US3110549A - Method of preparing formed collagen - Google Patents
Method of preparing formed collagen Download PDFInfo
- Publication number
- US3110549A US3110549A US112213A US11221361A US3110549A US 3110549 A US3110549 A US 3110549A US 112213 A US112213 A US 112213A US 11221361 A US11221361 A US 11221361A US 3110549 A US3110549 A US 3110549A
- Authority
- US
- United States
- Prior art keywords
- collagen
- pulp
- heating
- fibers
- sheets
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 102000008186 Collagen Human genes 0.000 title claims description 78
- 108010035532 Collagen Proteins 0.000 title claims description 78
- 229920001436 collagen Polymers 0.000 title claims description 78
- 238000000034 method Methods 0.000 title description 22
- 238000010438 heat treatment Methods 0.000 claims description 33
- 239000000835 fiber Substances 0.000 claims description 29
- 230000007935 neutral effect Effects 0.000 claims description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 239000007787 solid Substances 0.000 description 6
- 238000002156 mixing Methods 0.000 description 5
- 235000011837 pasties Nutrition 0.000 description 5
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 4
- 239000007858 starting material Substances 0.000 description 4
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 3
- 235000011130 ammonium sulphate Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000001125 extrusion Methods 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 239000010985 leather Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 229910052684 Cerium Inorganic materials 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- WGLPBDUCMAPZCE-UHFFFAOYSA-N Trioxochromium Chemical compound O=[Cr](=O)=O WGLPBDUCMAPZCE-UHFFFAOYSA-N 0.000 description 1
- 238000010009 beating Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- GWXLDORMOJMVQZ-UHFFFAOYSA-N cerium Chemical compound [Ce] GWXLDORMOJMVQZ-UHFFFAOYSA-N 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000005096 rolling process Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 238000003828 vacuum filtration Methods 0.000 description 1
Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B60—VEHICLES IN GENERAL
- B60R—VEHICLES, VEHICLE FITTINGS, OR VEHICLE PARTS, NOT OTHERWISE PROVIDED FOR
- B60R1/00—Optical viewing arrangements; Real-time viewing arrangements for drivers or passengers using optical image capturing systems, e.g. cameras or video systems specially adapted for use in or on vehicles
- B60R1/12—Mirror assemblies combined with other articles, e.g. clocks
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
- C08L89/00—Compositions of proteins; Compositions of derivatives thereof
- C08L89/04—Products derived from waste materials, e.g. horn, hoof or hair
- C08L89/06—Products derived from waste materials, e.g. horn, hoof or hair derived from leather or skin, e.g. gelatin
-
- D—TEXTILES; PAPER
- D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
- D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
- D01F4/00—Monocomponent artificial filaments or the like of proteins; Manufacture thereof
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01K—MEASURING TEMPERATURE; MEASURING QUANTITY OF HEAT; THERMALLY-SENSITIVE ELEMENTS NOT OTHERWISE PROVIDED FOR
- G01K1/00—Details of thermometers not specially adapted for particular types of thermometer
- G01K1/14—Supports; Fastening devices; Arrangements for mounting thermometers in particular locations
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B60—VEHICLES IN GENERAL
- B60R—VEHICLES, VEHICLE FITTINGS, OR VEHICLE PARTS, NOT OTHERWISE PROVIDED FOR
- B60R1/00—Optical viewing arrangements; Real-time viewing arrangements for drivers or passengers using optical image capturing systems, e.g. cameras or video systems specially adapted for use in or on vehicles
- B60R1/12—Mirror assemblies combined with other articles, e.g. clocks
- B60R2001/123—Mirror assemblies combined with other articles, e.g. clocks with thermometers
Definitions
- native collagen which has been reduced by mechanical means to the form of discrete fibers. This can be accomplished in various wa s.
- the native collagen can be subjected to a preliminary treatment in a paper beating machine in much the same way as cellulose is treated to form a fibrous pulp. If desired,'the beaten collagen can be dewatered, and store-d prior to use in the present process. It will be understood that in preparing collagen fibers from animal hides, such as cattle hides, that the grain layer and the flesh layer are preferably separated from the coriurn, which is the collagen-containing layer.
- an aqueous pulp of collagen fibers is heated at a substantially neutral pH.
- the pulp should be in the form of a soft pasty mass.
- discrete fibers of native collagen are mixed with sufiicient water to form a doughy pulp containing from 10 to 25% solids by weight. Since the pulp is to be heated at a substantially neutral pH, there will normally be no need to add any acidic or basic reagents to the pulp.
- the doughy, substantially neutral pulp of fibrous collagen is heated at a temperature within the. range from 40 to 65 C. It is desirable to control the heating step to solubilize a portion of the collagen without appreciably shrinking the collagen fibers.
- the collagen in the fibers begins to melt and to be extracted into the solution as gelatin rather than as reconstituta-ble collagen.
- temperatures above 62 C. this undesirable conversion may occur to some extent, and at temperatures above 65 C., it is almost certain to occur to an objectionably large extent;
- the temperature of the heating is too low, the desired con version to reconstitutable collagen proceeds too slowly.
- the optimum temperature of heating is within the range from 54 to 62 C. At temper occurring within this range there is little fiber shrinkage and formation of gelatin. At the same time, however, the conversion of a portion of the fibrous collagen to solubilized but reconstitutable collagen is facilitated.
- the pulp will contain 12 to 18% solids and will be at a pH of approximately 6.0. This pulp is then heated at a temperature of 55 to 60 C. until 10 to 12% of the collagen has been solubilized.
- the desired solubilization can usually be obtained in approximately one hour. It will be understood, of course, can be varied considerably, and that the time lWlll usually vary inversely with thetemperature.
- the pulp can be observed to see whether the shrinkage of the fibers is being avoided, and samples can be taken and subjected to vacuum filtration to measure the percent of collagen which has been solubilized.
- the solubilized collagen willpass through the filter, which upon being separated from the water by drying, can be compared on a weight basis with the dried insolubleresidue.
- the doughy pulp is formed into the desired shape.
- the pulp may be extruded to form sheets or filaments.
- the dough is forced under pressure through a die.
- the die will provide a horizontally extending slit corresponding to the desired width of the sheet. provide one or more orifices to the diameter of the filaments.
- the dough can fall upon a moving conveyor belt which is timed to permit the continuity of the sheets or filaments to be maintained.
- uniform sheets or films of any desired thickness maybe produced. The thickness will usually correspond to that of natural leather.
- the diameters of the filaments can also be varied as desired. For some purposes, it may be advantageous to form the collagen. dough in a mold to produce solid or hollow bodies,
- the forming or extrusion step is preferably carried out while the pulp is still atan elevated temperature.
- temperatures of to are suitable, and parcorresponding in diameter ticularly good results are obtained at a temperature of around 50 C.
- the temperature is not particularlycritical providing the dough is sufficiently fluid to permit it to be satisfactorily formed by extrusion or other forming procedure.
- the sheets may be fixed In this step, the
- temperature of the sheets should usually be reduced below 20 C. More specifically, temperatures in the range of 2 to 10 C. are suitable.
- the chilling may be accomplished in various ways, such as by passing the sheets over chilled rollers.
- the ammonium sulfate solution may be injected into the formed collagen at spaced This procedure is believed to increase the strength of the formed collagen by encouraging the precipitation of the solubilized collagen.
- the sheets or filaments may also be subjected to other procedures which are well-known in the processing of leather.
- the sheets may be tanned with various standard tanning solutions, such as an aqueous solution containing 1% chromic oxide and 2% sodium formats.
- the starting material was native collagen fibers Whi had been prepared from the corium layer of fresh unlimed cattle skins by mechanically subdividing the coriuin into discrete fibers by means of a paper beater.
- the cerium was treated in an aqueous slurry in the beater, and the resulting fiberswere subsequently dewatered and dried to provide the starting material.
- the doughy pulp was formed into a sheet by a hand rolling procedure.
- the sheet was cold set at 4 C. for ten minutes, and then immersed in a bath of half saturated ammonium sulfate (plldil). After one hour the sheet was examined and found to be exceedingly strong.
- the sheet was then tanned according to standard procedures, using a chrome tanning reagent.
- a method of preparing formed collagen comprising mixing discrete fibers of native collagen with water to form a doughy pulp, said pulp having a substantially neutral pH, heating said pulp at a temperature within the range from 40 to 65 C. to solubilize a portion of the collagen therein without appreciably shrinking said fibers, continuing said heating until at least 5% by weight of the collagen in said pulp has been solubilized while the major portion of the said collagenremains infibrillar form, and thereatter forming said pulp.
- a method of preparing formed collagen comprising mixing discrete fibers of native collagen with water to form a doughy pulp, said pulp having'a pH above 5.0 but below 8.0 and containing from to solids by Weight, heating said pulp at a temperature within the range from to 65 C. to solubilize a portion of the collagen therein without appreciably shrinking said fibers, continuing said heating until from 8 to 30% by l weight of the collagen in said pulp has been solubilized, and thereafter forming said pulp.
- said pulp having a pH above 5.0 but below 8.0 and being in the form of a soft pasty mass
- said heating step being controlled to transform from 8 to 30% by weight of the fibrous collagen in said pulp to solubilized collagen without appreciable shrinkage of the collagen fibers, termi- 'd heating step while the major portion of said collagen remains in fibrous form, extruding the heated pulp to a predetermined form, and chilling the formed collagen.
- aqueous pulp of collagen fibers said pulp having a pH of from 5.0 to 7.0 and being in the form of a soft pasty mass, said heating step being controlled to transform from 8 to 15% by Wei ht of the fibrous collagen in said pulp to solubilized collagen without appreciable shrinkage of the collagen fibers, extruding the heated pulp to form sheets, and chilling said sheets.
- a method of preparing collagen sheets comprising heating an aqueous pulp of collagen fibers, said pulp having a pH of from 5.5 to 7.0 and being in the form of a soft pasty mass, said heating'step being controlled to transform at least 8 to 15% by weight of the fibrous collagen in said pulp to solubilized collagen without appreciable shrinkage of the collagen fibers, said heating being carried out at a temperature of substantially from '54 to 62 C. and being terminated While the major portion of said collagen remains in fibrous form, extruding the heated pulp to form sheets, and chilling said sheets.
Landscapes
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Polymers & Plastics (AREA)
- Physics & Mathematics (AREA)
- Materials Engineering (AREA)
- Biochemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Physics & Mathematics (AREA)
- General Chemical & Material Sciences (AREA)
- Textile Engineering (AREA)
- Dermatology (AREA)
- Multimedia (AREA)
- Mechanical Engineering (AREA)
- Paper (AREA)
- Laminated Bodies (AREA)
- Treatment And Processing Of Natural Fur Or Leather (AREA)
Priority Applications (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US112213A US3110549A (en) | 1961-05-24 | 1961-05-24 | Method of preparing formed collagen |
| FR7411A FR1322010A (fr) | 1961-05-24 | 1962-05-16 | Procédé pour la préparation de collagène mis en forme |
| ES277559A ES277559A1 (es) | 1961-05-24 | 1962-05-22 | Método de preparación de colágeno configurado |
| GB19899/62A GB949424A (en) | 1961-05-24 | 1962-05-23 | Improved method of preparing formed collagen |
| AT423362A AT248599B (de) | 1961-05-24 | 1962-05-23 | Verfahren zur Herstellung von Faserkunstleder |
| BE617977A BE617977A (fr) | 1961-05-24 | 1962-05-23 | Procédé de préparation de collagène moulé |
| NL278815D NL278815A (fr) | 1961-05-24 | 1962-05-24 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US112213A US3110549A (en) | 1961-05-24 | 1961-05-24 | Method of preparing formed collagen |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| US3110549A true US3110549A (en) | 1963-11-12 |
Family
ID=22342691
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| US112213A Expired - Lifetime US3110549A (en) | 1961-05-24 | 1961-05-24 | Method of preparing formed collagen |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US3110549A (fr) |
| AT (1) | AT248599B (fr) |
| BE (1) | BE617977A (fr) |
| ES (1) | ES277559A1 (fr) |
| FR (1) | FR1322010A (fr) |
| GB (1) | GB949424A (fr) |
| NL (1) | NL278815A (fr) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4014971A (en) * | 1973-05-11 | 1977-03-29 | Perkins Rodney C | Method for making a tympanic membrane prosthesis |
| KR20180082478A (ko) * | 2015-11-10 | 2018-07-18 | 메드스킨 솔루션즈 닥터. 수버랙 아게 | 타겟화된 구조 디자인의 생체 적합성 매트릭스 제조 방법 |
| EP3583255B1 (fr) * | 2017-02-15 | 2023-08-23 | Ecco Sko A/S | Procédé et appareil permettant de fabriquer une fibre coupée à base de fibre de protéine naturelle et une laine brute à base de fibre coupée. |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US1656681A (en) * | 1925-08-07 | 1928-01-17 | Samuel Jacob | Method of manufacturing artificial sausage skins |
| US2631942A (en) * | 1951-05-01 | 1953-03-17 | United Shoe Machinery Corp | Methods of forming fibers from collagen |
| US2838363A (en) * | 1954-10-19 | 1958-06-10 | Armour & Co | Method of preparing filaments and sheets from procollagen |
| US2927345A (en) * | 1955-06-13 | 1960-03-08 | American Cyanamid Co | Apparatus for casting gelatin upon a cooled drum including drum warp compensating means |
| US3034852A (en) * | 1960-01-26 | 1962-05-15 | Japan Leather Mfg Co Ltd | Solubilization of insoluble collagen fibers and reconstitution thereof |
-
1961
- 1961-05-24 US US112213A patent/US3110549A/en not_active Expired - Lifetime
-
1962
- 1962-05-16 FR FR7411A patent/FR1322010A/fr not_active Expired
- 1962-05-22 ES ES277559A patent/ES277559A1/es not_active Expired
- 1962-05-23 AT AT423362A patent/AT248599B/de active
- 1962-05-23 BE BE617977A patent/BE617977A/fr unknown
- 1962-05-23 GB GB19899/62A patent/GB949424A/en not_active Expired
- 1962-05-24 NL NL278815D patent/NL278815A/xx unknown
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US1656681A (en) * | 1925-08-07 | 1928-01-17 | Samuel Jacob | Method of manufacturing artificial sausage skins |
| US2631942A (en) * | 1951-05-01 | 1953-03-17 | United Shoe Machinery Corp | Methods of forming fibers from collagen |
| US2838363A (en) * | 1954-10-19 | 1958-06-10 | Armour & Co | Method of preparing filaments and sheets from procollagen |
| US2927345A (en) * | 1955-06-13 | 1960-03-08 | American Cyanamid Co | Apparatus for casting gelatin upon a cooled drum including drum warp compensating means |
| US3034852A (en) * | 1960-01-26 | 1962-05-15 | Japan Leather Mfg Co Ltd | Solubilization of insoluble collagen fibers and reconstitution thereof |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4014971A (en) * | 1973-05-11 | 1977-03-29 | Perkins Rodney C | Method for making a tympanic membrane prosthesis |
| KR20180082478A (ko) * | 2015-11-10 | 2018-07-18 | 메드스킨 솔루션즈 닥터. 수버랙 아게 | 타겟화된 구조 디자인의 생체 적합성 매트릭스 제조 방법 |
| CN108367101A (zh) * | 2015-11-10 | 2018-08-03 | 医疗美容解决方案祖韦拉克医生公司 | 用于生产具有靶向结构设计的生物相容性基质的方法 |
| US20180326116A1 (en) * | 2015-11-10 | 2018-11-15 | Medskin Solutions Dr. Suwelack Ag | Method for producing a biocompatible matrix with targeted structural design |
| US11369715B2 (en) * | 2015-11-10 | 2022-06-28 | Medskin Solutions Dr. Suwelack Ag | Method for producing a biocompatible matrix with targeted structural design |
| EP3583255B1 (fr) * | 2017-02-15 | 2023-08-23 | Ecco Sko A/S | Procédé et appareil permettant de fabriquer une fibre coupée à base de fibre de protéine naturelle et une laine brute à base de fibre coupée. |
| EP3583256B1 (fr) * | 2017-02-15 | 2023-11-01 | Ecco Sko A/S | Filament et fils produits sur la base d'une protéine naturelle |
Also Published As
| Publication number | Publication date |
|---|---|
| GB949424A (en) | 1964-02-12 |
| AT248599B (de) | 1966-08-10 |
| ES277559A1 (es) | 1962-10-16 |
| NL278815A (fr) | 1964-11-10 |
| FR1322010A (fr) | 1963-03-22 |
| BE617977A (fr) | 1962-09-17 |
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