric acid(48% by weight) and stirred frequently. The pH value of the solution is 3Ø After 3 hours the liquor is discarded. It is washed several times thereafter with deionised water until a neutral 25 pH value is reachedO It is subsequently melted out with 150% deionised water for 4 hours at 70C. 150 g of material not capable o being melted out are obtained. Conversion of the starting material is 85%. The mixture is thereafter filtered. For deodorisation purposes, 0~5 g of activated 30 charcoal are added to the filtrate. After centrifuging~
filtering is effected again. The product is thereafter evaporated in a vacuum evaporator at 30OC. The foregoing B and following percentages relate to ~eight in relation to .
:
-: . ;
:, ~l~Z550 the (water-corltaining) raw hide material used unless otherwise stated.
~ .
1000 g of freshly limed split ox hide are weighed in a 2-litre beaker and mixed with loS litres of water at 400C~ The preparation has added to it
The present invention relates to a new process ~or the treatment of collagen-containing materials.
Collagen-containing raw materials are used in industry for the manufacture of various products wherein the collagen is not decomposed substantially below a molecular weight of 1 x 104. Examples of such products include gelatine, glue, collagen ~hreads and collagen films ~see G. Reich in the monograph "Collagen", pages 256 to 2~2 J Verlag Steinkopff~ Dresden, 1966).
Methods of obtaining such products froD~ collagen may be illustrated by reference to the manufacture of gelatine.
The starting material for the manufacture of gelatine is, as is known, collagen which is a fibrous protein contained in bones and in the connective tissue of animals and forming the reticular tissue of the corium, numeTous internal membranes, tendons, cartilages and fish scales.
The structure of collagen is largely known.
~elatine is manufactured industTially predominantly fTom bones and skin (bone and skin gelatine).
The raw materials for the manufacture of gelatine are mainly waste products and by-products of tanneries, the leather-processing industry slaughterhouses and butcher's shops. Skin gelatine is manufactured from, for e~ample, calf and ox heads, flank and leg sectinns which may be fresh, limed or salted, split leather ~in the limed, dried or salted state) for making glue, and the skins of slaughtered piglets etc. Bone gelatine is manufactured from for example crushed bones, skin bone, waste from leg material, various head bones, shoulder blades~ etc.
.- ~
:. :
. :
- - llZZSSO
The structure of the collagen is par-tly retained upon conversion into the desired Einal produc-ts such as gelatine, glue, collagen threads and collagen films!
and industrial processes for obtaining these said products need to take this requirement into accound.
From the point of view of the decomposition or pretreatment of the raw material, there are two types of gelatine: alkaline-limed gelàtines, and acid-limed gelatines.
The acid-limed gelatines which are manufactured mainly from the skins of piglets are not concerned in the present invention Treatment with alkali (liming)causes a chemical transformation o the collagen ("ripening'l~, so that it subsequently dissolves upon boiling in hot water.
Gelatine manufacture thus comprises a series of working steps. Whèn bones are used as raw materials, cleaning, defatting and crushing steps are initially carried out.
Tricalcium phosphate in the bony tissue is then dissolv~d out by treatment or 8 to 14 days with dilute acid ("maceration"~,-the bone material is then washed and is subsequently limed with a 5% to 15% calcium hydroYide solution for approximately 3 to 16 weeks. After liming is completed the bones are freed from adherent lime in mechanica`l washing machines and are neutralised. This . . .
.;: : , : : :
' ~ss~
washing and cleaning of the raw material obtained from the liming operation requires large quantities of water.
The gelatine is then extracted with water from the neutrally washed bone collagen as a colloidal solution at temperatures between 40C and 90~C in several "offtakes".
~ hen skin is used as raw material, the procedure is analogous to that fox bones. Untreated skin material is firstly freed from preserving salts by the addition of milk of lime (to initiate the swelling process). It is then treated for approximately 3 weeks with milk of lime of 6 to 7 ~e to effect complete loosening of the hair.
The hairs are subsequently removed and the skin material is crushad and again limed fox approximately 12 to 15 weeks with milk of lime. The skin collagen is then further processed, as described for bone gelatine.
The extraction of gelatine from split skins follows the procedure for untreated skin material The skins are crushed and subsequently limed for approximately 8 to 14 weeks. Furthex treatment is effected as for bone gelatine.
The colla~en content of the treated raw material is generally known.
It is clear that the degree of decomposition of the collagen and, consequently, the quality of the decomposition product depends on the decomposition process and the thermal 25 ` hydrolysis~ In aqueous solution, for example, the gelatine ; molecules are present with relative molecular weights of approximately 4000 to approximately 4 x 106. In practice, molecular weights of approximately ll,Q00 to 100/000 are expected for gelatine.
The various measures, especially liming of the ~ ~!
collagen-containing material, require disproportionately long times and there;have been numerous attempts to shorten the liming process and, if possible, to impro~e the quality of products such as gelatinec US-PS 2,741,575 and 1,741,576 teach the use of micro-organisms such as Saccharomyces, Mycoderma or Torulopis for treating raw materials for use in the manufacture of glue ~from skins~ and gelatine.
USSR-PA 151,745 proposed the use of an enzyme extract of Asper~illus ~lavus and also pancreatine to acce-lerate the liming of leather waste. Japanese patent speci-fication 7006274 recommends the treatment of collagen-con~ain-ing material with acid proteases at an acid pH value for the manufacture of gelatine. The treatment of calfskin at pH 2.9 with proctase from A. ni~er var. macrosporus for 48 hours is given as an example.
According to Bull. Soc. Sci., PhotogrO Jap. No. 16, 30 (1966), a urther possibility for manufacturing gelatine involves the conversion of collagen fibres into soluble monomeric collagen molecules by means of proteolytic enz~mes, An enzyme is recommended which has a wide specificity, for example, pronase in ~e presence of calcium chl~ride. Accor-ding to German Offenlegungsschrift 2,629,594, a solution o a neutral or alkaline proteolytic en~yme at a pH value be~ween 7 and 13 for a period of 4 to 72 hours at 20C to 400C is advantageously used for the "alkaline or neutral conditioning"
of collagen in the extraction of gelatine. Trypsine, Baclllus proteases and the alkalases as described in British patent 1,234,784, are specifically mentioned.
We have now surprisingly found that the treatment .
~Z55~
time for decomposition of collagen, e.g. as present in bone material after maceration and in the raw materials based on skin tissue or connective tissue, optionally after removal of preserving salt, hairs, etc., can be reduced by the presence in the treatment medium of urea and/or guanidine and/or an acid addition`salt thereof.
According to the present invention there is provided a process for the treatment of collagen-containing material which comprises treating a collagen-containing material with a neutral and/or alkaline protease in a treatment medium having a pH of from 6.5 to 13 and containing urea and/or guanidine and/or a salt, e.g. derived from a strong mineral acid such as hydrochloric or sulphuric acid of urea or guanidine, whereby the solubility of the collagen contained in the said material is increased such that the collagen can be extracted with hot water.
Collagen-containing materials for use in the treat-ment process according to the invention include the a~oresaid materials based on bones, skins and hides, especially bone material, fresh limed or salted skins and split hides which are limed dried or salted.
The neutral and alkaline proteases which may be employed in the process according to the invention may be obtained fLom micro-organisms or from higher organisms, e.g. neutral and/or alkaline proteases of bacterial origin, for example the proteases isolated from Bacillus strains.
Examples of such protease~s include neutral and/or alkaline proteases from B. licheniformis, B. firmus, B. pumilis, ~lZ~550 B. cereus, B. mycoides, B. alcal'o-phi`lus, B. subtilis and B. parasiticus, as well as the neutral bacterial protease from Streptomyces griseus. Neutral and/or alkaline fungal proteases may also be employed, for example -those from Aspergillus species (such as ~ arasiticus, A oryzae, A. sojae or A. flavus) PaeciIomyces varioti, Rhizopus chinensis and Mucor pu_illus, as well as vegetable proteases such as papain, bromelain and ficin. The pancreatic proteases can also be employed as well as combination of any of the above enzymes. The designation "neutral" or "alkaline" proteases relates to the relative pH range (Ullmann's Encyclopaedia of Industrial Chemistry, edited by E. Bartholome et al., volume 10, pages 517 to 522, Verlag Chemie Weinheim, 1975). By neutral proteases are meant those active in a pH range between 5.5. and 7.5 and by alkaline proteases are meant those active in a pH range between 7 and 12.
In the process of the present invention, it is desirable to adjust the pH value to a value approximating to that for the opeimum activity of the enzyme or enzymes used. The temperature must also, if required, be adjusted according to the temperature at which the selected enzymes display satisfactory activity. In general, temperatures of 18C to 4QC ar~ preerred. Concentrations of from 1 to 10, especially 2 to 5, Lohlein-Volhard units (L.V.E., as defined hereinafter~ per gram of collagen contained in the ra~ material are the preferred concentrat-ions for the enzymes used in the process according to the , ..
~;
, ~ ~
25Sg~
invention.
The enzymes may be employed in conventional manner having regard to the known optimal temperatures r stability conditions etc for the enzymes providing that such - 5 parameters are suitable for use on an industrial scale.
It is extremely surprising that in the process according to the invention, the necessary transformation of the col~agen in the starting materials can be carried out satisfactorilyon an industrial scale by the use of neutral or alkaline proteases with the addition of urea, guanidine or an acid addition salt thereof. The urea, guanidine or acid addition salt is preferably added to the enzymatic mixture in an amount of from 0.004 g to 0.04 g, preferably 0.01 g to 0.03 g, per g of collagen in the dry collagen-containing raw material.
- Otherwise the process can be carried out using conventional techniques in the art.
The process of the present invention enables the ripeni~ times to be reduced to approximately 4 to 24 hours.
This reduction is an important one.
The enzymatic decomposition process to obtain gelatin according to the present invention may be discontinued when a condition of "ripeness" is reached.
For deinition of "ripeness" see G. Reich, loc. cit., p.
244; see also Example 1. The enzyme or enzymes are subsequently appropriately inactivated, for example, by acidification of the material.
Further treatment to product gelatine, glue, 112Z55~
- 7a -collagen threads and collagen fibre may be effected in conventional manner.
In the process accordiny to the present invention, conventional additives such as activators, stabilisers and 5 the like, may be used ln the enzymatic reaction. The proteolytic activity of enzymes is determined conventionally by the Anson haeoglobin method (M.L. Anson, J. Gen.
Physiol., 22, 79 (1939)) or by the Lohlein-Volhard method to determine proteolytic activity (Gerbereichem. Teschenbuch, 10 Dresden-Leipzig 1955) as "LVE" (Lohlein-Volhard unit~.
By one Lohlein-Volhard unit is meant that quantity of enzyme in grams which digests 1.725 mg of casèin under the speciic conditions of the method.
As indicated earlier, the collagen product obtained 15 by the treatment of the collagen containing material according to the process of the invention may be further processed, in particular to produce shaped articles, eg in the form of films, or may be spun to produce a thread.
1~a22550 The following Examples illustrate the process according to the invention.
Example 1 Starting material ~or treatment is bull hide softened with water and limed with lime and sodium sulphide 1 kg of bull hide is mixed with 1.5 litres of water at 400C. The temperature is kept at 40OC in a water bath and treated without stirring with 1 g of alkaline bacterial proteinase from Bacillus licheniformis 9000 LVE~
- 4 g of urea 20 g of calcium hydroxide for 4 hours at pH 10Ø After this time, "readiness for boiling"
is reached, that is, the bull hide can be torn with the finger and the fibres isolated by rubbing between the fingers. The weight of the hide is reduced to 635 g. The hide material is thereafter first washed several times with deionised water. To inhibit the enzyme activity, it is brought into solution with 200 % desalted ~ater at 20C, 4 g of sulphuric acid(48% by weight) and stirred frequently. The pH value of the solution is 3Ø After 3 hours the liquor is discarded. It is washed several times thereafter with deionised water until a neutral 25 pH value is reachedO It is subsequently melted out with 150% deionised water for 4 hours at 70C. 150 g of material not capable o being melted out are obtained. Conversion of the starting material is 85%. The mixture is thereafter filtered. For deodorisation purposes, 0~5 g of activated 30 charcoal are added to the filtrate. After centrifuging~
filtering is effected again. The product is thereafter evaporated in a vacuum evaporator at 30OC. The foregoing B and following percentages relate to ~eight in relation to .
:
-: . ;
:, ~l~Z550 the (water-corltaining) raw hide material used unless otherwise stated.
~ .
1000 g of freshly limed split ox hide are weighed in a 2-litre beaker and mixed with loS litres of water at 400C~ The preparation has added to it
2 g of bacterial proteinase from Bacillus subtillis with 9000 LVE, 8 g of urea~
10 g of sodium hydroxide solution (33% by wei~ht) The pH value of the solution obtained is 11,5. To stabilise the temperature, it is treated in a water both for 8 hours at 40C. After this time the hide is ripe, and in this sta~e its weight is 300 g. Further treatment is effec~ed, as des-cribed in Example 1. No residue is obtained ater mel~ing-ou~. Total conversion of the starting material is effected.
Example 3 1000 g of limed split bull hide are weighed in a 2-litre beaker and mixed with 1,5 litres o~ water at 400C.
2Q Treatment is effected without stirring and in a thermostat at 40C to maintain a constant temperature. The treatment time is 10 hours. The preparation has added to it 1.5 g of bacterial proteinase from Bacillus firmus with 9000 LVE, 6.0 g of urea, 20.0 g of hydrate of lime.
The pH Yalue of the solution is 10.2. Melting-out, wa~hing and inhibition of enzyme act;vity are carried out analogously to Example 1 After melting-out, a residue of 50 g of material , - ., .
: - , ,, ' ~
Z~550 10 _ not capable of being melted out are obtained. 90% of the starting material is converted.
1000 g of limed split cowhide are weighed in a 2-litre beaker and mixed with 1.5 litres of water at 40C.
Treatment is effected without stirring. The solution has added to it:
1.5 g of fungal proteina~e from Asper~illus parasiticus with 9000 LVE, 6.0 g of gl~anidine hydrochloride, 20.0 g of hydrate of lime.
The pH value of the solution is 10.2. Washing, inhibition of enzyme activity and melting-out are carried out analo-gously to Example 1. After melting-out, a residue ~ 80 g of material not capable of being melted out is obtained.
80~/o of the starting material is convertedO
.
10 g of sodium hydroxide solution (33% by wei~ht) The pH value of the solution obtained is 11,5. To stabilise the temperature, it is treated in a water both for 8 hours at 40C. After this time the hide is ripe, and in this sta~e its weight is 300 g. Further treatment is effec~ed, as des-cribed in Example 1. No residue is obtained ater mel~ing-ou~. Total conversion of the starting material is effected.
Example 3 1000 g of limed split bull hide are weighed in a 2-litre beaker and mixed with 1,5 litres o~ water at 400C.
2Q Treatment is effected without stirring and in a thermostat at 40C to maintain a constant temperature. The treatment time is 10 hours. The preparation has added to it 1.5 g of bacterial proteinase from Bacillus firmus with 9000 LVE, 6.0 g of urea, 20.0 g of hydrate of lime.
The pH Yalue of the solution is 10.2. Melting-out, wa~hing and inhibition of enzyme act;vity are carried out analogously to Example 1 After melting-out, a residue of 50 g of material , - ., .
: - , ,, ' ~
Z~550 10 _ not capable of being melted out are obtained. 90% of the starting material is converted.
1000 g of limed split cowhide are weighed in a 2-litre beaker and mixed with 1.5 litres of water at 40C.
Treatment is effected without stirring. The solution has added to it:
1.5 g of fungal proteina~e from Asper~illus parasiticus with 9000 LVE, 6.0 g of gl~anidine hydrochloride, 20.0 g of hydrate of lime.
The pH value of the solution is 10.2. Washing, inhibition of enzyme activity and melting-out are carried out analo-gously to Example 1. After melting-out, a residue ~ 80 g of material not capable of being melted out is obtained.
80~/o of the starting material is convertedO
.
Claims (14)
PROPERTY OR PRIVILEGE IS CLAIMED ARE DEFINED AS FOLLOWS:
1. A process for the treatment of collagen-containg material which comprises treating a collagen-containing material with a neutral and/or alkaline protease in a treatment medium having a pH of from 6.5 to 13 and containing urea and/or guanidine and/or a salt of urea or guanidine, whereby the solubility in hot water of the collagen contained in the said material is increased.
2. A process as claimed in claim 1 wherein the collagen-containing material is derived from bone material; fresh, limed or salted skins; or fresh, limed or salted hides.
3. A process as claimed in claim 1 wherein the urea, guanidine and/or acid addition salt thereof is employed in a total amount of 0.004 to 0.04 g per g of collagen in the collagen-containing material.
4. A process as claimed in claim 1 wherein the urea, guanidine and/or acid addition salt thereof is employed in a total amount of 0.01 to 0.03 g per g of collagen in the collagen-containing material.
5. A process as claimed in any one of claims 1 to 3, wherein the said protease comprises an bacterical protease derived from Bacillus subtilis or Bacillus firmus; or a fungal protease derived from Aspergillus parasiticus.
6. A process as claimed in any one of claims 1 to 3, wherein the said protease is employed in a total amount of 1 to 10 Lohlein-Volhard units per gram of collagen in the collagen-containing material.
7. A process as claimed in any one of claims 1 to 3 wherein the said protease is employed in a total amount of 2 to 5 Lohlein-units per gram of collagen in the collagen-containing material.
8. A process as claimed in any one of claims l to 3 wherein treatment is effected for a period of 4 to 24 hours.
9. A process as claimed in any one of claims 1 to 3 wherein treatment is effected at a temperature of 18° to 40°C.
10. A process as claimed in any one of claims 1 to 3 wherein the said protease is subsequently deactivated after the protease treatment of the collagen-containing material.
11. A process as claimed in any one of claims 1 to 3 wherein the treated collagen-containing material is subsequently subjected to a melting out process to produce gelatin or glue.
12. A process as claimed in claim 1 wherein the treated collagen-containing material is subsequently used to produce a shaped article.
13. A process as claimed in claim 12 wherein the shaped article is in the form of a film.
14. A process as claimed in any of claims 1 to 3 wherein the treated collagen-containing material is subsequently spun to produce a thread.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DEP2813075.8 | 1978-03-25 | ||
| DE19782813075 DE2813075A1 (en) | 1978-03-25 | 1978-03-25 | PROCESSING PROCESS OF RAW MATERIAL CONTAINING COLLAGEN |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1122550A true CA1122550A (en) | 1982-04-27 |
Family
ID=6035423
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA324,147A Expired CA1122550A (en) | 1978-03-25 | 1979-03-26 | Process for the treatment of collagen-containing materials |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US4220724A (en) |
| JP (1) | JPS54163895A (en) |
| AR (1) | AR222988A1 (en) |
| BR (1) | BR7901801A (en) |
| CA (1) | CA1122550A (en) |
| DE (1) | DE2813075A1 (en) |
| ES (1) | ES477038A1 (en) |
| FR (1) | FR2420551A1 (en) |
| GB (1) | GB2023613B (en) |
| IT (1) | IT7967411A0 (en) |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2943520C2 (en) * | 1979-10-27 | 1982-05-19 | Fa. Carl Freudenberg, 6940 Weinheim | Process for the production of collagen sponge for medical or cosmetic purposes |
| DE2944461A1 (en) * | 1979-11-03 | 1981-05-14 | Röhm GmbH, 6100 Darmstadt | METHOD FOR SOFTENING SKINS AND SKIN |
| SE426902B (en) * | 1980-05-23 | 1983-02-21 | Einar Sjolander | SINGLE WRAP AND SET FOR ITS PREPARATION |
| US4908220A (en) * | 1988-03-31 | 1990-03-13 | North Carolina State University | Feather-lysate, a hydrolyzed feather feed ingredient and animal feeds containing the same |
| US4959311A (en) * | 1988-03-31 | 1990-09-25 | North Carolina State University | Method of degrading keratinaceous material and bacteria useful therefore |
| SE467739B (en) * | 1991-04-05 | 1992-09-07 | Collagen Casing Einar Sjoeland | PROCEDURE FOR PREPARING THE COLLAGEN AND COLLAGEN MADE BY THE PROCEDURE AND APPLICATION OF THE COLLAGEN |
| US5374539A (en) * | 1991-06-17 | 1994-12-20 | Nimni; Marcel E. | Process for purifying collagen and generating bioprosthesis |
| DK87692D0 (en) * | 1992-07-03 | 1992-07-03 | Novo Nordisk As | |
| US5316942A (en) * | 1993-06-16 | 1994-05-31 | Battelle Memorial Institute | Process for the production of low-cost soluble high-molecular weight collagen |
| US5736010A (en) * | 1993-06-16 | 1998-04-07 | Ranpak Corporation | Paper strengthened with solubilized collagen and method |
| US5711853A (en) * | 1993-06-16 | 1998-01-27 | Ranpak Corp. | Paper strengthened with solubilized collagen and method |
| US5700354A (en) * | 1993-06-16 | 1997-12-23 | Ranpak Corp. | Paper strengthened with solubilized collagen and method |
| RU2084468C1 (en) * | 1995-02-17 | 1997-07-20 | Межотраслевой научно-технический комплекс "Микрохирургия глаза" | Method of preparing the biocompatible polymeric material |
| US6165490A (en) * | 1996-04-05 | 2000-12-26 | Staar Surgical Ag | Biological material, method of preparing such materials, uses thereof and products made therefrom |
| RU2089198C1 (en) * | 1995-11-30 | 1997-09-10 | Межотраслевой научно-технический комплекс "Микрохирургия глаза" | Method of preparing biomaterial for using in ophthalmology |
| US5766245A (en) * | 1996-12-30 | 1998-06-16 | Staar Surgical, Ag | Intraocular lens for correcting moderate to severe hypermetropia |
| US6100381A (en) * | 1998-11-03 | 2000-08-08 | Eastman Kodak Company | Enzyme method of manufacturing gelatin |
| US6037451A (en) * | 1998-11-03 | 2000-03-14 | Eastman Kodak Company | Method of degreasing bone for gelatin manufacture |
| US20030115686A1 (en) * | 2001-12-22 | 2003-06-26 | Gary Grey | Hair relaxer or straightener without lye or drying effect |
| TWI263678B (en) * | 2004-10-27 | 2006-10-11 | Fisheries Res Inst Council Of | Collagen of fish scale and method of making thereof |
| CN105010737A (en) * | 2015-07-27 | 2015-11-04 | 徐州鸿丰高分子材料有限公司 | Method for preparing meat powder based on removed meat and waste residues of alkali tanning skins |
| WO2020207370A1 (en) * | 2019-04-08 | 2020-10-15 | Novozymes A/S | Method for extracting gelatin |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2741575A (en) * | 1951-08-23 | 1956-04-10 | Armour & Co | Hide glue manufacture |
| US2741576A (en) * | 1954-12-15 | 1956-04-10 | Armour & Co | Method of preparing animal glue |
| FR2283226A1 (en) * | 1974-07-30 | 1976-03-26 | Opi | HAIR RECOVERY PROCESS BY SOLUTION OF THE SKIN |
| GB1557005A (en) * | 1975-07-11 | 1979-12-05 | Novo Industri As | Gelatine extraction |
| CH610346A5 (en) * | 1975-12-01 | 1979-04-12 | Michel Hooreman | Process for obtaining gelatin |
| DE2643012C2 (en) * | 1976-09-24 | 1982-05-19 | Röhm GmbH, 6100 Darmstadt | Process for dissolving machine glue, skin flaps, shavings and the like |
-
1978
- 1978-03-25 DE DE19782813075 patent/DE2813075A1/en active Granted
-
1979
- 1979-01-22 ES ES477038A patent/ES477038A1/en not_active Expired
- 1979-02-14 AR AR275499A patent/AR222988A1/en active
- 1979-02-22 FR FR7904514A patent/FR2420551A1/en active Granted
- 1979-02-23 IT IT7967411A patent/IT7967411A0/en unknown
- 1979-03-13 US US06/020,085 patent/US4220724A/en not_active Expired - Lifetime
- 1979-03-22 JP JP3240479A patent/JPS54163895A/en active Pending
- 1979-03-23 BR BR7901801A patent/BR7901801A/en unknown
- 1979-03-26 GB GB7910511A patent/GB2023613B/en not_active Expired
- 1979-03-26 CA CA324,147A patent/CA1122550A/en not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| BR7901801A (en) | 1979-11-20 |
| IT7967411A0 (en) | 1979-02-23 |
| AR222988A1 (en) | 1981-07-15 |
| FR2420551B1 (en) | 1984-02-24 |
| DE2813075A1 (en) | 1979-10-11 |
| US4220724A (en) | 1980-09-02 |
| ES477038A1 (en) | 1979-12-16 |
| GB2023613B (en) | 1982-08-25 |
| GB2023613A (en) | 1980-01-03 |
| DE2813075C2 (en) | 1989-10-05 |
| JPS54163895A (en) | 1979-12-26 |
| FR2420551A1 (en) | 1979-10-19 |
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